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Conserved domains on  [gi|21312260|ref|NP_082546|]
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aldehyde dehydrogenase X, mitochondrial precursor [Mus musculus]

Protein Classification

aldehyde dehydrogenase family protein( domain architecture ID 10163008)

aldehyde dehydrogenase family protein similar to human retinal dehydrogenase 1 that catalyzes the oxidation of retinaldehyde to retinoic acid

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
33-513 0e+00

NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.


:

Pssm-ID: 143459  Cd Length: 481  Bit Score: 1023.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  33 NPEICYNKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGSPWRRMDASERGRLLNRLAD 112
Cdd:cd07141   1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 113 LVERDRVYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLV 192
Cdd:cd07141  81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 193 MQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLI 272
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 273 QKAAGESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGN 352
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 353 PFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKI 432
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 433 EEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480

                .
gi 21312260 513 K 513
Cdd:cd07141 481 K 481
 
Name Accession Description Interval E-value
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
33-513 0e+00

NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.


Pssm-ID: 143459  Cd Length: 481  Bit Score: 1023.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  33 NPEICYNKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGSPWRRMDASERGRLLNRLAD 112
Cdd:cd07141   1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 113 LVERDRVYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLV 192
Cdd:cd07141  81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 193 MQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLI 272
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 273 QKAAGESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGN 352
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 353 PFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKI 432
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 433 EEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480

                .
gi 21312260 513 K 513
Cdd:cd07141 481 K 481
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
22-518 0e+00

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 731.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   22 STAAALPNPI-PNPEICYNKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGsPWRRMDA 100
Cdd:PLN02466  40 TAAAAVEEPItPPVQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTA 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  101 SERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGV 180
Cdd:PLN02466 119 YERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGV 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  181 CGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKV 260
Cdd:PLN02466 199 AGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKL 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  261 AFTGSTEVGHLIQKAAGESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLER 340
Cdd:PLN02466 279 AFTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK 358
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  341 TVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIF 420
Cdd:PLN02466 359 AKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIF 438
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  421 GPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDG 500
Cdd:PLN02466 439 GPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYS 518
                        490
                 ....*....|....*...
gi 21312260  501 LRAYTEVKTVTikVPEKN 518
Cdd:PLN02466 519 LNNYLQVKAVV--TPLKN 534
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
47-510 0e+00

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 673.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260    47 WHDAVSKkTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLET 126
Cdd:pfam00171   1 WVDSESE-TIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   127 LDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGN 206
Cdd:pfam00171  77 LENGKPLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   207 TVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTL 286
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   287 ELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDK 366
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   367 EQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGL 446
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21312260   447 AAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVT-CHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDaDGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and ...
39-517 0e+00

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and conversion];


Pssm-ID: 223944 [Multi-domain]  Cd Length: 472  Bit Score: 595.43  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  39 NKLFINNEWHDAVSkkTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDR 118
Cdd:COG1012   1 YKLLIDGEWVDGAS--TIEVINPATGEVIATVPAATAEDVDAAVAAARAAFE---AWSRLSAEERAAILRRIADLLEARA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 119 VYLASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKL 198
Cdd:COG1012  76 EELAALITLETGKPISEARG-EIARAADFIRYYAEEARRLEGETIPTDKGSKALVRREPLGVVGAITPWNFPLALAAWKL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 199 APALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGE 278
Cdd:COG1012 155 APALAAGNTVVLKPSEQTPLSALALAELAAEAGLPAGVLNVVTGGGAEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAA 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 279 sNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDT 358
Cdd:COG1012 235 -NLKPVTLELGGKSPAIVLEDADLDAAVDAAVFGAFFNAGQRCTAASRLIVHESVYDEFVERLVARAASLKVGDPLDPST 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 359 QQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGerGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQR 438
Cdd:COG1012 314 DLGPLISEEQLDRVEGYIEDAVAEGARLLAGGKRPG--GYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIEL 391
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 439 ANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNI--VTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIKVPE 516
Cdd:COG1012 392 ANDTEYGLAAAIFTRDLARAFRVARRLEAGMVGINDYTGgaDIAYLPFGGVKQSGLGREGGKYGLEEFTEVKTVTIKLGP 471

                .
gi 21312260 517 K 517
Cdd:COG1012 472 A 472
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
42-508 0e+00

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131 [Multi-domain]  Cd Length: 467  Bit Score: 518.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260    42 FINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:TIGR01804   1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQG---EWAAMSPMERGRILRRAADLIRERNEEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   122 ASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPA 201
Cdd:TIGR01804  78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   202 LATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNL 281
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAG-HL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   282 KRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQG 361
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   362 PQVDKEQFERILGYIRLGQKEGAKLLCGGERLG----ERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQ 437
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPEnvglQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21312260   438 RANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVK 508
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
 
Name Accession Description Interval E-value
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
33-513 0e+00

NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.


Pssm-ID: 143459  Cd Length: 481  Bit Score: 1023.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  33 NPEICYNKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGSPWRRMDASERGRLLNRLAD 112
Cdd:cd07141   1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 113 LVERDRVYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLV 192
Cdd:cd07141  81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 193 MQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLI 272
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 273 QKAAGESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGN 352
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 353 PFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKI 432
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 433 EEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480

                .
gi 21312260 513 K 513
Cdd:cd07141 481 K 481
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
39-512 0e+00

ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.


Pssm-ID: 143410  Cd Length: 476  Bit Score: 887.32  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  39 NKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGSpWRRMDASERGRLLNRLADLVERDR 118
Cdd:cd07091   4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIERDR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 119 VYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKL 198
Cdd:cd07091  83 DELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 199 APALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGE 278
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 279 SNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDT 358
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 359 QQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQR 438
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21312260 439 ANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07091 403 ANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
38-510 0e+00

Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.


Pssm-ID: 143460  Cd Length: 476  Bit Score: 741.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  38 YNKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGsPWRRMDASERGRLLNRLADLVERD 117
Cdd:cd07142   3 HTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLEKH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 118 RVYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWK 197
Cdd:cd07142  82 ADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 198 LAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAG 277
Cdd:cd07142 162 VGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 278 ESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELD 357
Cdd:cd07142 242 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKG 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 358 TQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQ 437
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21312260 438 RANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
22-518 0e+00

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 731.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   22 STAAALPNPI-PNPEICYNKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGsPWRRMDA 100
Cdd:PLN02466  40 TAAAAVEEPItPPVQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTA 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  101 SERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGV 180
Cdd:PLN02466 119 YERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGV 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  181 CGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKV 260
Cdd:PLN02466 199 AGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKL 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  261 AFTGSTEVGHLIQKAAGESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLER 340
Cdd:PLN02466 279 AFTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK 358
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  341 TVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIF 420
Cdd:PLN02466 359 AKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIF 438
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  421 GPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDG 500
Cdd:PLN02466 439 GPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYS 518
                        490
                 ....*....|....*...
gi 21312260  501 LRAYTEVKTVTikVPEKN 518
Cdd:PLN02466 519 LNNYLQVKAVV--TPLKN 534
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
40-512 0e+00

Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.


Pssm-ID: 143462  Cd Length: 484  Bit Score: 693.38  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  40 KLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgSPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:cd07144   9 GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNRD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 120 YLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLA 199
Cdd:cd07144  87 LLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 200 PALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGeS 279
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA-Q 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 280 NLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQR-KVGNPFELDT 358
Cdd:cd07144 246 NLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDT 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 359 QQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGE---RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEV 435
Cdd:cd07144 326 VVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEA 405
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21312260 436 IQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07144 406 IKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
41-514 0e+00

Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.


Pssm-ID: 143461  Cd Length: 481  Bit Score: 685.80  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  41 LFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgSPWRR-MDASERGRLLNRLADLVERDRV 119
Cdd:cd07143   9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWGLkVSGSKRGRCLSKLADLMERNLD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 120 YLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLA 199
Cdd:cd07143  87 YLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 200 PALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGES 279
Cdd:cd07143 167 PALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 280 NLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQ 359
Cdd:cd07143 247 NLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTF 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 360 QGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRA 439
Cdd:cd07143 327 QGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRA 406
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21312260 440 NNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIKV 514
Cdd:cd07143 407 NDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
47-510 0e+00

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 673.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260    47 WHDAVSKkTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLET 126
Cdd:pfam00171   1 WVDSESE-TIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   127 LDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGN 206
Cdd:pfam00171  77 LENGKPLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   207 TVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTL 286
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   287 ELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDK 366
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   367 EQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGL 446
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21312260   447 AAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVT-CHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDaDGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
34-515 0e+00

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 653.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   34 PEICYNKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGsPWRRMDASERGRLLNRLADL 113
Cdd:PLN02766  16 PEIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  114 VERDRVYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVM 193
Cdd:PLN02766  95 IEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTM 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  194 QGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQ 273
Cdd:PLN02766 175 FFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIM 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  274 KAAGESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNP 353
Cdd:PLN02766 255 QAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDP 334
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  354 FELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIE 433
Cdd:PLN02766 335 FDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVE 414
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  434 EVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIK 513
Cdd:PLN02766 415 EAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTP 494

                 ..
gi 21312260  514 VP 515
Cdd:PLN02766 495 LY 496
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
42-512 0e+00

Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.


Pssm-ID: 143437  Cd Length: 482  Bit Score: 624.72  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  42 FINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlGSPWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:cd07119   1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFD-SGEWPHLPAQERAALLFRIADKIREDAEEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 122 ASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPA 201
Cdd:cd07119  80 ARLETLNTGKTLRESEI-DIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 202 LATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNL 281
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NV 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 282 KRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQG 361
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 362 PQVDKEQFERILGYIRLGQKEGAKLLCGGERLGE----RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQ 437
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21312260 438 RANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
79-512 0e+00

NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.


Pssm-ID: 143397 [Multi-domain]  Cd Length: 432  Bit Score: 616.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  79 DLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKW 158
Cdd:cd07078   1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 159 HGKTIP-MDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVV 237
Cdd:cd07078  77 HGEVIPsPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 238 NIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNM 317
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 318 GQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL-GER 396
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLeGGK 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 397 GFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYN 476
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 21312260 477 IVTC-HTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07078 396 VGAEpSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
54-512 0e+00

Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.


Pssm-ID: 143430 [Multi-domain]  Cd Length: 462  Bit Score: 613.84  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  54 KTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGSpWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPF 133
Cdd:cd07112   2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 134 QESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVA 213
Cdd:cd07112  81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 214 EQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGESNLKRVTLELGGKSP 293
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 294 SIVLADA-DMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERI 372
Cdd:cd07112 241 NIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 373 LGYIRLGQKEGAKLLCGGERLGE--RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAV 450
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRVLTetGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21312260 451 FTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
58-512 0e+00

Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.


Pssm-ID: 143432 [Multi-domain]  Cd Length: 457  Bit Score: 611.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlGSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESy 137
Cdd:cd07114   1 SINPATGEPWARVPEASAADVDRAVAAARAAFE-GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRET- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 138 VLDLDEVIKVYRYFAGWADKWHGKTIPMD-GEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQT 216
Cdd:cd07114  79 RAQVRYLAEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 217 PLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIV 296
Cdd:cd07114 159 PASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIV 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 297 LADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYI 376
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYV 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 377 RLGQKEGAKLLCGGERLGE----RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFT 452
Cdd:cd07114 318 ARAREEGARVLTGGERPSGadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 453 RDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07114 398 RDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and ...
39-517 0e+00

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and conversion];


Pssm-ID: 223944 [Multi-domain]  Cd Length: 472  Bit Score: 595.43  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  39 NKLFINNEWHDAVSkkTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDR 118
Cdd:COG1012   1 YKLLIDGEWVDGAS--TIEVINPATGEVIATVPAATAEDVDAAVAAARAAFE---AWSRLSAEERAAILRRIADLLEARA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 119 VYLASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKL 198
Cdd:COG1012  76 EELAALITLETGKPISEARG-EIARAADFIRYYAEEARRLEGETIPTDKGSKALVRREPLGVVGAITPWNFPLALAAWKL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 199 APALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGE 278
Cdd:COG1012 155 APALAAGNTVVLKPSEQTPLSALALAELAAEAGLPAGVLNVVTGGGAEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAA 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 279 sNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDT 358
Cdd:COG1012 235 -NLKPVTLELGGKSPAIVLEDADLDAAVDAAVFGAFFNAGQRCTAASRLIVHESVYDEFVERLVARAASLKVGDPLDPST 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 359 QQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGerGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQR 438
Cdd:COG1012 314 DLGPLISEEQLDRVEGYIEDAVAEGARLLAGGKRPG--GYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIEL 391
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 439 ANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNI--VTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIKVPE 516
Cdd:COG1012 392 ANDTEYGLAAAIFTRDLARAFRVARRLEAGMVGINDYTGgaDIAYLPFGGVKQSGLGREGGKYGLEEFTEVKTVTIKLGP 471

                .
gi 21312260 517 K 517
Cdd:COG1012 472 A 472
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
58-514 0e+00

Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.


Pssm-ID: 143433 [Multi-domain]  Cd Length: 453  Bit Score: 592.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:cd07115   1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 138 VLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTP 217
Cdd:cd07115  78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 218 LSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGeSNLKRVTLELGGKSPSIVL 297
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVF 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 298 ADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIR 377
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 378 LGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDK 457
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21312260 458 AIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIKV 514
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
58-512 0e+00

Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.


Pssm-ID: 143412 [Multi-domain]  Cd Length: 455  Bit Score: 577.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:cd07093   1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP---GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 138 VLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTP 217
Cdd:cd07093  78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 218 LSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVL 297
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 298 ADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIR 377
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 378 LGQKEGAKLLCGGERLG----ERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTR 453
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21312260 454 DLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
40-512 0e+00

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.


