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Conserved domains on  [gi|6324950|ref|NP_015019|]
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Protein Classification

aldehyde dehydrogenase family protein (domain architecture ID 10162896)

aldehyde dehydrogenase family protein similar to NAD or NADP or NAD(P)-dependent aldehyde dehydrogenase that performs the conversion of acetaldehyde to acetate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
42-514 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: 880.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   42 EQPTGLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNGIDPIDRGKALYRLAELIEQ 121
Cdd:cd07091   1 EQPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  122 DKDVIASIETLDNGKAIS-SSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAW 200
Cdd:cd07091  81 DRDELAALESLDNGKPLEeSAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  201 KIAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSA 280
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  281 AA-GLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDE 359
Cdd:cd07091 241 AKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  360 STFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVI 439
Cdd:cd07091 321 DTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324950  440 NMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAVR 514
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475
 
Name Accession Description Interval E-value
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
42-514 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: 880.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   42 EQPTGLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNGIDPIDRGKALYRLAELIEQ 121
Cdd:cd07091   1 EQPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  122 DKDVIASIETLDNGKAIS-SSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAW 200
Cdd:cd07091  81 DRDELAALESLDNGKPLEeSAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  201 KIAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSA 280
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  281 AA-GLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDE 359
Cdd:cd07091 241 AKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  360 STFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVI 439
Cdd:cd07091 321 DTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324950  440 NMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAVR 514
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
53-513 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: 395119  Cd Length: 458  Bit Score: 671.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950     53 FVPSkQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVIASIETL 132
Cdd:pfam00171   1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAAREAFP--AWRKTPAAERAAILRKAADLLEERRDELAELETL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    133 DNGKAISSSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTV 212
Cdd:pfam00171  78 ETGKPLAEARGEVDRAIDTLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    213 VLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELG 292
Cdd:pfam00171 158 VLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGDALVEHPDVRKVSFTGSTAVGRHIAEAAAKNLKRVTLELG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    293 GKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQL 372
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEGIVFGAFGNAGQVCTAASRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    373 NKILKYVDIGKNEGATLITGGERLGsKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAG 452
Cdd:pfam00171 318 ERVLSYVEDAKEEGAKLLTGGELLD-NGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAG 396
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324950    453 IHTSNINTALKVADRVNAGTVWINTYNDFHH-AVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:pfam00171 397 VFTNDLERALRVAERLEAGMVWINDYTTGDAdGQPFGGFKQSGFGREGGPYGLEEYTEVKTV 458
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and ...
45-519 0e+00

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


Pssm-ID: 223944  Cd Length: 472  Bit Score: 595.43  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   45 TGLFINNKFVPSkqNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKD 124
Cdd:COG1012   1 YKLLIDGEWVDG--ASTIEVINPATGEVIATVPAATAEDVDAAVAAARAAFE--AWSRLSAEERAAILRRIADLLEARAE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  125 VIASIETLDNGKAISSSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAP 204
Cdd:COG1012  77 ELAALITLETGKPISEARGEIARAADFIRYYAEEARRLEGETIPTDKGSKALVRREPLGVVGAITPWNFPLALAAWKLAP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  205 ALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGL 284
Cdd:COG1012 157 ALAAGNTVVLKPSEQTPLSALALAELAAEAGLPAGVLNVVTGGGAEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAANL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  285 KKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQG 364
Cdd:COG1012 237 KPVTLELGGKSPAIVLEDADLDAAVDAAVFGAFFNAGQRCTAASRLIVHESVYDEFVERLVARAASLKVGDPLDPSTDLG 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  365 AQTSQMQLNKILKYVDIGKNEGATLITGGERLGskGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMAND 444
Cdd:COG1012 317 PLISEEQLDRVEGYIEDAVAEGARLLAGGKRPG--GYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIELAND 394
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324950  445 SEYGLAAGIHTSNINTALKVADRVNAGTVWINTYN--DFHHAVPFGGFNASGLGREMSVDALQNYLQVKAVRAKLDE 519
Cdd:COG1012 395 TEYGLAAAIFTRDLARAFRVARRLEAGMVGINDYTggADIAYLPFGGVKQSGLGREGGKYGLEEFTEVKTVTIKLGP 471
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
32-513 0e+00