Pssm-ID: 143471 [Multi-domain]  Cd Length: 480  Bit Score: 570.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  40 KLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:cd07559   2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 120 YLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLA 199
Cdd:cd07559  79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 200 PALATGNTVVMKVAEQTPLSALYLASLIKEAgFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEs 279
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 280 NLKRVTLELGGKSPSIVLADA-----DMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPF 354
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 355 ELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGE----RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFK 430
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLggldKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 431 KIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476

                ..
gi 21312260 511 TI 512
Cdd:cd07559 477 LV 478
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
39-513 0e+00

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.


Pssm-ID: 143458  Cd Length: 486  Bit Score: 567.89  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  39 NKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlGSPWRRMDASERGRLLNRLADLVERDR 118
Cdd:cd07140   6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFE-NGEWGKMNARDRGRLMYRLADLMEEHQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 119 VYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEH----FCFTRHEPVGVCGQIIPWNFPLVMQ 194
Cdd:cd07140  85 EELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARpnrnLTLTKREPIGVCGIVIPWNYPLMML 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 195 GWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQK 274
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 275 AAGESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPF 354
Cdd:cd07140 245 SCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 355 ELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFK--KI 432
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDdgDV 404
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 433 EEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484

                .
gi 21312260 513 K 513
Cdd:cd07140 485 E 485
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
59-512 0e+00

Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.


Pssm-ID: 143427 [Multi-domain]  Cd Length: 454  Bit Score: 547.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYV 138
Cdd:cd07109   2 FDPSTGEVFARIARGGAADVDRAVQAARRAFE--SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 139 lDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPL 218
Cdd:cd07109  80 -DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 219 SALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLA 298
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 299 DADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGnPFELDTQQGPQVDKEQFERILGYIRL 378
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGFVAR 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 379 GQKEGAKLLCGGERL---GERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDL 455
Cdd:cd07109 317 ARARGARIVAGGRIAegaPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21312260 456 DKAIYFTQALQAGTVWVNTYNIVT-CHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNYGAGGgIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
58-510 0e+00

NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.


Pssm-ID: 143409 [Multi-domain]  Cd Length: 457  Bit Score: 540.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:cd07090   1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 138 VlDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTP 217
Cdd:cd07090  78 V-DIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 218 LSALYLASLIKEAGFPPGVVNIITGYGPTaGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGeSNLKRVTLELGGKSPSIVL 297
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIF 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 298 ADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIR 377
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 378 LGQKEGAKLLCGGERLG-----ERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFT 452
Cdd:cd07090 315 SAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21312260 453 RDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
40-512 0e+00

Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.


Pssm-ID: 143435  Cd Length: 475  Bit Score: 537.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  40 KLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:cd07117   2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 120 YLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLA 199
Cdd:cd07117  79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 200 PALATGNTVVMKVAEQTPLSALYLASLIKEAgFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEs 279
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 280 NLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQ 359
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 360 QGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGE----RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEV 435
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTEngldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21312260 436 IQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
59-512 0e+00

Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.


Pssm-ID: 143421 [Multi-domain]  Cd Length: 451  Bit Score: 534.32  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESyv 138
Cdd:cd07103   2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 139 ldLDEVikVY-----RYFAGWADKWHGKTIP-MDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKV 212
Cdd:cd07103  77 --RGEV--DYaasflEWFAEEARRIYGRTIPsPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 213 AEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVG-HLIQKAAgeSNLKRVTLELGGK 291
Cdd:cd07103 153 AEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGkLLMAQAA--DTVKRVSLELGGN 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 292 SPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFER 371
Cdd:cd07103 231 APFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEK 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 372 ILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVF 451
Cdd:cd07103 311 VEALVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVF 390
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21312260 452 TRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07103 391 TRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
40-510 0e+00

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 532.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   40 KLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLV-ERDR 118
Cdd:PRK13252   8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERND 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  119 VyLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKL 198
Cdd:PRK13252  85 E-LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  199 APALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTaGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGE 278
Cdd:PRK13252 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAA 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  279 SnLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDT 358
Cdd:PRK13252 243 S-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPAT 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  359 QQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGE----RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEE 434
Cdd:PRK13252 322 NFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDE 401
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21312260  435 VIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:PRK13252 402 VIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
58-511 0e+00

Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.


Pssm-ID: 143428 [Multi-domain]  Cd Length: 456  Bit Score: 528.46  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESy 137
Cdd:cd07110   1 VINPATEATIGEIPAATAEDVDAAVRAARRAF---PRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 138 VLDLDEVIKVYRYFAGWA---DKWHGKTIPMDGEHF-CFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVA 213
Cdd:cd07110  77 AWDVDDVAGCFEYYADLAeqlDAKAERAVPLPSEDFkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 214 EQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSP 293
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSP 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 294 SIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERIL 373
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 374 GYIRLGQKEGAKLLCGGER--LGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVF 451
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 452 TRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVT 511
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
41-511 0e+00

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.


Pssm-ID: 143456 [Multi-domain]  Cd Length: 466  Bit Score: 527.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  41 LFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:cd07138   1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP---AWSATSVEERAALLERIAEAYEARADE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 121 LASLETLDNGKP------FQ-ESYVLDLDEVIKVYRYFAgWADKWHGKTIpmdgehfcftRHEPVGVCGQIIPWNFPLVM 193
Cdd:cd07138  78 LAQAITLEMGAPitlaraAQvGLGIGHLRAAADALKDFE-FEERRGNSLV----------VREPIGVCGLITPWNWPLNQ 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 194 QGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQ 273
Cdd:cd07138 147 IVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVA 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 274 KAAGESnLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNP 353
Cdd:cd07138 227 EAAADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDP 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 354 FELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGG----ERLgERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKF 429
Cdd:cd07138 306 RDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpgrpEGL-ERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPY 384
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 430 KKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNtYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKT 509
Cdd:cd07138 385 DDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKS 463

                ..
gi 21312260 510 VT 511
Cdd:cd07138 464 IQ 465
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
42-508 0e+00

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131 [Multi-domain]  Cd Length: 467  Bit Score: 518.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260    42 FINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:TIGR01804   1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQG---EWAAMSPMERGRILRRAADLIRERNEEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   122 ASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPA 201
Cdd:TIGR01804  78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   202 LATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNL 281
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAG-HL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   282 KRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQG 361
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   362 PQVDKEQFERILGYIRLGQKEGAKLLCGGERLG----ERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQ 437
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPEnvglQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21312260   438 RANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVK 508
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
61-512 3.76e-180

Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.


Pssm-ID: 143436 [Multi-domain]  Cd Length: 454  Bit Score: 513.81  E-value: 3.76e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  61 PTTGEVIGHVAEGDRADVDLAVKAAREAFRLGsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVlD 140
Cdd:cd07118   4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-E 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 141 LDEVIKVYRYFAGWADKWHGKTIPMDGEH-FCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLS 219
Cdd:cd07118  82 IEGAADLWRYAASLARTLHGDSYNNLGDDmLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 220 ALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLAD 299
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFAD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 300 ADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLG 379
Cdd:cd07118 241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 380 QKEGAKLLCGGERLGER-GFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKA 458
Cdd:cd07118 321 RAEGATLLLGGERLASAaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 21312260 459 IYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
41-512 5.67e-176

Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.


Pssm-ID: 143457 [Multi-domain]  Cd Length: 471  Bit Score: 503.65  E-value: 5.67e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  41 LFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGsPWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:cd07139   1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 121 LASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADK--WHGKTIPMDGEHfCFTRHEPVGVCGQIIPWNFPLVMQGWKL 198
Cdd:cd07139  80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDfpFEERRPGSGGGH-VLVRREPVGVVAAIVPWNAPLFLAALKI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 199 APALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGE 278
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 279 sNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDT 358
Cdd:cd07139 238 -RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPAT 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 359 QQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLG--ERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVI 436
Cdd:cd07139 317 QIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAglDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAV 396
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21312260 437 QRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNiVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07139 397 RIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFR-LDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
PLN02467 PLN02467
betaine aldehyde dehydrogenase
27-511 9.07e-174

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 499.26  E-value: 9.07e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   27 LPNPIPNpeicyNKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFR--LGSPWRRMDASERG 104
Cdd:PLN02467   1 MAIPVPR-----RQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKrnKGKDWARTTGAVRA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  105 RLLNRLADLVERDRVYLASLETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWHGK-----TIPMDgEHFCFTRHEPVG 179
Cdd:PLN02467  76 KYLRAIAAKITERKSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEALDAKqkapvSLPME-TFKGYVLKEPLG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  180 VCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDK 259
Cdd:PLN02467 154 VVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDK 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  260 VAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLE 339
Cdd:PLN02467 234 IAFTGSTATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLE 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  340 RTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLG--ERGFFIKPTVFGDVQDGMRIAKE 417
Cdd:PLN02467 313 KLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWRE 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  418 EIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELG 497
Cdd:PLN02467 393 EVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELG 472
                        490
                 ....*....|....
gi 21312260  498 EDGLRAYTEVKTVT 511
Cdd:PLN02467 473 EWGLENYLSVKQVT 486
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
42-512 1.49e-171

Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.


Pssm-ID: 143449  Cd Length: 478  Bit Score: 492.63  E-value: 1.49e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  42 FINNEWHDAVSKKTFPTVNPTTG-EVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:cd07131   2 YIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFP---EWRKVPAPRRAEYLFRAAELLKKRKEE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 121 LASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIPMD-GEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLA 199
Cdd:cd07131  79 LARLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 200 PALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGES 279
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 280 NlKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQ 359
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 360 QGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL----GERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEV 435
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLtgggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21312260 436 IQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNI-VTCHTPFGGFKESGNG-RELGEDGLRAYTEVKTVTI 512
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
83-512 8.85e-171

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143395 [Multi-domain]  Cd Length: 367  Bit Score: 486.35  E-value: 8.85e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  83 KAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKT 162
Cdd:cd06534   1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLGGPE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 163 IP-MDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIIT 241
Cdd:cd06534  77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 242 GYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCC 321
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 322 CAGSRTFVEESIYREFLERTVekakqrkvgnpfeldtqqgpqvdkeqferilgyirlgqkegakllcggerlgergffik 401
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 402 pTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTC- 480
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGp 335
                       410       420       430
                ....*....|....*....|....*....|..
gi 21312260 481 HTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
42-510 2.15e-169

Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.


Pssm-ID: 143415  Cd Length: 473  Bit Score: 487.14  E-value: 2.15e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  42 FINNEWHDAVSkkTFPTVNPT-TGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:cd07097   4 YIDGEWVAGGD--GEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 121 LASLETLDNGKPFQESyvldLDEV---IKVYRYFAGWADKWHGKTIP-MDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGW 196
Cdd:cd07097  79 LARLLTREEGKTLPEA----RGEVtraGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAW 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 197 KLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAA 276
Cdd:cd07097 155 KIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAA 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 277 GeSNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFEL 356
Cdd:cd07097 235 A-ARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 357 DTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL--GERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEE 434
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDE 393
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21312260 435 VIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNI-VTCHTPFGGFKESGNG-RELGEDGLRAYTEVKTV 510
Cdd:cd07097 394 ALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
59-512 3.88e-168

Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.


Pssm-ID: 143411 [Multi-domain]  Cd Length: 450  Bit Score: 482.98  E-value: 3.88e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYV 138
Cdd:cd07092   2 VDPATGEEIATVPDASAADVDAAVAAAHAAFP---SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 139 LDLDEVIKVYRYFAGWADKWHGktiPMDGE----HFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAE 214
Cdd:cd07092  79 DELPGAVDNFRFFAGAARTLEG---PAAGEylpgHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 215 QTPLSALYLASLIKEaGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGeSNLKRVTLELGGKSPS 294
Cdd:cd07092 156 TTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAA-DTLKRVHLELGGKAPV 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 295 IVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILG 374
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 375 YIRlGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRD 454
Cdd:cd07092 314 FVE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21312260 455 LDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
59-510 8.58e-168

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.


Pssm-ID: 143408 [Multi-domain]  Cd Length: 459  Bit Score: 482.51  E-value: 8.58e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlGSPWRrMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYV 138
Cdd:cd07089   2 INPATEEVIGTAPDAGAADVDAAIAAARRAFD-TGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 139 LDLDEVIKVYRYFAGWADKWHGKTI-----PMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVA 213
Cdd:cd07089  80 MQVDGPIGHLRYFADLADSFPWEFDlpvpaLRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 214 EQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSP 293
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSA 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 294 SIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERIL 373
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 374 GYIRLGQKEGAKLLCGGERL--GERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVF 451
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPagLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21312260 452 TRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
59-512 8.88e-168

Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.


Pssm-ID: 143424 [Multi-domain]  Cd Length: 446  Bit Score: 481.64  E-value: 8.88e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYv 138
Cdd:cd07106   2 INPATGEVFASAPVASEAQLDQAVAAAKAAF---PGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 139 LDLDEVIKVYRYFAGWADKwhGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPL 218
Cdd:cd07106  78 FEVGGAVAWLRYTASLDLP--DEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 219 SALYLASLIKEAgFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLA 298
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAK-TLKRVTLELGGNDAAIVLP 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 299 DADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRL 378
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 379 GQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKA 458
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 21312260 459 IYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
41-504 9.81e-168

Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.


Pssm-ID: 143429 [Multi-domain]  Cd Length: 480  Bit Score: 483.05  E-value: 9.81e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  41 LFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:cd07111  24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALPGHVRARHLYRIARHIQKHQRL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 121 LASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKwhgktipMDGEhfcFTRHEPVGVCGQIIPWNFPLVMQGWKLAP 200
Cdd:cd07111 101 FAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQL-------LDTE---LAGWKPVGVVGQIVPWNFPLLMLAWKICP 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 201 ALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTaGAAIAQHMDVDKVAFTGSTEVGHLIQKA-AGES 279
Cdd:cd07111 171 ALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRAtAGTG 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 280 nlKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQ 359
Cdd:cd07111 250 --KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAID 327
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 360 QGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRA 439
Cdd:cd07111 328 MGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALA 407
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21312260 440 NNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAY 504
Cdd:cd07111 408 NNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
40-513 7.43e-160

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 462.84  E-value: 7.43e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   40 KLFINNEWhDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:PRK13473   4 KLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFP---EWSQTTPKERAEALLKLADAIEENAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  120 YLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTipmDGE----HFCFTRHEPVGVCGQIIPWNFPLVMQG 195
Cdd:PRK13473  80 EFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKA---AGEylegHTSMIRRDPVGVVASIAPWNYPLMMAA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  196 WKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAgFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVG-HLIQK 274
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGkHVLSA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  275 AAGesNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPF 354
Cdd:PRK13473 236 AAD--SVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPD 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  355 ELDTQQGPQVDKEQFERILGYIRLGQKEG-AKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIE 433
Cdd:PRK13473 314 DEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  434 EVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIK 513
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
58-512 2.10e-159

Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.


Pssm-ID: 143425 [Multi-domain]  Cd Length: 456  Bit Score: 461.07  E-value: 2.10e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESy 137
Cdd:cd07107   1 VINPATGQVLARVPAASAADVDRAVAAARAAFP---EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAM- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 138 VLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTP 217
Cdd:cd07107  77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 218 LSALYLASLIKEAgFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGESnLKRVTLELGGKSPSIVL 297
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 298 ADADMEHAVDqcheALFFNM-----GQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERI 372
Cdd:cd07107 235 PDADPEAAAD----AAVAGMnftwcGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRV 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 373 LGYIRLGQKEGAKLLCGGER----LGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAA 448
Cdd:cd07107 311 MHYIDSAKREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTA 390
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21312260 449 AVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07107 391 AIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
58-512 2.16e-158

Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.


Pssm-ID: 143426  Cd Length: 457  Bit Score: 458.36  E-value: 2.16e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:cd07108   1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 138 VLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTP 217
Cdd:cd07108  78 RPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 218 LSALYLASLIKEAgFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVL 297
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVF 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 298 ADADMEHAVDQCHEAL-FFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYI 376
Cdd:cd07108 236 PDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 377 RLGQKE-GAKLLCGG----ERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVF 451
Cdd:cd07108 316 DLGLSTsGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21312260 452 TRDLDKAIYFTQALQAGTVWVNtynivTCHTP-----FGGFKESGNGRELGEDG-LRAYTEVKTVTI 512
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVN-----QGGGQqpgqsYGGFKQSGLGREASLEGmLEHFTQKKTVNI 457
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
41-513 8.27e-157

Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.


Pssm-ID: 143431  Cd Length: 477  Bit Score: 454.98  E-value: 8.27e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  41 LFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgSPWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:cd07113   2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 121 LASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKT----IP-MDGEHF-CFTRHEPVGVCGQIIPWNFPLVMQ 194
Cdd:cd07113  80 LAQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsIPsMQGERYtAFTRREPVGVVAGIVPWNFSVMIA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 195 GWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTaGAAIAQHMDVDKVAFTGSTEVGHLIQK 274
Cdd:cd07113 160 VWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGR 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 275 AAgESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPF 354
Cdd:cd07113 239 QA-ASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPM 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 355 ELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPT--VFGDVQDgmRIAKEEIFGPVQPLFKFKKI 432
Cdd:cd07113 318 DESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTlvLARSADS--RLMREETFGPVVSFVPYEDE 395
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 433 EEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07113 396 EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475

                .
gi 21312260 513 K 513
Cdd:cd07113 476 R 476
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
39-512 2.92e-156

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 454.35  E-value: 2.92e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   39 NKLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGSpWRRMDASERGRLLNRLADLVERDR 118
Cdd:PRK09847  20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLADLMEAHA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  119 VYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKL 198
Cdd:PRK09847  99 EELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  199 APALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGE 278
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  279 SNLKRVTLELGGKSPSIVLADA-DMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELD 357
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  358 TQQGPQVDKEQFERILGYIRLGQKEGAKLLCGgeRLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQ 437
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21312260  438 RANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
42-512 1.10e-154

Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.


Pssm-ID: 143407 [Multi-domain]  Cd Length: 468  Bit Score: 449.41  E-value: 1.10e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  42 FINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:cd07088   1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA---WERLPAIERAAYLRKLADLIRENADEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 122 ASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIPMD--GEHFcFTRHEPVGVCGQIIPWNFPLVMQGWKLA 199
Cdd:cd07088  78 AKLIVEEQGKTLSLARV-EVEFTADYIDYMAEWARRIEGEIIPSDrpNENI-FIFKVPIGVVAGILPWNFPFFLIARKLA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 200 PALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEs 279
Cdd:cd07088 156 PALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE- 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 280 NLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQ 359
Cdd:cd07088 235 NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATD 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 360 QGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL-GERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQR 438
Cdd:cd07088 315 MGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIEL 394
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21312260 439 ANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07088 395 ANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
42-512 2.99e-153

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.


Pssm-ID: 143434 [Multi-domain]  Cd Length: 479  Bit Score: 446.13  E-value: 2.99e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  42 FINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:cd07116   4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAK---EAWGKTSVAERANILNKIADRMEANLEML 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 122 ASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPA 201
Cdd:cd07116  81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 202 LATGNTVVMKVAEQTPLSALYLASLIKEAgFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNL 281
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NI 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 282 KRVTLELGGKSPSIVLADADMEHA--VDQCHE--ALF-FNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFEL 356
Cdd:cd07116 239 IPVTLELGGKSPNIFFADVMDADDafFDKALEgfVMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDT 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 357 DTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGER-----LGERGFFIKPTVFGDVQdgMRIAKEEIFGPVQPLFKFKK 431
Cdd:cd07116 319 ETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelggLLGGGYYVPTTFKGGNK--MRIFQEEIFGPVLAVTTFKD 396
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 432 IEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVT 511
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 476

                .
gi 21312260 512 I 512
Cdd:cd07116 477 V 477
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
42-512 2.98e-152

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).


Pssm-ID: 143405 [Multi-domain]  Cd Length: 478  Bit Score: 443.54  E-value: 2.98e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  42 FINNEWHDAvSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:cd07086   2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 122 ASLETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWHGKTIPMD-GEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAP 200
Cdd:cd07086  78 GRLVSLEMGKILPEG-LGEVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 201 ALATGNTVVMKVAEQTPLSALYLASLIKEA----GFPPGVVNIITGYGPtAGAAIAQHMDVDKVAFTGSTEVGHLIQKAA 276
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETV 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 277 GESNlKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFEL 356
Cdd:cd07086 236 ARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 357 DTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL--GERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEE 434
Cdd:cd07086 315 GTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 435 VIQRANNTRYGLAAAVFTRDLDKAIYFTQA--LQAGTVWVntyNIVT----CHTPFGGFKESGNGRELGEDGLRAYTEVK 508
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNV---NIPTsgaeIGGAFGGEKETGGGRESGSDAWKQYMRRS 471

                ....
gi 21312260 509 TVTI 512
Cdd:cd07086 472 TCTI 475
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
56-512 1.41e-150

Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143467 [Multi-domain]  Cd Length: 453  Bit Score: 438.18  E-value: 1.41e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  56 FPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGspwRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQE 135
Cdd:cd07149   1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 136 SYVlDLDEVIKVYRYFAGWADKWHGKTIPMD----GEH-FCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVM 210
Cdd:cd07149  78 ARK-EVDRAIETLRLSAEEAKRLAGETIPFDaspgGEGrIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 211 KVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGesnLKRVTLELGG 290
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGS 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 291 KSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFE 370
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 371 RILGYIRLGQKEGAKLLCGGERlgeRGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAV 450
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGKR---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21312260 451 FTRDLDKAIYFTQALQAGTVWVN---TYNIVtcHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMINdssTFRVD--HMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
41-511 6.08e-150

Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.


Pssm-ID: 143442  Cd Length: 512  Bit Score: 438.97  E-value: 6.08e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  41 LFINNEWHDavSKKTFPTVNP-TTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:cd07124  35 LVIGGKEVR--TEEKIESRNPaDPSEVLGTVQKATKEEAEAAVQAARAAFP---TWRRTPPEERARLLLRAAALLRRRRF 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 120 YLASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIPM-DGEHfCFTRHEPVGVCGQIIPWNFPL-VMQGWK 197
Cdd:cd07124 110 ELAAWMVLEVGKNWAEADA-DVAEAIDFLEYYAREMLRLRGFPVEMvPGED-NRYVYRPLGVGAVISPWNFPLaILAGMT 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 198 LApALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAA- 276
Cdd:cd07124 188 TA-ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAa 266
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 277 ----GESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGN 352
Cdd:cd07124 267 kvqpGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGD 346
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 353 PFELDTQQGPQVDKEQFERILGYIRLGQKEGaKLLCGGERLGE--RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFK 430
Cdd:cd07124 347 PEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 431 KIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVN---TYNIVTCHtPFGGFKESG-NGRELGEDGLRAYTE 506
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkiTGALVGRQ-PFGGFKMSGtGSKAGGPDYLLQFMQ 504

                ....*
gi 21312260 507 VKTVT 511
Cdd:cd07124 505 PKTVT 509
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
42-510 2.62e-148

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 434.12  E-value: 2.62e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   42 FINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:PLN02278  28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLTASERSKILRRWYDLIIANKEDL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  122 ASLETLDNGKPFQESYvldlDEVikVY-----RYFAGWADKWHGKTIPM-DGEHFCFTRHEPVGVCGQIIPWNFPLVMQG 195
Cdd:PLN02278 105 AQLMTLEQGKPLKEAI----GEV--AYgasflEYFAEEAKRVYGDIIPSpFPDRRLLVLKQPVGVVGAITPWNFPLAMIT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  196 WKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKA 275
Cdd:PLN02278 179 RKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAG 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  276 AGESnLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFE 355
Cdd:PLN02278 259 AAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFE 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  356 LDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEV 435
Cdd:PLN02278 338 EGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEA 417
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21312260  436 IQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:PLN02278 418 IAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
56-512 1.10e-145

Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.


Pssm-ID: 143463 [Multi-domain]  Cd Length: 456  Bit Score: 425.99  E-value: 1.10e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  56 FPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQE 135
Cdd:cd07145   1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAK---DVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 136 SyVLDLDEVIKVYRYFAGWADKWHGKTIPMDG-----EHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVM 210
Cdd:cd07145  78 S-RVEVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 211 KVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGeSNLKRVTLELGG 290
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 291 KSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFE 370
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 371 RILGYIRLGQKEGAKLLCGGERlgERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAV 450
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGKR--DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21312260 451 FTRDLDKAIYFTQALQAGTVWVN-TYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
56-512 5.37e-144

Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.


Pssm-ID: 143468 [Multi-domain]  Cd Length: 451  Bit Score: 421.35  E-value: 5.37e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  56 FPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQE 135
Cdd:cd07150   1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 136 SYVldldEVIKVYRYF---AGWADKWHGKTIPMDGE-HFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMK 211
Cdd:cd07150  78 AWF----ETTFTPELLraaAGECRRVRGETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 212 VAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGeSNLKRVTLELGGK 291
Cdd:cd07150 154 PSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG-RHLKKITLELGGK 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 292 SPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFER 371
Cdd:cd07150 233 NPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVER 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 372 ILGYIRLGQKEGAKLLCGGERLGErgfFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVF 451
Cdd:cd07150 313 IKRQVEDAVAKGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAIL 389
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21312260 452 TRDLDKAIYFTQALQAGTVWVNTYNIVT-CHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07150 390 TNDLQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
77-512 4.44e-140

ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.


Pssm-ID: 143422 [Multi-domain]  Cd Length: 431  Bit Score: 410.77  E-value: 4.44e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  77 DVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWAD 156
Cdd:cd07104   1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAF-EVGAAIAILREAAGLPR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 157 KWHGKTIPMDGE-HFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLS-ALYLASLIKEAGFPP 234
Cdd:cd07104  77 RPEGEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 235 GVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALF 314
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 315 FNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERlg 394
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY-- 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 395 eRGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVN- 473
Cdd:cd07104 314 -EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINd 392
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 21312260 474 -TYNiVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07104 393 qTVN-DEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
58-511 2.83e-138

Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.


Pssm-ID: 143438 [Multi-domain]  Cd Length: 455  Bit Score: 407.11  E-value: 2.83e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlGSPWRRmDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:cd07120   1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFD-ETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 138 VlDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTP 217
Cdd:cd07120  79 F-EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 218 LSALYLASLIKEA-GFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQkAAGESNLKRVTLELGGKSPSIV 296
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIM-AAAAPTLKRLGLELGGKTPCIV 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 297 LADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYI 376
Cdd:cd07120 237 FDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 377 RLGQKEGAKLLCGGERLGE---RGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTR 453
Cdd:cd07120 317 ERAIAAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21312260 454 DLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVT 511
Cdd:cd07120 397 DLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
78-512 6.84e-133

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.


Pssm-ID: 143418 [Multi-domain]  Cd Length: 429  Bit Score: 392.21  E-value: 6.84e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  78 VDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESyvldLDEVIK---VYRYFAGW 154
Cdd:cd07100   1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA----RAEVEKcawICRYYAEN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 155 ADKW-HGKTIPMDGEHfCFTRHEPVGVCGQIIPWNFPL--VMQGwkLAPALATGNTVVMKVAEQTPLSALYLASLIKEAG 231
Cdd:cd07100  74 AEAFlADEPIETDAGK-AYVRYEPLGVVLGIMPWNFPFwqVFRF--AAPNLMAGNTVLLKHASNVPGCALAIEELFREAG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 232 FPPGV-VNIITGYGpTAGAAIAqHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCH 310
Cdd:cd07100 151 FPEGVfQNLLIDSD-QVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTAV 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 311 EALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGG 390
Cdd:cd07100 228 KGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGG 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 391 ERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTV 470
Cdd:cd07100 308 KRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMV 387
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 21312260 471 WVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07100 388 FINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
59-512 2.26e-131

ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.