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259  Cd Length: 538  Bit Score: 574.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    32 PIKLPNGLEYEQptgLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNGIDPIDRGKA 111
Cdd:PLN02466  48 PITPPVQVSYTQ---LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRI 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   112 LYRLAELIEQDKDVIASIETLDNGKAISSSRG-DVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIP 190
Cdd:PLN02466 125 LLRFADLLEKHNDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIP 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   191 WNFPLLMWAWKIAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGST 270
Cdd:PLN02466 205 WNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGST 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   271 ATGRHIYQSAA-AGLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASE 349
Cdd:PLN02466 285 DTGKIVLELAAkSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARAL 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   350 SIKVGDPFDESTFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTV 429
Cdd:PLN02466 365 KRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSI 444
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   430 TKFKSADEVINMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQ 509
Cdd:PLN02466 445 LKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQ 524

                 ....
gi 6324950   510 VKAV 513
Cdd:PLN02466 525 VKAV 528
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
48-511 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  Cd Length: 467  Bit Score: 520.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950     48 FINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFsnGSWNGIDPIDRGKALYRLAELIEQDKDVIA 127
Cdd:TIGR01804   1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    128 SIETLDNGKAIS-SSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPAL 206
Cdd:TIGR01804  79 KLETLDTGKTLQeTIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPAL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    207 VTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKK 286
Cdd:TIGR01804 159 AAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKH 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    287 VTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQ 366
Cdd:TIGR01804 239 VTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    367 TSQMQLNKILKYVDIGKNEGATLITGGERLG----SKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMA 442
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGRPEnvglQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324950    443 NDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVK 511
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
 
Name Accession Description Interval E-value
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
42-514 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: 880.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   42 EQPTGLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNGIDPIDRGKALYRLAELIEQ 121
Cdd:cd07091   1 EQPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  122 DKDVIASIETLDNGKAIS-SSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAW 200
Cdd:cd07091  81 DRDELAALESLDNGKPLEeSAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  201 KIAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSA 280
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  281 AA-GLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDE 359
Cdd:cd07091 241 AKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  360 STFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVI 439
Cdd:cd07091 321 DTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324950  440 NMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAVR 514
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
41-517 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: 675.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   41 YEQPTGLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFsNGSWN-GIDPIDRGKALYRLAELI 119
Cdd:cd07143   3 YEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAF-ETDWGlKVSGSKRGRCLSKLADLM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  120 EQDKDVIASIETLDNGKAI-SSSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMW 198
Cdd:cd07143  82 ERNLDYLASIEALDNGKTFgTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMC 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  199 AWKIAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQ 278
Cdd:cd07143 162 AWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVME 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  279 SAA-AGLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPF 357
Cdd:cd07143 242 AAAkSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPF 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  358 DESTFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADE 437
Cdd:cd07143 322 AEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEE 401
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  438 VINMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAVRAKL 517
Cdd:cd07143 402 AIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
53-513 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: 395119  Cd Length: 458  Bit Score: 671.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950     53 FVPSkQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVIASIETL 132
Cdd:pfam00171   1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAAREAFP--AWRKTPAAERAAILRKAADLLEERRDELAELETL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    133 DNGKAISSSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTV 212
Cdd:pfam00171  78 ETGKPLAEARGEVDRAIDTLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    213 VLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELG 292
Cdd:pfam00171 158 VLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGDALVEHPDVRKVSFTGSTAVGRHIAEAAAKNLKRVTLELG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    293 GKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQL 372
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEGIVFGAFGNAGQVCTAASRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    373 NKILKYVDIGKNEGATLITGGERLGsKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAG 452
Cdd:pfam00171 318 ERVLSYVEDAKEEGAKLLTGGELLD-NGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAG 396
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324950    453 IHTSNINTALKVADRVNAGTVWINTYNDFHH-AVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:pfam00171 397 VFTNDLERALRVAERLEAGMVWINDYTTGDAdGQPFGGFKQSGFGREGGPYGLEEYTEVKTV 458
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
45-516 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: 668.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   45 TGLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGS-WNGIDPIDRGKALYRLAELIEQDK 123
Cdd:cd07141   7 TKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSpWRTMDASERGRLLNKLADLIERDR 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  124 DVIASIETLDNGKAIS-SSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKI 202
Cdd:cd07141  87 AYLASLETLDNGKPFSkSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKL 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  203 APALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAA 282
Cdd:cd07141 167 APALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGK 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  283 -GLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDEST 361
Cdd:cd07141 247 sNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKT 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  362 FQGAQTSQMQLNKILKYVDIGKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINM 441
Cdd:cd07141 327 EQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIER 406
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324950  442 ANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAVRAK 516
Cdd:cd07141 407 ANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
38-513 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: 657.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   38 GLEYEQPTGLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNgSWNGIDPIDRGKALYRLAE 117
Cdd:cd07144   1 GKSYDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDKLAD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  118 LIEQDKDVIASIETLDNGKAISS-SRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLL 196
Cdd:cd07144  80 LVEKNRDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  197 MWAWKIAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHI 276
Cdd:cd07144 160 MAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLV 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  277 YQSAAAGLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKA-ASESIKVGD 355
Cdd:cd07144 240 MKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEhVKQNYKVGS 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  356 PFDESTFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERLG---SKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKF 432
Cdd:cd07144 320 PFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPeglGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKF 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  433 KSADEVINMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKA 512
Cdd:cd07144 400 KTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKA 479