Pssm-ID: 143413 [Multi-domain]  Cd Length: 453  Bit Score: 389.48  E-value: 2.26e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYV 138
Cdd:cd07094   4 HNPYDGEVIGKVPADDRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 139 lDLDEVIKVYRYFAGWADKWHGKTIPMD-----GEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVA 213
Cdd:cd07094  81 -EVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 214 EQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGesnLKRVTLELGGKSP 293
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNAP 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 294 SIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERIL 373
Cdd:cd07094 237 VIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVE 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 374 GYIRLGQKEGAKLLCGGERlgeRGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTR 453
Cdd:cd07094 317 RWVEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR 393
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 454 DLDKAIYFTQALQAGTVWVNTYNIV-TCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07094 394 DLNVAFKAAEKLEVGGVMVNDSSAFrTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
40-511 2.58e-128

Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.


Pssm-ID: 143404 [Multi-domain]  Cd Length: 478  Bit Score: 382.25  E-value: 2.58e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  40 KLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRV 119
Cdd:cd07085   2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENLD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 120 YLASLETLDNGKPFQESYVlDLDEVIKVYRYFAGwadkwhgktIP--MDGEHF--------CFTRHEPVGVCGQIIPWNF 189
Cdd:cd07085  79 ELARLITLEHGKTLADARG-DVLRGLEVVEFACS---------IPhlLKGEYLenvargidTYSYRQPLGVVAGITPFNF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 190 PLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVG 269
Cdd:cd07085 149 PAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVG 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 270 HLIQKAAGeSNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRK 349
Cdd:cd07085 228 EYIYERAA-ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLK 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 350 VGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL----GERGFFIKPTVFGDVQDGMRIAKEEIFGPVQP 425
Cdd:cd07085 307 VGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVkvpgYENGNFVGPTILDNVTPDMKIYKEEIFGPVLS 386
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 426 LFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNtyniV-----TCHTPFGGFKES--GNGRELGE 498
Cdd:cd07085 387 IVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VpipvpLAFFSFGGWKGSffGDLHFYGK 462
                       490
                ....*....|...
gi 21312260 499 DGLRAYTEVKTVT 511
Cdd:cd07085 463 DGVRFYTQTKTVT 475
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
59-512 6.28e-128

Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.


Pssm-ID: 143417 [Multi-domain]  Cd Length: 453  Bit Score: 380.41  E-value: 6.28e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESyV 138
Cdd:cd07099   1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRA---WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADA-G 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 139 LDLDEVIKVYRYFAGWADK-------WHGKTIPmdgEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMK 211
Cdd:cd07099  77 LEVLLALEAIDWAARNAPRvlaprkvPTGLLMP---NKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 212 VAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQhmDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGK 291
Cdd:cd07099 154 PSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA--GVDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGK 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 292 SPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFER 371
Cdd:cd07099 231 DPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDI 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 372 ILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVF 451
Cdd:cd07099 311 VRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVF 390
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21312260 452 TRDLDKAIYFTQALQAGTVWVN--TYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07099 391 SRDLARAEAIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
41-511 7.44e-128

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 382.36  E-value: 7.44e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   41 LFINNEWHDavSKKTFPTVNPT-TGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:PRK03137  39 LIIGGERIT--TEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE---TWKKWSPEDRARILLRAAAIIRRRKH 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  120 YLASLETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKW-HGKTI-PMDGEHfCFTRHEPVGVCGQIIPWNFPL-VMQGW 196
Cdd:PRK03137 114 EFSAWLVKEAGKPWAEA-DADTAEAIDFLEYYARQMLKLaDGKPVeSRPGEH-NRYFYIPLGVGVVISPWNFPFaIMAGM 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  197 KLAPaLATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVG-HLIQKA 275
Cdd:PRK03137 192 TLAA-IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGlRIYERA 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  276 A----GESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVG 351
Cdd:PRK03137 271 AkvqpGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVG 350
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  352 NPfELDTQQGPQVDKEQFERILGYIRLGQKEGaKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKK 431
Cdd:PRK03137 351 NP-EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD 428
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  432 IEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVN---TYNIVTCHtPFGGFKESG-NGRELGEDGLRAYTEV 507
Cdd:PRK03137 429 FDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgcTGAIVGYH-PFGGFNMSGtDSKAGGPDYLLLFLQA 507

                 ....
gi 21312260  508 KTVT 511
Cdd:PRK03137 508 KTVS 511
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
45-513 1.16e-122

NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.


Pssm-ID: 143469 [Multi-domain]  Cd Length: 465  Bit Score: 367.40  E-value: 1.16e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  45 NEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAfrlGSPWRRMDASERGRLLNRLADLVERDRVYLASL 124
Cdd:cd07151   1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA---QKEWAATLPQERAEILEKAAQILEERRDEIVEW 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 125 ETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWHGKTIPMD---GEHFCFtrHEPVGVCGQIIPWNFPLVMQGWKLAPA 201
Cdd:cd07151  78 LIRESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPSDvpgKENRVY--REPLGVVGVISPWNFPLHLSMRSVAPA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 202 LATGNTVVMKVAEQTPLSA-LYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsN 280
Cdd:cd07151 155 LALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR-H 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 281 LKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQ 360
Cdd:cd07151 234 LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVV 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 361 GPQVDKEQFERILGYIRLGQKEGAKLLCGGERlgeRGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRAN 440
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAN 390
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21312260 441 NTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIV-TCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIK 513
Cdd:cd07151 391 DTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
59-512 7.17e-122

Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.


Pssm-ID: 143464 [Multi-domain]  Cd Length: 451  Bit Score: 364.76  E-value: 7.17e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  59 VNPTTGEVIGHVAEGDRadvdlavKAAREAFRLGSPWR-RMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:cd07146   4 RNPYTGEVVGTVPAGTE-------EALREALALAASYRsTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 138 VlDLDEVIKVYRYFAGWADKWHGKTIPMD-----GEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKV 212
Cdd:cd07146  77 Y-EVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 213 AEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGesnLKRVTLELGGKS 292
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGND 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 293 PSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERI 372
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 373 LGYIRLGQKEGAKLLCGGERlgeRGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFT 452
Cdd:cd07146 313 ENRVEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21312260 453 RDLDKAIYFTQALQAGTVWVNT---YNivTCHTPFGGFKESGNG-RELGEDGLRAYTEVKTVTI 512
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNEvpgFR--SELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
40-513 1.68e-119

NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.


Pssm-ID: 143401 [Multi-domain]  Cd Length: 473  Bit Score: 359.58  E-value: 1.68e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  40 KLFINNEWHDAvSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgSPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:cd07082   3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR--GWWPTMPLEERIDCLHKFADLLKENKE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 120 YLASLETLDNGKPFQES---------YVLDLDEVIKvyryfagwadKWHGKTIPMDGEHF-----CFTRHEPVGVCGQII 185
Cdd:cd07082  80 EVANLLMWEIGKTLKDAlkevdrtidYIRDTIEELK----------RLDGDSLPGDWFPGtkgkiAQVRREPLGVVLAIG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 186 PWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGS 265
Cdd:cd07082 150 PFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGS 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 266 TEVGHLIQKAAGesnLKRVTLELGGKSPSIVLADADMEHAVDQCHE-ALFFNmGQCCCAGSRTFVEESIYREFLERTVEK 344
Cdd:cd07082 230 TEVGNRLKKQHP---MKRLVLELGGKDPAIVLPDADLELAAKEIVKgALSYS-GQRCTAIKRVLVHESVADELVELLKEE 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 345 AKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERgfFIKPTVFGDVQDGMRIAKEEIFGPVQ 424
Cdd:cd07082 306 VAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREGGN--LIYPTLLDPVTPDMRLAWEEPFGPVL 383
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 425 PLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYnivtC-----HTPFGGFKESGNGRELGED 499
Cdd:cd07082 384 PIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSK----CqrgpdHFPFLGRKDSGIGTQGIGD 459
                       490
                ....*....|....
gi 21312260 500 GLRAYTEVKTVTIK 513
Cdd:cd07082 460 ALRSMTRRKGIVIN 473
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
49-511 2.12e-117

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 356.11  E-value: 2.12e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   49 DAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLD 128
Cdd:PRK09407  27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQR---AWAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  129 NGK----PFQEsyVLDldeVIKVYRYFAGWA-----DKWHGKTIPMdgehfcFTR----HEPVGVCGQIIPWNFPLVMQG 195
Cdd:PRK09407 104 TGKarrhAFEE--VLD---VALTARYYARRApkllaPRRRAGALPV------LTKttelRQPKGVVGVISPWNYPLTLAV 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  196 WKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHmdVDKVAFTGSTEVGHLIQKA 275
Cdd:PRK09407 173 SDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQ 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  276 AGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFE 355
Cdd:PRK09407 251 AGR-RLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYD 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  356 LDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERG-FFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEE 434
Cdd:PRK09407 330 YSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDE 409
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  435 VIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVN-----TYNIVTchTPFGGFKESGNGRELGEDGLRAYTEVKT 509
Cdd:PRK09407 410 AVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVD--APMGGMKDSGLGRRHGAEGLLKYTESQT 487

                 ..
gi 21312260  510 VT 511
Cdd:PRK09407 488 IA 489
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
61-511 6.89e-116

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).


Pssm-ID: 143419 [Multi-domain]  Cd Length: 454  Bit Score: 349.69  E-value: 6.89e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  61 PTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGK----PFQEs 136
Cdd:cd07101   3 PFTGEPLGELPQSTPADVEAAFARARAAQR---AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKarrhAFEE- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 137 yVLDldeVIKVYRYFAGWADKW-----HGKTIPMdgehfcFTR----HEPVGVCGQIIPWNFPLVMQGWKLAPALATGNT 207
Cdd:cd07101  79 -VLD---VAIVARYYARRAERLlkprrRRGAIPV------LTRttvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 208 VVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHmdVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLE 287
Cdd:cd07101 149 VVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGR-RLIGCSLE 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 288 LGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKE 367
Cdd:cd07101 226 LGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQA 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 368 QFERILGYIRLGQKEGAKLLCGGERLGERG-FFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGL 446
Cdd:cd07101 306 QLDRVTAHVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGL 385
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 447 AAAVFTRDLDKAIYFTQALQAGTVWVN-----TYNIVTchTPFGGFKESGNGRELGEDGLRAYTEVKTVT 511
Cdd:cd07101 386 NASVWTRDGARGRRIAARLRAGTVNVNegyaaAWASID--APMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
56-512 2.38e-113

Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.


Pssm-ID: 143465 [Multi-domain]  Cd Length: 452  Bit Score: 343.07  E-value: 2.38e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  56 FPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQE 135
Cdd:cd07147   1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 136 SYVlDLDEVIKVYRYFAGWADKWHGKTIPMDG-----EHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVM 210
Cdd:cd07147  78 ARG-EVARAIDTFRIAAEEATRIYGEVLPLDIsargeGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 211 KVAEQTPLSALYLASLIKEAGFPPGVVNIITGygPTAGAAI-AQHMDVDKVAFTGSTEVGHLIQKAAGEsnlKRVTLELG 289
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELG 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 290 GKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQF 369
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 370 ERILGYIRLGQKEGAKLLCGGERlgeRGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAA 449
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 450 VFTRDLDKAIYFTQALQAGTVWVN---TYNIVtcHTPFGGFKESGNGRElgedGLR----AYTEVKTVTI 512
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVINdvpTFRVD--HMPYGGVKDSGIGRE----GVRyaieEMTEPRLLVI 452
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
77-512 1.92e-112

Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.


Pssm-ID: 143423 [Multi-domain]  Cd Length: 432  Bit Score: 339.94  E-value: 1.92e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  77 DVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNG--KPFQEsyvLDLDEVIKVYRYFAGW 154
Cdd:cd07105   1 DADQAVEAAAAAF---PAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGatAAWAG---FNVDLAAGMLREAASL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 155 ADKWHGKTIPMDGE-HFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFP 233
Cdd:cd07105  75 ITQIIGGSIPSDKPgTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 234 PGVVNIITGY---GPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCH 310
Cdd:cd07105 155 KGVLNVVTHSpedAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAAL 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 311 EALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGnpfelDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGG 390
Cdd:cd07105 234 FGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGG 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 391 -ERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGT 469
Cdd:cd07105 309 lADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 21312260 470 VWVNTYNIVTCHT-PFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07105 389 VHINGMTVHDEPTlPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
64-497 1.15e-111

NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.


Pssm-ID: 143470 [Multi-domain]  Cd Length: 443  Bit Score: 338.50  E-value: 1.15e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  64 GEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKpFQESYVLDLDE 143
Cdd:cd07152   1 GAVLGEVGVADAADVDRAAARAAAAQR---AWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGS-IRPKAGFEVGA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 144 VIKVYRYFAGWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSA-LY 222
Cdd:cd07152  77 AIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 223 LASLIKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADM 302
Cdd:cd07152 157 IARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADL 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 303 EHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKE 382
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAA 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 383 GAKLLCGGERlgeRGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFT 462
Cdd:cd07152 315 GARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALA 391
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 21312260 463 QALQAGTVWVN--TYNiVTCHTPFGGFKESGNGRELG 497
Cdd:cd07152 392 DRLRTGMLHINdqTVN-DEPHNPFGGMGASGNGSRFG 427
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
42-514 8.16e-111

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 337.65  E-value: 8.16e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   42 FINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:PRK11241  14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRWFNLMMEHQDDL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  122 ASLETLDNGKPFQE-----SYVLDLDEvikvyrYFAGWADKWHGKTIP-MDGEHFCFTRHEPVGVCGQIIPWNFPLVMQG 195
Cdd:PRK11241  91 ARLMTLEQGKPLAEakgeiSYAASFIE------WFAEEGKRIYGDTIPgHQADKRLIVIKQPIGVTAAITPWNFPAAMIT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  196 WKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVG-HLIQK 274
Cdd:PRK11241 165 RKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGrQLMEQ 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  275 AAgeSNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPF 354
Cdd:PRK11241 245 CA--KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGL 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  355 ELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEE 434
Cdd:PRK11241 323 EKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEAD 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  435 VIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIKV 514
Cdd:PRK11241 403 VIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
59-510 8.10e-109

Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.