                .
gi 6324950  513 V 513
Cdd:cd07144 480 V 480
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
64-513 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  Cd Length: 457  Bit Score: 613.79  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   64 VINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSRG 143
Cdd:cd07114   1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  144 DVDLVINYLKSSAGFADKIDGRMIDTGR-THFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAESTPL 222
Cdd:cd07114  81 QVRYLAEWYRYYAGLADKIEGAVIPVDKgDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  223 SALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIVFAD 302
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  303 AELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKILKYVDIG 382
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARA 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  383 KNEGATLITGGERLG----SKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTSNI 458
Cdd:cd07114 321 REEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6324950  459 NTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07114 401 ARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
43-513 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: 608.72  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   43 QPTGLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNGIDPIDRGKALYRLAELIEQD 122
Cdd:cd07142   2 KHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  123 KDVIASIETLDNGKAISSSR-GDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWK 201
Cdd:cd07142  82 ADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  202 IAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAA 281
Cdd:cd07142 162 VGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  282 AG-LKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDES 360
Cdd:cd07142 242 KSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKG 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  361 TFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVIN 440
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324950  441 MANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
85-515 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: 596.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   85 EEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSRGDVDLVINYLKSSAGFADKIDG 164
Cdd:cd07078   1 DAAVAAARAAFK--AWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  165 RMIDTGRT-HFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINI 243
Cdd:cd07078  79 EVIPSPDPgELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  244 VSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEV 323
Cdd:cd07078 159 VTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  324 CCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERL-GSKGYF 402
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLeGGKGYF 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  403 IKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFH 482
Cdd:cd07078 319 VPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGA 398
                       410       420       430
                ....*....|....*....|....*....|....
gi 6324950  483 HA-VPFGGFNASGLGREMSVDALQNYLQVKAVRA 515
Cdd:cd07078 399 EPsAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and ...
45-519 0e+00