Pssm-ID: 143420 [Multi-domain]  Cd Length: 452  Bit Score: 331.52  E-value: 8.10e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQEsYV 138
Cdd:cd07102   1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG---WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQ-AG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 139 LDLDEVIKVYRYFAGWADKWHGKTIPMDGEHFC-FTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTP 217
Cdd:cd07102  77 GEIRGMLERARYMISIAEEALADIRVPEKDGFErYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 218 LSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHmDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVL 297
Cdd:cd07102 157 LCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP-RIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYVR 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 298 ADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIR 377
Cdd:cd07102 235 PDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIA 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 378 LGQKEGAKLLCGGERLGER---GFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRD 454
Cdd:cd07102 315 DAIAKGARALIDGALFPEDkagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKD 394
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21312260 455 LDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07102 395 IARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
150-513 3.60e-101

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 310.51  E-value: 3.60e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  150 YFAGWADKWHGKTIPMD--GEH-FCFTRhePVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASL 226
Cdd:PRK10090  43 YMAEWARRYEGEIIQSDrpGENiLLFKR--ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKI 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  227 IKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAV 306
Cdd:PRK10090 121 VDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAV 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  307 DQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFE-LDTQQGPQVDKEQFERILGYIRLGQKEGAK 385
Cdd:PRK10090 200 KAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGAR 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  386 LLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQAL 465
Cdd:PRK10090 280 VALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGL 359
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 21312260  466 QAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIK 513
Cdd:PRK10090 360 KFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVVYLQ 407
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
59-511 2.68e-100

Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.


Pssm-ID: 143416 [Multi-domain]  Cd Length: 465  Bit Score: 310.00  E-value: 2.68e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPfqesyV 138
Cdd:cd07098   1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQR---EWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKT-----M 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 139 LD--LDEVIKVyryfagwADK--W---HG----KTIPMDGEHFCFTR-----HEPVGVCGQIIPWNFPLVMQGWKLAPAL 202
Cdd:cd07098  73 VDasLGEILVT-------CEKirWtlkHGekalRPESRPGGLLMFYKrarveYEPLGVVGAIVSWNYPFHNLLGPIIAAL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 203 ATGNTVVMKVAEQTPLSALYLASLIKEA----GFPPGVVNIITGYGPTaGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGE 278
Cdd:cd07098 146 FAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAE 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 279 SnLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDT 358
Cdd:cd07098 225 S-LTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDV 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 359 QQGPQVDKEQFERILGYIRLGQKEGAKLLCGGER----LGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEE 434
Cdd:cd07098 304 DVGAMISPARFDRLEELVADAVEKGARLLAGGKRyphpEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEE 383
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21312260 435 VIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTY--NIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVT 511
Cdd:cd07098 384 AVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFgvNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
gabD1 PRK09406
succinic semialdehyde dehydrogenase; Reviewed
58-512 2.28e-94

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181826 [Multi-domain]  Cd Length: 457  Bit Score: 294.34  E-value: 2.28e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:PRK09406   5 TINPATGETVKTFTALTDDEVDAAIARAHARFR---DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  138 vldlDEVIKVYRYFAGWADkwHGKTI----PMD----GEHFCFTRHEPVGVCGQIIPWNFPLvmqgWKL----APALATG 205
Cdd:PRK09406  82 ----AEALKCAKGFRYYAE--HAEALladePADaaavGASRAYVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  206 NTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITgYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGESnLKRVT 285
Cdd:PRK09406 152 NVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTV 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  286 LELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVD 365
Cdd:PRK09406 230 LELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLAT 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  366 KEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYG 445
Cdd:PRK09406 310 EQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFG 389
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21312260  446 LAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:PRK09406 390 LGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
44-512 1.24e-93

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.


Pssm-ID: 143448  Cd Length: 474  Bit Score: 292.96  E-value: 1.24e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  44 NNEWhdAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYLAS 123
Cdd:cd07130   4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKEALGK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 124 LETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWHGKTIPmdGE---HFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAP 200
Cdd:cd07130  79 LVSLEMGKILPEG-LGEVQEMIDICDFAVGLSRQLYGLTIP--SErpgHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 201 ALATGNTVVMKVAEQTPLSAL----YLASLIKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAA 276
Cdd:cd07130 156 ALVCGNVVVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAV 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 277 GEsNLKRVTLELGGKSPSIVLADADMEHAVDqcheALFF----NMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGN 352
Cdd:cd07130 235 AA-RFGRSLLELGGNNAIIVMEDADLDLAVR----AVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGD 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 353 PFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPT-VFGDVQDGmrIAKEEIFGPVQPLFKFKK 431
Cdd:cd07130 310 PLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTiVEGLSDAP--IVKEETFAPILYVLKFDT 387
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 432 IEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTyNIVTCHT----PFGGFKESGNGRELGEDGLRAYTEV 507
Cdd:cd07130 388 LEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNV-NIGTSGAeiggAFGGEKETGGGRESGSDAWKQYMRR 466

                ....*
gi 21312260 508 KTVTI 512
Cdd:cd07130 467 STCTI 471
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
41-511 3.78e-89

ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.


Pssm-ID: 143402 [Multi-domain]  Cd Length: 500  Bit Score: 282.16  E-value: 3.78e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  41 LFINNEWHDAVSKKTfpTVNP-TTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:cd07083  21 LVIGGEWVDTKERMV--SVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFK---TWKDWPQEDRARLLLKAADLLRRRRR 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 120 YLASLETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWHGKTI------PMDGEHFcftrHEPVGVCGQIIPWNFPLVM 193
Cdd:cd07083  96 ELIATLTYEVGKNWVEA-IDDVAEAIDFIRYYARAALRLRYPAVevvpypGEDNESF----YVGLGAGVVISPWNFPVAI 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 194 QGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQ 273
Cdd:cd07083 171 FTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIY 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 274 KAAGE-----SNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQR 348
Cdd:cd07083 251 EAAARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERL 330
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 349 KVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGaKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFK 428
Cdd:cd07083 331 SVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIR 409
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 429 FK--KIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNI--VTCHTPFGGFKESG-NGRELGEDGLRA 503
Cdd:cd07083 410 YKddDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITgaLVGVQPFGGFKLSGtNAKTGGPHYLRR 489

                ....*...
gi 21312260 504 YTEVKTVT 511
Cdd:cd07083 490 FLEMKAVA 497
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
21-497 6.67e-86

Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.


Pssm-ID: 143443 [Multi-domain]  Cd Length: 518  Bit Score: 274.46  E-value: 6.67e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  21 YSTAAALPNPIPNPEICY----NKLFINNEWHDAVSKktfptvnPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWR 96
Cdd:cd07125  17 EALADALKAFDEKEWEAIpiinGEETETGEGAPVIDP-------ADHERTIGEVSLADAEDVDAALAIAAAAF---AGWS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  97 RMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESyvldLDEV---IKVYRYFAGWADK-WHGKTIPMDGEHFCF 172
Cdd:cd07125  87 ATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADA----DAEVreaIDFCRYYAAQARElFSDPELPGPTGELNG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 173 TRHEP--VGVCgqIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAA 250
Cdd:cd07125 163 LELHGrgVFVC--ISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 251 IAQHMDVDKVAFTGSTEVGHLIQKAAGESNLKRVTL--ELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTF 328
Cdd:cd07125 241 LVAHPRIDGVIFTGSTETAKLINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLY 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 329 VEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEgAKLLCGGERLGERGFFIKPTVFGDV 408
Cdd:cd07125 321 LQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIV 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 409 qdGMRIAKEEIFGPVQPL--FKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVN---TYNIVTCHtP 483
Cdd:cd07125 400 --GIFDLTTEVFGPILHVirFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrniTGAIVGRQ-P 476
                       490
                ....*....|....
gi 21312260 484 FGGFKESGNGRELG 497
Cdd:cd07125 477 FGGWGLSGTGPKAG 490
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
77-494 9.20e-81

N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.


Pssm-ID: 143414 [Multi-domain]  Cd Length: 431  Bit Score: 258.36  E-value: 9.20e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  77 DVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESyvldLDEV----------IK 146
Cdd:cd07095   1 QVDAAVAAARAAFP---GWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA----QTEVaamagkidisIK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 147 VYRYFAGwadkwhGKTIPMdGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASL 226
Cdd:cd07095  74 AYHERTG------ERATPM-AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVEL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 227 IKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGESNLKRVTLELGGKSPSIVLADADMEHAV 306
Cdd:cd07095 147 WEEAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAA 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 307 DQCHEALFFNMGQCCCAGSRTFVEESIY-REFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERilgYIRLGQK---E 382
Cdd:cd07095 226 YLIVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAAR---YLLAQQDllaL 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 383 GAKLLCGGERLGERGFFIKPTVFgDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFT 462
Cdd:cd07095 303 GGEPLLAMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFL 381
                       410       420       430
                ....*....|....*....|....*....|...
gi 21312260 463 QALQAGTV-WVNTYNIVTCHTPFGGFKESGNGR 494
Cdd:cd07095 382 ARIRAGIVnWNRPTTGASSTAPFGGVGLSGNHR 414
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
59-493 2.22e-76

Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143466 [Multi-domain]  Cd Length: 455  Bit Score: 247.72  E-value: 2.22e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  59 VNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLGSPWrrMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYV 138
Cdd:cd07148   4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 139 lDLDEVIKVYRYFAGWADKWHGKTIPMD----GE-HFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVA 213
Cdd:cd07148  82 -EVTRAIDGVELAADELGQLGGREIPMGltpaSAgRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 214 EQTPLSALYLASLIKEAGFPPGVVNIITgygptAGAAIAQHMDVD-KVA---FTGSTEVG-HLIQKAAGESnlkRVTLEL 288
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVP-----CENAVAEKLVTDpRVAffsFIGSARVGwMLRSKLAPGT---RCALEH 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 289 GGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQ 368
Cdd:cd07148 233 GGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPRE 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 369 FERILGYIRLGQKEGAKLLCGGERLGERGFfiKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAA 448
Cdd:cd07148 313 VDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQA 390
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 21312260 449 AVFTRDLDKAIYFTQALQAGTVWVNTynivtcHT-------PFGGFKESGNG 493
Cdd:cd07148 391 AVFTKDLDVALKAVRRLDATAVMVND------HTafrvdwmPFAGRRQSGYG 436
MMSDH TIGR01722
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ...
40-511 9.35e-76

methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130783  Cd Length: 477  Bit Score: 246.72  E-value: 9.35e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260    40 KLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRV 119
Cdd:TIGR01722   2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   120 YLASLETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWHGKTIP-----MDgehfCFTRHEPVGVCGQIIPWNFPLVMQ 194
Cdd:TIGR01722  79 EIAELITAEHGKTHSDA-LGDVARGLEVVEHACGVNSLLKGETSTqvatrVD----VYSIRQPLGVCAGITPFNFPAMIP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   195 GWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQK 274
Cdd:TIGR01722 154 LWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   275 aAGESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSrTFVEESIYREFLERTVEKAKQRKVGNPF 354
Cdd:TIGR01722 233 -TGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAIS-AAVLVGAADEWVPEIRERAEKIRIGPGD 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   355 ELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLG----ERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFK 430
Cdd:TIGR01722 311 DPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKvdgyEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEAD 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   431 KIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNtyniVTCHTP-----FGGFKES--GNGRELGEDGLRA 503
Cdd:TIGR01722 391 TLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN----VPIPVPlpyfsFTGWKDSffGDHHIYGKQGTHF 466

                  ....*...
gi 21312260   504 YTEVKTVT 511
Cdd:TIGR01722 467 YTRGKTVT 474
PRK13968 PRK13968
putative succinate semialdehyde dehydrogenase; Provisional
58-510 2.77e-73

putative succinate semialdehyde dehydrogenase; Provisional


Pssm-ID: 184426 [Multi-domain]  Cd Length: 462  Bit Score: 239.76  E-value: 2.77e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   58 TVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESY 137
Cdd:PRK13968  11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFR---DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  138 VldldEVIKVyryfAGWADkW---HG----KTIPMDGEHF-CFTRHEPVGVCGQIIPWNFPL--VMQGwkLAPALATGNT 207
Cdd:PRK13968  88 A----EVAKS----ANLCD-WyaeHGpamlKAEPTLVENQqAVIEYRPLGTILAIMPWNFPLwqVMRG--AVPILLAGNG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  208 VVMKVAEQTPLSALYLASLIKEAGFPPGVVniitGYGPTAGAAIAQHMDVDKVA---FTGSTEVGHLIQKAAGESnLKRV 284
Cdd:PRK13968 157 YLLKHAPNVMGCAQLIAQVFKDAGIPQGVY----GWLNADNDGVSQMINDSRIAavtVTGSVRAGAAIGAQAGAA-LKKC 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  285 TLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQV 364
Cdd:PRK13968 232 VLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMA 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  365 DKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRY 444
Cdd:PRK13968 312 RFDLRDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEF 391
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21312260  445 GLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:PRK13968 392 GLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
95-510 1.64e-72

Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.


Pssm-ID: 143452 [Multi-domain]  Cd Length: 433  Bit Score: 236.74  E-value: 1.64e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  95 WRRMDASERGRLLNRLADLVE--RDRVYLASLEtlDNGKPFQEsyvLDLDEVIKVY-------RYFAGW-ADKWHGKTIP 164
Cdd:cd07134  14 LRASTAAERIAKLKRLKKAILarREEIIAALAA--DFRKPAAE---VDLTEILPVLseinhaiKHLKKWmKPKRVRTPLL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 165 MDGEHfCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAgFPPGVVNIITGyg 244
Cdd:cd07134  89 LFGTK-SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 245 ptaGAAIAQH---MDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCC 321
Cdd:cd07134 165 ---DAEVAQAlleLPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 322 CAGSRTFVEESIYREFLERtVEKAKQRKVGNpfELDTQQGPQ----VDKEQFERILGYIRLGQKEGAKLLCGGE-RLGER 396
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEH-LKAEIEKFYGK--DAARKASPDlariVNDRHFDRLKGLLDDAVAKGAKVEFGGQfDAAQR 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 397 gfFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDlDKAI-YFTQALQAGTVWVNT- 474
Cdd:cd07134 318 --YIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKD-KANVnKVLARTSSGGVVVNDv 394
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 21312260 475 -YNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07134 395 vLHFLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
81-512 8.12e-72

ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.