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


Pssm-ID: 223944  Cd Length: 472  Bit Score: 595.43  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   45 TGLFINNKFVPSkqNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKD 124
Cdd:COG1012   1 YKLLIDGEWVDG--ASTIEVINPATGEVIATVPAATAEDVDAAVAAARAAFE--AWSRLSAEERAAILRRIADLLEARAE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  125 VIASIETLDNGKAISSSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAP 204
Cdd:COG1012  77 ELAALITLETGKPISEARGEIARAADFIRYYAEEARRLEGETIPTDKGSKALVRREPLGVVGAITPWNFPLALAAWKLAP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  205 ALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGL 284
Cdd:COG1012 157 ALAAGNTVVLKPSEQTPLSALALAELAAEAGLPAGVLNVVTGGGAEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAANL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  285 KKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQG 364
Cdd:COG1012 237 KPVTLELGGKSPAIVLEDADLDAAVDAAVFGAFFNAGQRCTAASRLIVHESVYDEFVERLVARAASLKVGDPLDPSTDLG 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  365 AQTSQMQLNKILKYVDIGKNEGATLITGGERLGskGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMAND 444
Cdd:COG1012 317 PLISEEQLDRVEGYIEDAVAEGARLLAGGKRPG--GYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIELAND 394
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324950  445 SEYGLAAGIHTSNINTALKVADRVNAGTVWINTYN--DFHHAVPFGGFNASGLGREMSVDALQNYLQVKAVRAKLDE 519
Cdd:COG1012 395 TEYGLAAAIFTRDLARAFRVARRLEAGMVGINDYTggADIAYLPFGGVKQSGLGREGGKYGLEEFTEVKTVTIKLGP 471
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
48-519 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: 593.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   48 FINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNGIDPIDRGKALYRLAELIEQDKDVIA 127
Cdd:cd07119   1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  128 SIETLDNGKAISSSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALV 207
Cdd:cd07119  81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  208 TGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKV 287
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  288 TLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQT 367
Cdd:cd07119 241 ALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLV 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  368 SQMQLNKILKYVDIGKNEGATLITGGERLG----SKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMAN 443
Cdd:cd07119 321 SAEHREKVLSYIQLGKEEGARLVCGGKRPTgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLAN 400
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324950  444 DSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAVRAKLDE 519
Cdd:cd07119 401 DTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLSP 476
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
32-513 0e+00

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259  Cd Length: 538  Bit Score: 574.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    32 PIKLPNGLEYEQptgLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNGIDPIDRGKA 111
Cdd:PLN02466  48 PITPPVQVSYTQ---LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRI 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   112 LYRLAELIEQDKDVIASIETLDNGKAISSSRG-DVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIP 190
Cdd:PLN02466 125 LLRFADLLEKHNDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIP 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   191 WNFPLLMWAWKIAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGST 270
Cdd:PLN02466 205 WNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGST 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   271 ATGRHIYQSAA-AGLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASE 349
Cdd:PLN02466 285 DTGKIVLELAAkSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARAL 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   350 SIKVGDPFDESTFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTV 429
Cdd:PLN02466 365 KRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSI 444
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   430 TKFKSADEVINMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQ 509
Cdd:PLN02466 445 LKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQ 524

                 ....
gi 6324950   510 VKAV 513
Cdd:PLN02466 525 VKAV 528
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
64-513 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  Cd Length: 453  Bit Score: 574.77  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   64 VINPSTEEEICHIYEGREDDVEEAVQAADRAFSNgsWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSRG 143
Cdd:cd07115   1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  144 -DVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAESTPL 222
Cdd:cd07115  79 lDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  223 SALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIVFAD 302
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  303 AELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKILKYVDIG 382
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  383 KNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTSNINTAL 462
Cdd:cd07115 319 REEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 6324950  463 KVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07115 399 RVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
46-511 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  Cd Length: 480  Bit Score: 574.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   46 GLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDV 125
Cdd:cd07559   2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK--TWGKTSVAERANILNKIADRIEENLEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  126 IASIETLDNGKAISSSRG-DVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAP 204
Cdd:cd07559  80 LAVAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  205 ALVTGNTVVLKTAESTPLSALYVSKYIPQAgIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGL 284
Cdd:cd07559 160 ALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  285 KKVTLELGGKSPNIVFADA-----ELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDE 359
Cdd:cd07559 239 IPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDP 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  360 STFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERLGS----KGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSA 435
Cdd:cd07559 319 ETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLggldKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDE 398
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324950  436 DEVINMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVK 511
Cdd:cd07559 399 EEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
59-513 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  Cd Length: 462  Bit Score: 563.38  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   59 NKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAI 138
Cdd:cd07112   1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  139 SSSR-GDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTA 217
Cdd:cd07112  81 SDALaVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  218 ESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQ-SAAAGLKKVTLELGGKSP 296
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEySGQSNLKRVWLECGGKSP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  297 NIVFADAE-LKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKI 375
Cdd:cd07112 241 NIVFADAPdLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  376 LKYVDIGKNEGATLITGGERL--GSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGI 453
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  454 HTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
64-513 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  Cd Length: 455  Bit Score: 558.72  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   64 VINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSR- 142
Cdd:cd07093   1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP--GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARt 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  143 GDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAESTPL 222
Cdd:cd07093  79 RDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  223 SALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIVFAD 302
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFAD 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  303 AELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKILKYVDIG 382
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  383 KNEGATLITGGERLGS----KGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTSNI 458
Cdd:cd07093 319 RAEGATILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6324950  459 NTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
45-513 0e+00