Pssm-ID: 143406 [Multi-domain]  Cd Length: 426  Bit Score: 234.73  E-value: 8.12e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  81 AVKAAREAFRLGS----PWRRmdaserGRLLNRLADLVERDRVYLASLETlDNGKPFQESYVLD---LDEVIKVY-RYFA 152
Cdd:cd07087   3 LVARLRETFLTGKtrslEWRK------AQLKALKRMLTENEEEIAAALYA-DLGKPPAEAYLTEiavVLGEIDHAlKHLK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 153 GWADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAgF 232
Cdd:cd07087  76 KWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-F 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 233 PPGVVNIITGYGPTAGAAIAQHMDvdKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEA 312
Cdd:cd07087 155 DPEAVAVVEGGVEVATALLAEPFD--HIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAWG 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 313 LFFNMGQCCCAGSRTFVEESIYREFLERtVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIrlgqkEGAKLLCGGER 392
Cdd:cd07087 232 KFLNAGQTCIAPDYVLVHESIKDELIEE-LKKAIKEFYGEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGGQV 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 393 -LGERgfFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVW 471
Cdd:cd07087 306 dKEER--YIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVC 383
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 21312260 472 VNTYNI-VTCHT-PFGGFKESGNGRELGEDGLRAYTEVKTVTI 512
Cdd:cd07087 384 VNDVLLhAAIPNlPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
54-497 5.93e-71

Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 226683 [Multi-domain]  Cd Length: 769  Bit Score: 241.15  E-value: 5.93e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  54 KTFPTVNPTT-GEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKP 132
Cdd:COG4230 127 EPRPVINPADpDDIVGTVTEATEADVEQALEAAVAAA---PIWSATPPAERAAILERAADLMEAQMPQLMGLLVREAGKT 203
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 133 FQESyVLDLDEVIKVYRYFAGWADkwhgktipmdgEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKV 212
Cdd:COG4230 204 LSNA-IAEVREAVDFLRYYAGQAR-----------DTFGNLTHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 271
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 213 AEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGESNLKRVTL--ELGG 290
Cdd:COG4230 272 AEQTPLIAAQAVRLLHEAGVPPGVLQLLPGRGETVGAALTADARVAGVMFTGSTEVARLIQRQLAKRQGRPIPLiaETGG 351
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 291 KSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIyrefLERTVEKAK----QRKVGNPFELDTQQGPQVDK 366
Cdd:COG4230 352 QNAMIVDSSALAEQVVADVLASAFDSAGQRCSALRVLCLQEDV----ADRILTMLKgamaELRVGNPDRLTTDVGPVIDA 427
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 367 EQFERILGYIRlGQKEGAKLLCGGERLGE--RGFFIKPTVFGdvQDGMRIAKEEIFGPVQPLFKFK--KIEEVIQRANNT 442
Cdd:COG4230 428 EAKANIEKHIQ-TMRSKGRLVHQAAAPNSlqKGTFVAPTLIE--LENLDELQREVFGPVLHVVRYKrdELDEVIDQINAT 504
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21312260 443 RYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTyNI---VTCHTPFGGFKESGNGRELG 497
Cdd:COG4230 505 GYGLTLGVHTRIDETIAHVTERAHAGNLYVNR-NIvgaVVGVQPFGGEGLSGTGPKAG 561
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
40-515 1.14e-69

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 231.18  E-value: 1.14e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   40 KLFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRV 119
Cdd:PLN00412  17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA---WAKTPLWKRAELLHKAAAILKEHKA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  120 YLASLETLDNGKPFQESyvldLDEVIK---VYRYFA-------GWADKWHGKTIPMDGEH-FCFTRHEPVGVCGQIIPWN 188
Cdd:PLN00412  94 PIAECLVKEIAKPAKDA----VTEVVRsgdLISYTAeegvrilGEGKFLVSDSFPGNERNkYCLTSKIPLGVVLAIPPFN 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  189 FPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGStEV 268
Cdd:PLN00412 170 YPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DT 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  269 GHLIQKAAGESNLKrvtLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQR 348
Cdd:PLN00412 249 GIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKL 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  349 KVGNPfELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGErgfFIKPTVFGDVQDGMRIAKEEIFGPVQPLFK 428
Cdd:PLN00412 326 TVGPP-EDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGN---LIWPLLLDNVRPDMRIAWEEPFGPVLPVIR 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  429 FKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNIVTC-HTPFGGFKESGNGRELGEDGLRAYTEV 507
Cdd:PLN00412 402 INSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQGITNSINMMTKV 481

                 ....*...
gi 21312260  508 KTVTIKVP 515
Cdd:PLN00412 482 KSTVINLP 489
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
41-494 2.39e-69

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 230.23  E-value: 2.39e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   41 LFINNEWHdAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:PRK09457   3 LWINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  121 LASLETLDNGKPFQESyvldLDEV----------IKVYRYFAGwadkwHGKTIPMDGEhfCFTRHEPVGVCGQIIPWNFP 190
Cdd:PRK09457  79 LAEVIARETGKPLWEA----ATEVtaminkiaisIQAYHERTG-----EKRSEMADGA--AVLRHRPHGVVAVFGPYNFP 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  191 LVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGH 270
Cdd:PRK09457 148 GHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGY 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  271 LI-QKAAGESNlKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIY-REFLERTVEKAKQR 348
Cdd:PRK09457 227 LLhRQFAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRL 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  349 KVGNPFElDTQ--QGPQVDKEQFERILGYIRLGQKEGAKLLCGGERLGERGFFIKPTVFgDVQDGMRIAKEEIFGPVQPL 426
Cdd:PRK09457 306 TVGRWDA-EPQpfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQV 383
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21312260  427 FKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTV-WVNTYNIVTCHTPFGGFKESGNGR 494
Cdd:PRK09457 384 VRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHR 452
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
40-512 4.39e-69

bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 239.33  E-value: 4.39e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260    40 KLFINNEWH----DAVSKKTFPTVNPT-TGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLV 114
Cdd:PRK11904  544 AAFLEKQWQagpiINGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPA---WSRTPVEERAAILERAADLL 620
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   115 ERDRVYLASLETLDNGKPFQESyvldLDEV---IKVYRYFAGWADKWHGKTIPM---DGEHfCFTRHEPVGV--CgqIIP 186
Cdd:PRK11904  621 EANRAELIALCVREAGKTLQDA----IAEVreaVDFCRYYAAQARRLFGAPEKLpgpTGES-NELRLHGRGVfvC--ISP 693
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   187 WNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGST 266
Cdd:PRK11904  694 WNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGST 773
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   267 EVGHLIQKAAGESNLKRVTL--ELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEK 344
Cdd:PRK11904  774 ETARIINRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGA 853
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   345 AKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEgAKLLCGGE--RLGERGFFIKPTVFgDVqDGMRIAKEEIFGP 422
Cdd:PRK11904  854 MAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPlpAGTENGHFVAPTAF-EI-DSISQLEREVFGP 930
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   423 VQPLFKFKK--IEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNI--VTCHTPFGGFKESGNGRELGe 498
Cdd:PRK11904  931 ILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIgaVVGVQPFGGQGLSGTGPKAG- 1009
                         490
                  ....*....|....*...
gi 21312260   499 dG----LRAYTEvKTVTI 512
Cdd:PRK11904 1010 -GphylLRFATE-KTVTV 1025
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
42-493 1.98e-67

bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 235.53  E-value: 1.98e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260    42 FINNEWH-------DAVSKKTFPTVNP-TTGEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADL 113
Cdd:PRK11905  548 FAAKTWHaapllagGDVDGGTRPVLNPaDHDDVVGTVTEASAEDVERALAAAQAAF---PEWSATPAAERAAILERAADL 624
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   114 VERDRVYLASLETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWhgktipmdgehFCFTRHEPVGVCGQIIPWNFPLVM 193
Cdd:PRK11905  625 MEAHMPELFALAVREAGKTLANA-IAEVREAVDFLRYYAAQARRL-----------LNGPGHKPLGPVVCISPWNFPLAI 692
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   194 QGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQ 273
Cdd:PRK11905  693 FTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQ 772
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   274 KAAGESNLKRVTL--ELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVG 351
Cdd:PRK11905  773 RTLAKRSGPPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIG 852
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   352 NPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLlcggERLG-----ERGFFIKPTVFgDVqDGMRIAKEEIFGPVqpL 426
Cdd:PRK11905  853 DPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPlpaetEKGTFVAPTLI-EI-DSISDLEREVFGPV--L 924
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21312260   427 ----FKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTyNI---VTCHTPFGGFKESGNG 493
Cdd:PRK11905  925 hvvrFKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNR-NIigaVVGVQPFGGEGLSGTG 997
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
22-511 1.05e-66

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 226.17  E-value: 1.05e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   22 STAAALPNPIPNpeicynklFINNEWHDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDAS 101
Cdd:PLN02419 105 STQPQMPPRVPN--------LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL---WRNTPIT 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  102 ERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWHGKTIP-MDGEHFCFTRHEPVGV 180
Cdd:PLN02419 174 TRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEYLPnVSNGVDTYSIREPLGV 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  181 CGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGaAIAQHMDVDKV 260
Cdd:PLN02419 253 CAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAV 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  261 AFTGSTEVG-HLIQKAAGESnlKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSR-TFVEESiyREFL 338
Cdd:PLN02419 332 SFVGSNTAGmHIYARAAAKG--KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA--KSWE 407
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  339 ERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL----GERGFFIKPTVFGDVQDGMRI 414
Cdd:PLN02419 408 DKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMEC 487
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  415 AKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNtyniVTCHTPFGGFKESGNGR 494
Cdd:PLN02419 488 YKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN----VPIPVPLPFFSFTGNKA 563
                        490       500
                 ....*....|....*....|....
gi 21312260  495 EL-------GEDGLRAYTEVKTVT 511
Cdd:PLN02419 564 SFagdlnfyGKAGVDFFTQIKLVT 587
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
57-497 2.49e-66

delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273518 [Multi-domain]  Cd Length: 500  Bit Score: 222.48  E-value: 2.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260    57 PTVNPTT-GEVIGHVAEGDRADVDLAVKAAREAFrlgSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQE 135
Cdd:TIGR01238  54 PVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAF---PTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   136 SyVLDLDEVIKVYRYFAGWADKwhgkTIPMDGehfcftrHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQ 215
Cdd:TIGR01238 131 A-IAEVREAVDFCRYYAKQVRD----VLGEFS-------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQ 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   216 TPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGESNLKRVTL--ELGGKSP 293
Cdd:TIGR01238 199 TSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNA 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   294 SIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERIL 373
Cdd:TIGR01238 279 MIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLL 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   374 GYI---RLGQKEGAKLLCGGERLGERGFFIKPTVFGdvQDGMRIAKEEIFGPVQPLFKFK--KIEEVIQRANNTRYGLAA 448
Cdd:TIGR01238 359 AHIehmSQTQKKIAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTM 436
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 21312260   449 AVFTRDLDKAIYFTQALQAGTVWVNTYNI--VTCHTPFGGFKESGNGRELG 497
Cdd:TIGR01238 437 GVHSRIETTYRWIEKHARVGNCYVNRNQVgaVVGVQPFGGQGLSGTGPKAG 487
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
42-512 6.57e-65

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 218.94  E-value: 6.57e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   42 FINNEWHdaVSKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLgspWRRMDASERGRLLNRLADLVERDRVYL 121
Cdd:PLN02315  24 YVGGEWR--ANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI---WMQVPAPKRGEIVRQIGDALRAKLDYL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  122 ASLETLDNGKPFQESyVLDLDEVIKVYRYFAGWADKWHGKTIPMD-GEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAP 200
Cdd:PLN02315  99 GRLVSLEMGKILAEG-IGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  201 ALATGNTVVMKVAEQTPLSAL----YLASLIKEAGFPPGVVNIITGyGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAA 276
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  277 gESNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFEL 356
Cdd:PLN02315 257 -NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  357 DTQQGP---QVDKEQFERILGYIRlgqKEGAKLLCGGERLGERGFFIKPTVFgDVQDGMRIAKEEIFGPVQPLFKFKKIE 433
Cdd:PLN02315 336 GTLLGPlhtPESKKNFEKGIEIIK---SQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLE 411
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  434 EVIQRANNTRYGLAAAVFTRDLDkaIYFT----QALQAGTVWVNT-YNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVK 508
Cdd:PLN02315 412 EAIEINNSVPQGLSSSIFTRNPE--TIFKwigpLGSDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRS 489

                 ....
gi 21312260  509 TVTI 512
Cdd:PLN02315 490 TCTI 493
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
76-510 6.52e-64

Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.


Pssm-ID: 143453 [Multi-domain]  Cd Length: 436  Bit Score: 214.39  E-value: 6.52e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  76 ADVDLAVKAAREAFRLGspwRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVLD----LDEVIKVYRYF 151
Cdd:cd07135   5 DEIDSIHSRLRATFRSG---KTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEvsgvKNDILHMLKNL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 152 AGWA-DKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEA 230
Cdd:cd07135  82 KKWAkDEKVKDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 231 gFPPGVVNIITGYGPTAGAAIAQHMdvDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCH 310
Cdd:cd07135 162 -LDPDAFQVVQGGVPETTALLEQKF--DKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELAAKRIL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 311 EALFFNMGQCCCAGSRTFVEESIYREFLERtVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIrlgQKEGAKLLCGG 390
Cdd:cd07135 238 WGKFGNAGQICVAPDYVLVDPSVYDEFVEE-LKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLL---DTTKGKVVIGG 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 391 ERlGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRD---LDKAIYFTQAlqA 467
Cdd:cd07135 314 EM-DEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDkseIDHILTRTRS--G 390
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 21312260 468 GTVWVNTYNIVTCHT-PFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07135 391 GVVINDTLIHVGVDNaPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
ALDH_YwdH-P39616 cd07136
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...
127-510 4.25e-62

Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.


Pssm-ID: 143454 [Multi-domain]  Cd Length: 449  Bit Score: 210.05  E-value: 4.25e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 127 LDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHG-KTIPMDGEHF---CFTRHEPVGVCGQIIPWNFP--LVMQgwKLAP 200
Cdd:cd07136  46 KDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKpKRVKTPLLNFpskSYIYYEPYGVVLIIAPWNYPfqLALA--PLIG 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 201 ALATGNTVVMKVAEQTPLSALYLASLIKEAgFPPGVVNIITGYGPTAGAAIAQHMDvdKVAFTGSTEVGHLIQKAAGEsN 280
Cdd:cd07136 124 AIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELLDQKFD--YIFFTGSVRVGKIVMEAAAK-H 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 281 LKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFElDTQQ 360
Cdd:cd07136 200 LTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLE-SPDY 278
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 361 GPQVDKEQFERILGYIrlgqkEGAKLLCGGERlGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRAN 440
Cdd:cd07136 279 GRIINEKHFDRLAGLL-----DNGKIVFGGNT-DRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIK 352
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21312260 441 NTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVN--TYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07136 353 SRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtIMHLANPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
ALDH_CALDH_CalB cd07133
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...
174-510 3.36e-60

Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.


Pssm-ID: 143451 [Multi-domain]  Cd Length: 434  Bit Score: 204.26  E-value: 3.36e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 174 RHEPVGVCGQIIPWNFPLVMQgwkLAP---ALATGNTVVMKVAEQTP-LSALyLASLIKEAgFPPGVVNIITGyGPTAGA 249
Cdd:cd07133  98 EYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPrTSAL-LAELLAEY-FDEDEVAVVTG-GADVAA 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 250 AIAqHMDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFV 329
Cdd:cd07133 172 AFS-SLPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLV 249
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 330 EESIYREFLERTVEKAKQR---KVGNPfeldtQQGPQVDKEQFERILGYIRLGQKEGAKLL-CG--GERLGERGfFIKPT 403
Cdd:cd07133 250 PEDKLEEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIeLNpaGEDFAATR-KLPPT 323
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 404 VFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVN-TYNIVTCHT 482
Cdd:cd07133 324 LVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINdTLLHVAQDD 403
                       330       340
                ....*....|....*....|....*....
gi 21312260 483 -PFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07133 404 lPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
ALDH_F4-17_P5CDH cd07123
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ...
64-491 1.65e-57

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.


Pssm-ID: 143441 [Multi-domain]  Cd Length: 522  Bit Score: 199.74  E-value: 1.65e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  64 GEVIGHVAEGDRADVDLAVKAAREAfrlGSPWRRMDASERGRLLNRLADLVE---RDRVYLASLetLDNGK-PFQEsyvl 139
Cdd:cd07123  57 AHVLATYHYADAALVEKAIEAALEA---RKEWARMPFEDRAAIFLKAADLLSgkyRYELNAATM--LGQGKnVWQA---- 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 140 DLD---EVIKVYRYFAGWADKWHGKTiPMDGEHFCFTR--HEPV-GVCGQIIPWNFPLVMQGWKLAPALaTGNTVVMKVA 213
Cdd:cd07123 128 EIDaacELIDFLRFNVKYAEELYAQQ-PLSSPAGVWNRleYRPLeGFVYAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPS 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 214 EQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGES-----NLKRVTLEL 288
Cdd:cd07123 206 DTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENldryrTYPRIVGET 285
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 289 GGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQ 368
Cdd:cd07123 286 GGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKA 365
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 369 FERILGYIRLGQKE-GAKLLCGGERLGERGFFIKPTVFgDVQDGM-RIAKEEIFGPVQPLFKF--KKIEEVIQRANNT-R 443
Cdd:cd07123 366 FDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVI-ETTDPKhKLMTEEIFGPVLTVYVYpdSDFEETLELVDTTsP 444
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 21312260 444 YGLAAAVFTRDlDKAIY-FTQALQ--AGTVWVN---TYNIVTCHtPFGGFKESG 491
Cdd:cd07123 445 YALTGAIFAQD-RKAIReATDALRnaAGNFYINdkpTGAVVGQQ-PFGGARASG 496
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
76-513 3.44e-53

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 187.16  E-value: 3.44e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   76 ADVDLAVKAAREAFRLGS----PWRRMdasergRLLNRLADLVERDRVYLASLEtLDNGKPFQESYVLDLDEVIKVYRYF 151
Cdd:PTZ00381   7 EIIPPIVKKLKESFLTGKtrplEFRKQ------QLRNLLRMLEENKQEFSEAVH-KDLGRHPFETKMTEVLLTVAEIEHL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  152 AGWADKWhGKTIPMDGE-HF----CFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASL 226
Cdd:PTZ00381  80 LKHLDEY-LKPEKVDTVgVFgpgkSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  227 IKEAgFPPGVVNIITGYGPTAGAAIAQHMDVdkVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAV 306
Cdd:PTZ00381 159 LTKY-LDPSYVRVIEGGVEVTTELLKEPFDH--IFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  307 DQCHEALFFNMGQCCCAGSRTFVEESIYREFLErTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIrlgQKEGAKL 386
Cdd:PTZ00381 235 RRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIE-ALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELI---KDHGGKV 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  387 LCGGErLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQ 466
Cdd:PTZ00381 311 VYGGE-VDIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTS 389
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 21312260  467 AGTVWVN--TYNIVTCHTPFGGFKESGNGRELGEDGLRAYTEVKTVTIK 513
Cdd:PTZ00381 390 SGAVVINdcVFHLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNK 438
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
57-493 6.01e-52

trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 190.57  E-value: 6.01e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260    57 PTVNP-TTGEVIGHVAEGDRADVDLAVKAAREAfrlGSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQE 135
Cdd:PRK11809  662 PVINPaDPRDIVGYVREATPAEVEQALESAVNA---APIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSN 738
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   136 SyVLDLDEVIKVYRYFAGWADkwhgktipmdgEHFCFTRHEPVG--VCgqIIPWNFPLVMQGWKLAPALATGNTVVMKVA 213
Cdd:PRK11809  739 A-IAEVREAVDFLRYYAGQVR-----------DDFDNDTHRPLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPA 804
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   214 EQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKA-AG--ESNLKRVTL--EL 288
Cdd:PRK11809  805 EQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNlAGrlDPQGRPIPLiaET 884
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   289 GGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRTFVEESIyrefLERTVEKAK----QRKVGNPFELDTQQGPQV 364
Cdd:PRK11809  885 GGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDV----ADRTLKMLRgamaECRMGNPDRLSTDIGPVI 960
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   365 DKEQFERILGYIRLGQKEGAK---LLCGGERLGERGFFIKPTV--FGDVQDgmriAKEEIFGPVQPLFKFKK--IEEVIQ 437
Cdd:PRK11809  961 DAEAKANIERHIQAMRAKGRPvfqAARENSEDWQSGTFVPPTLieLDSFDE----LKREVFGPVLHVVRYNRnqLDELIE 1036
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   438 RANNTRYGLAAAVFTRdLDKAI-YFTQALQAGTVWVNTyNIVTCHT---PFGGFKESGNG 493
Cdd:PRK11809 1037 QINASGYGLTLGVHTR-IDETIaQVTGSAHVGNLYVNR-NMVGAVVgvqPFGGEGLSGTG 1094
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
81-513 7.25e-48

Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.


Pssm-ID: 143450 [Multi-domain]  Cd Length: 443  Bit Score: 171.64  E-value: 7.25e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  81 AVKAAREAFRLGspwRRMDASERGRLLNRLADLV-ERDRVYLASLEtLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWH 159
Cdd:cd07132   3 AVRRAREAFSSG---KTRPLEFRIQQLEALLRMLeENEDEIVEALA-KDLRKPKFEAVLSEILLVKNEIKYAISNLPEWM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 160 -----GKTIP--MDGehfCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLI----- 227
Cdd:cd07132  79 kpepvKKNLAtlLDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyld 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 228 KEAgFPpgvvnIITGYGPTAGAAIAQHMDvdKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVD 307
Cdd:cd07132 156 KEC-YP-----VVLGGVEETTELLKQRFD--YIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSCDIDVAAR 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 308 QCHEALFFNMGQCCCAGSRTFVEESIYREFLERtVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIrlgqkEGAKLL 387
Cdd:cd07132 227 RIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEA-LKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVA 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 388 CGGE-RLGERgfFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQ 466
Cdd:cd07132 301 IGGQtDEKER--YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTS 378
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 21312260 467 AGTVWVN-TYNIVTCHT-PFGGFKESGNGRELGEDGLRAYTEVKTVTIK 513
Cdd:cd07132 379 SGGVCVNdTIMHYTLDSlPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
ALDH_F3FHI cd07137
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...
82-510 5.83e-46

Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.


Pssm-ID: 143455 [Multi-domain]  Cd Length: 432  Bit Score: 166.43  E-value: 5.83e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  82 VKAAREAFRLGspwRRMDASERGRLLNRLADLV-ERDRVYLASLETlDNGKPFQESYVLDLDEVIKVYRYFAGWADKW-- 158
Cdd:cd07137   5 VRELRETFRSG---RTRSAEWRKSQLKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRDEVSVLVSSCKLAIKELKKWma 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 159 --HGK----TIPMDGEHFCftrhEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAgF 232
Cdd:cd07137  81 peKVKtpltTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-L 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 233 PPGVVNIITGyGPTAGAAIAQHmDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEA 312
Cdd:cd07137 156 DTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGG 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 313 LF-FNMGQCCCAGSRTFVEESIYREFLERTVEKAKQRKVGNPFELDTQQgPQVDKEQFERILGYIRlGQKEGAKLLCGGE 391
Cdd:cd07137 233 KWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLS-RIVNSHHFQRLSRLLD-DPSVADKIVHGGE 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 392 RlGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVW 471
Cdd:cd07137 311 R-DEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVT 389
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 21312260 472 VNTYNI-VTCHT-PFGGFKESGNGRELGEDGLRAYTEVKTV 510
Cdd:cd07137 390 FNDTVVqYAIDTlPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
PLN02203 PLN02203
aldehyde dehydrogenase
86-511 4.47e-36

aldehyde dehydrogenase


Pssm-ID: 165847 [Multi-domain]  Cd Length: 484  Bit Score: 139.86  E-value: 4.47e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   86 REAFRLGS----PWRRmdaSERGRLLNRLADlvERDRVYLASLETLdnGKPFQESYVLDLDEVIKVYRYFAGWADKW--- 158
Cdd:PLN02203  16 RETYESGRtrslEWRK---SQLKGLLRLLKD--NEEAIFKALHQDL--GKHRVEAYRDEVGVLTKSANLALSNLKKWmap 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  159 -HGK----TIPMDGEHFcftrHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKeAGFP 233
Cdd:PLN02203  89 kKAKlplvAFPATAEVV----PEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIP-KYLD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  234 PGVVNIITGyGPTAGAAIAQHmDVDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIV---LADADMEHAVDQCH 310
Cdd:PLN02203 164 SKAVKVIEG-GPAVGEQLLQH-KWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdslSSSRDTKVAVNRIV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  311 EALFFN-MGQCCCAGSRTFVEE---SIYREFLERTVekaKQRKVGNPFELDTqQGPQVDKEQFERILGYirLGQKEGAKL 386
Cdd:PLN02203 241 GGKWGScAGQACIAIDYVLVEErfaPILIELLKSTI---KKFFGENPRESKS-MARILNKKHFQRLSNL--LKDPRVAAS 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  387 LCGGERLGERGFFIKPTVFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRD--LDKAIyfTQA 464
Cdd:PLN02203 315 IVHGGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNekLKRRI--LSE 392
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 21312260  465 LQAGTVWVNTYNI-VTCHT-PFGGFKESGNGRELGEDGLRAYTEVKTVT 511
Cdd:PLN02203 393 TSSGSVTFNDAIIqYACDSlPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
81-503 8.43e-34

ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.


Pssm-ID: 143403 [Multi-domain]  Cd Length: 442  Bit Score: 132.75  E-value: 8.43e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  81 AVKAAREAfrlGSPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQESYVLDLDEVIKVYRYFAGWADKWHG 160
Cdd:cd07084   4 ALLAADIS---TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 161 KTIPMDGEHFCFTRHE---PVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAG-FPPGV 236
Cdd:cd07084  81 EPGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPED 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 237 VNIITGYGPTaGAAIAQHMDVDKVAFTGSTEVGhliQKAAGESNLKRVTLELGGKSPSIVLADADMEHAV-DQCHEALFF 315
Cdd:cd07084 161 VTLINGDGKT-MQALLLHPNPKMVLFTGSSRVA---EKLALDAKQARIYLELAGFNWKVLGPDAQAVDYVaWQCVQDMTA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 316 NMGQCCCAGSRTFVEESIY-REFLERTVEKAKQRKVGnpfelDTQQGPqvdkEQFERILGYI-RLGQKEGAKLLCGGERL 393
Cdd:cd07084 237 CSGQKCTAQSMLFVPENWSkTPLVEKLKALLARRKLE-----DLLLGP----VQTFTTLAMIaHMENLLGSVLLFSGKEL 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 394 GER------GFFIKPTVFGDVQDGMRIAK---EEIFGPVQPLFKFKKIEE--VIQRANNTRYGLAAAVFTRDLDkaiyFT 462
Cdd:cd07084 308 KNHsipsiyGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPI----FL 383
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 21312260 463 QALqAGTVWVN--TYNIVTCHTPF-------GGFKESGNGRELGedGLRA 503
Cdd:cd07084 384 QEL-IGNLWVAgrTYAILRGRTGVapnqnhgGGPAADPRGAGIG--GPEA 430
PRK11903 PRK11903
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
42-503 4.14e-31

3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;


Pssm-ID: 237016 [Multi-domain]  Cd Length: 521  Bit Score: 126.36  E-value: 4.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260   42 FINNEWHDAVSKKTfPTVNPTTGEVIGHV-AEGdrADVDLAVKAAREafRLGSPWRRMDASERGRLLNRLADLVERDRVY 120
Cdd:PRK11903   8 YVAGRWQAGSGAGT-PLFDPVTGEELVRVsATG--LDLAAAFAFARE--QGGAALRALTYAQRAALLAAIVKVLQANRDA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  121 LASLETLDNGKPFQESYVlDLDEVIKVYRYFAGWADKWH-------------GKTIPMDGEHFCFTRHepvGVCGQIIPW 187
Cdd:PRK11903  83 YYDIATANSGTTRNDSAV-DIDGGIFTLGYYAKLGAALGdarllrdgeavqlGKDPAFQGQHVLVPTR---GVALFINAF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  188 NFPlvmqGW----KLAPALATGNTVVMKVAEQTPLSALYLASLIKEAG-FPPGVVNIITGygpTAGAAIAQHMDVDKVAF 262
Cdd:PRK11903 159 NFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG---SSAGLLDHLQPFDVVSF 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  263 TGSTEVGHLIQK-AAGESNLKRVTLELGGKSPSIVLADAD-----MEHAVDQCHEALFFNMGQCCCAGSRTFVEESIYRE 336
Cdd:PRK11903 232 TGSAETAAVLRShPAVVQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDA 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  337 FLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERIL-GYIRLgqKEGAKLLCGGERLG------ERGFFIKPTVFG--D 407
Cdd:PRK11903 312 VAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRaGLAAL--RAQAEVLFDGGGFAlvdadpAVAACVGPTLLGasD 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  408 VQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQA--GTVWVNTYNIVTCHT--- 482
Cdd:PRK11903 390 PDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADshGRVHVISPDVAALHTghg 469
                        490       500
                 ....*....|....*....|....*..
gi 21312260  483 ---P---FGGFKESGNGRELGedGLRA 503
Cdd:PRK11903 470 nvmPqslHGGPGRAGGGEELG--GLRA 494
PLN02174 PLN02174
aldehyde dehydrogenase family 3 member H1
176-510 1.62e-30

aldehyde dehydrogenase family 3 member H1


Pssm-ID: 177831  Cd Length: 484  Bit Score: 124.00  E-value: 1.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  176 EPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIkEAGFPPGVVNIITGYGPTAGAAIAQHM 255
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQKW 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  256 dvDKVAFTGSTEVGHLIQKAAGEsNLKRVTLELGGKSPSIVLADADMEHAVDQCHEALF-FNMGQCCCAGSRTFVEESIY 334
Cdd:PLN02174 190 --DKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYA 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  335 REFLERTVEKAKQRKVGNPFElDTQQGPQVDKEQFERILGYirLGQKEGA-KLLCGGERLGErGFFIKPTVFGDVQDGMR 413
Cdd:PLN02174 267 PKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKL--LDEKEVSdKIVYGGEKDRE-NLKIAPTILLDVPLDSL 342
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  414 IAKEEIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQAGTVWVNTYNI-VTCHT-PFGGFKESG 491
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVhLALHTlPFGGVGESG 422
                        330
                 ....*....|....*....
gi 21312260  492 NGRELGEDGLRAYTEVKTV 510
Cdd:PLN02174 423 MGAYHGKFSFDAFSHKKAV 441
ALDH_MaoC-N cd07128
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ...
42-503 3.02e-29

N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.


Pssm-ID: 143446 [Multi-domain]  Cd Length: 513  Bit Score: 120.84  E-value: 3.02e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  42 FINNEWHdAVSKKTFPTVNPTTGEVIGHVAeGDRADVDLAVKAAREAfrlGSP-WRRMDASERGRLLNRLADLV--ERDR 118
Cdd:cd07128   4 YVAGQWH-AGTGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYAREK---GGPaLRALTFHERAAMLKALAKYLmeRKED 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 119 VYLASLETldnGKPFQESYVlDLDEVIKVYRYFAGWA------DKWH--GKTIPMD------GEHFCFTRHepvGVCGQI 184
Cdd:cd07128  79 LYALSAAT---GATRRDSWI-DIDGGIGTLFAYASLGrrelpnAHFLveGDVEPLSkdgtfvGQHILTPRR---GVAVHI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 185 IPWNFPLvmqgW----KLAPALATGNTVVMKVAEQTPLSALYLASLIKEAG-FPPGVVNIITGygpTAGAAIAQHMDVDK 259
Cdd:cd07128 152 NAFNFPV----WgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG---SVGDLLDHLGEQDV 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 260 VAFTGSTEVG-------HLIQKAAgesnlkRVTLELGGKSPSIVLADA--DMEhAVDQCHEALFFNM----GQCCCAGSR 326
Cdd:cd07128 225 VAFTGSAATAaklrahpNIVARSI------RFNAEADSLNAAILGPDAtpGTP-EFDLFVKEVAREMtvkaGQKCTAIRR 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 327 TFVEESIYREFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERILGYIRLGQKEGAKLLCGGERL------GERGFFI 400
Cdd:cd07128 298 AFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFevvgadAEKGAFF 377
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 401 KPTVF-GDVQDGMRIAKE-EIFGPVQPLFKFKKIEEVIQRANNTRYGLAAAVFTRDLDKAIYFTQALQA--GTVWVNTYN 476
Cdd:cd07128 378 PPTLLlCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVLNRD 457
                       490       500       510
                ....*....|....*....|....*....|....*.
gi 21312260 477 IV---TCH-TPF-----GGFKESGNGRELGedGLRA 503
Cdd:cd07128 458 SAkesTGHgSPLpqlvhGGPGRAGGGEELG--GLRG 491
ALDH_F12_P5CDH cd07126
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ...
42-475 4.21e-19

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.


Pssm-ID: 143444  Cd Length: 489  Bit Score: 89.86  E-value: 4.21e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  42 FINNEWHDAvsKKTFPTVNPTTGEVIGHVAEGDRADVDLAVKAAREAFRLG--SPWRrmdASER----GRLLNRLADLVE 115
Cdd:cd07126   2 LVAGKWKGA--SNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGlhNPLK---NPERyllyGDVSHRVAHELR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 116 RDRV--YLASLetLDNGKPfqESYVLDLDEVIKVYRY---FAGWADKWHGKTIPMDGEHFCFTRHE---PVGVCGQIIPW 187
Cdd:cd07126  77 KPEVedFFARL--IQRVAP--KSDAQALGEVVVTRKFlenFAGDQVRFLARSFNVPGDHQGQQSSGyrwPYGPVAIITPF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 188 NFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQhMDVDKVAFTGSTE 267
Cdd:cd07126 153 NFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE-ANPRMTLFTGSSK 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 268 VGHliqKAAGESNlKRVTLELGGKSPSIVLAD-ADMEHAVDQCHEALFFNMGQCCCAGSRTFVEES-IYREFLERTVEKA 345
Cdd:cd07126 232 VAE---RLALELH-GKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKALA 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 346 KQRKVGnpfelDTQQGPqVDKEQFERILGYI-RLGQKEGAKLLCGGERLGERGffiKPTVFGDVQ--------------D 410
Cdd:cd07126 308 EQRKLE-----DLTIGP-VLTWTTERILDHVdKLLAIPGAKVLFGGKPLTNHS---IPSIYGAYEptavfvpleeiaieE 378
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21312260 411 GMRIAKEEIFGPVQPLFKFKKIEE--VIQRANNTRYGLAAAVFTRDldkaIYFTQALQAGTVWVNTY 475
Cdd:cd07126 379 NFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSND----IRFLQEVLANTVNGTTY 441
ALDH_KGSADH cd07129
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ...
78-321 2.64e-16

Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.


Pssm-ID: 143447 [Multi-domain]  Cd Length: 454  Bit Score: 81.05  E-value: 2.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  78 VDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDR---VYLASLET-LDNGKPFQEsyvldLDEVIKVYRYFAG 153
Cdd:cd07129   1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEALGdelVARAHAETgLPEARLQGE-----LGRTTGQLRLFAD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 154 WADK--WHGKTI-PMDGEHFCFTRHE---------PVGVCGqiiPWNFPL---VMQGwKLAPALATGNTVVMKVAEQTP- 217
Cdd:cd07129  73 LVREgsWLDARIdPADPDRQPLPRPDlrrmlvplgPVAVFG---ASNFPLafsVAGG-DTASALAAGCPVVVKAHPAHPg 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 218 LSALyLASLI----KEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAgesnLKR-----VTLEL 288
Cdd:cd07129 149 TSEL-VARAIraalRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAA----AARpepipFYAEL 223
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21312260 289 GGKSPSIVLADADMEHA---VDQCHEALFFNMGQCC 321
Cdd:cd07129 224 GSVNPVFILPGALAERGeaiAQGFVGSLTLGAGQFC 259
ALDH-like cd07077
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ...
78-474 2.75e-14

NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143396 [Multi-domain]  Cd Length: 397  Bit Score: 74.57  E-value: 2.75e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  78 VDLAVKAAREA-FRLGSPWRRMDASERGRLLNRLAdlverdrvylasletldngKPFQESYVLDLDEVIKVY---RYFAG 153
Cdd:cd07077  18 RDLIINAIANAlYDTRQRLASEAVSERGAYIRSLI-------------------ANWIAMMGCSESKLYKNIdteRGITA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 154 WADKWHGKTIPMDGEhfCFTRHEPVGVCGQIIPWNFPL-VMQgwKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAgF 232
Cdd:cd07077  79 SVGHIQDVLLPDNGE--TYVRAFPIGVTMHILPSTNPLsGIT--SALRGIATRNQCIFRPHPSAPFTNRALALLFQAA-D 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 233 PPGVVNIITGYGPTAGAAIAQ----HMDVDKVAFTGSTEVGHLIQKAageSNLKRVTLELGGKSPSIVLADADMEHAVDQ 308
Cdd:cd07077 154 AAHGPKILVLYVPHPSDELAEellsHPKIDLIVATGGRDAVDAAVKH---SPHIPVIGFGAGNSPVVVDETADEERASGS 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 309 CHEALFFNMGQCccagsrtFVEESIYrefLERTVEKAKqrkvgnpfeldtqqgpqvdKEQFERILGYIRLGQKEGAKLLc 388
Cdd:cd07077 231 VHDSKFFDQNAC-------ASEQNLY---VVDDVLDPL-------------------YEEFKLKLVVEGLKVPQETKPL- 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 389 ggerlgergffikptvFGDVQDGMRIAKEEIFGPVQPLFKFKKIEEVIQRANNTRY----GLAAAVFTRDLDKAIYFTQA 464
Cdd:cd07077 281 ----------------SKETTPSFDDEALESMTPLECQFRVLDVISAVENAWMIIEsgggPHTRCVYTHKINKVDDFVQY 344
                       410
                ....*....|
gi 21312260 465 LQAGTVWVNT 474
Cdd:cd07077 345 IDTASFYPNE 354
ALDH_F20_ACDH_EutE-like cd07081
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ...
78-474 1.74e-05

Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.


Pssm-ID: 143400 [Multi-domain]  Cd Length: 439  Bit Score: 47.26  E-value: 1.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260  78 VDLAVKAAREAFRlgsPWRRMDASERGRLLNRLADLVERDRVYLASLETLDNGKPFQEsyvldlDEVIKvyRYFAG---- 153
Cdd:cd07081   1 LDDAVAAAKVAQQ---GLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVE------DKVIK--NHFAAeyiy 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 154 --WADKWHGKTIPMDGEHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVM----KVAEQTPLSALYLASLI 227
Cdd:cd07081  70 nvYKDEKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFsphpRAKKVTQRAATLLLQAA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 228 KEAGFPPGVVNIITGYGPTAGAAIAQHMDVDKVAFTGstevGHLIQKAAGESNlKRVTLELGGKSPSIVLADADMEHAVD 307
Cdd:cd07081 150 VAAGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSG-KPAIGVGAGNTPVVIDETADIKRAVQ 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 308 QCHEALFFNMGQCCCAGSRTFVEESIYREFLERTVE------KAKQRKVGNPFEL-DTQQGPQVDKEQFERILGYIRLGQ 380
Cdd:cd07081 225 SIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGqgayklTAEELQQVQPVILkNGDVNRDIVGQDAYKIAAAAGLKV 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 381 KEGAKLLCGG-ERLGERGFFIkptvfgdvqdgmriakEEIFGPVQPLFKFKKIEEVIQRA----NNTRYGLAAAVFTRDL 455
Cdd:cd07081 305 PQETRILIGEvTSLAEHEPFA----------------HEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNI 368
                       410       420
                ....*....|....*....|..
gi 21312260 456 ---DKAIYFTQALQAGTVWVNT 474
Cdd:cd07081 369 kaiENMNQFANAMKTSRFVKNG 390
ALDH_PAD-PaaZ cd07127
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ...
181-329 8.65e-05

Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.


Pssm-ID: 143445  Cd Length: 549  Bit Score: 45.16  E-value: 8.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 181 CGQIIPWNfplvmqGWK-LAPALATGNTVVMKvaeQTPLSALYLASLIK-------EAGFPPGVVNIITgygPTAGAAIA 252
Cdd:cd07127 202 CSTFPTWN------GYPgLFASLATGNPVIVK---PHPAAILPLAITVQvarevlaEAGFDPNLVTLAA---DTPEEPIA 269
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312260 253 QHM----DVDKVAFTGSTEVG-HLIQKAAGesnlKRVTLELGGKSPSIVLADADMEHAVDQCHEALFFNMGQCCCAGSRT 327
Cdd:cd07127 270 QTLatrpEVRIIDFTGSNAFGdWLEANARQ----AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNI 345

                ..
gi 21312260 328 FV 329
Cdd:cd07127 346 YV 347
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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