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410  Cd Length: 501  Bit Score: 557.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    45 TGLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNGIDPIDRGKALYRLAELIEQDKD 124
Cdd:PLN02766  21 TKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   125 VIASIETLDNGKAISSSRG-DVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIA 203
Cdd:PLN02766 101 ELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVA 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   204 PALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAG 283
Cdd:PLN02766 181 PALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATS 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   284 -LKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTF 362
Cdd:PLN02766 261 nLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRAR 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   363 QGAQTSQMQLNKILKYVDIGKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMA 442
Cdd:PLN02766 341 QGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKA 420
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324950   443 NDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:PLN02766 421 NNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
46-511 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: 532.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   46 GLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDV 125
Cdd:cd07117   2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK--TWRKTTVAERANILNKIADIIDENKEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  126 IASIETLDNGKAISSSRG-DVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAP 204
Cdd:cd07117  80 LAMVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  205 ALVTGNTVVLKTAESTPLSALYVSKYIPQAgIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGL 284
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  285 KKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQG 364
Cdd:cd07117 239 IPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMG 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  365 AQTSQMQLNKILKYVDIGKNEGATLITGGERLGS----KGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVIN 440
Cdd:cd07117 319 AQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTEngldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVID 398
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324950  441 MANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVK 511
Cdd:cd07117 399 MANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMK 469
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
47-513 0e+00

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 522.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    47 LFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVI 126
Cdd:PRK13252   9 LYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK--IWAAMTAMERSRILRRAVDILRERNDEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   127 ASIETLDNGKAISSSRGdVDLV-----INYLkssAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWK 201
Cdd:PRK13252  87 AALETLDTGKPIQETSV-VDIVtgadvLEYY---AGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   202 IAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKiVGEAITNHPKIKKVAFTGSTATGRHIYQSAA 281
Cdd:PRK13252 163 SAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   282 AGLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDEST 361
Cdd:PRK13252 242 ASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPAT 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   362 FQGAQTSQMQLNKILKYVDIGKNEGATLITGGERL----GSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADE 437
Cdd:PRK13252 322 NFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLteggFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDE 401
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324950   438 VINMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:PRK13252 402 VIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
44-513 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: 521.67  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   44 PTGLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNGIDPIDRGKALYRLAELIEQDK 123
Cdd:cd07140   5 PHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLMEEHQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  124 DVIASIETLDNGKAISSS-RGDVDLVINYLKSSAGFADKIDGRMIDTGRTH----FSYTKRQPLGVCGQIIPWNFPLLMW 198
Cdd:cd07140  85 EELATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARpnrnLTLTKREPIGVCGIVIPWNYPLMML 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  199 AWKIAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQ 278
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  279 SAA-AGLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPF 357
Cdd:cd07140 245 SCAvSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  358 DESTFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSAD- 436
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDv 404
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324950  437 -EVINMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07140 405 dGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
48-511 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  Cd Length: 467  Bit Score: 520.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950     48 FINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFsnGSWNGIDPIDRGKALYRLAELIEQDKDVIA 127
Cdd:TIGR01804   1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    128 SIETLDNGKAIS-SSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPAL 206
Cdd:TIGR01804  79 KLETLDTGKTLQeTIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPAL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    207 VTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKK 286
Cdd:TIGR01804 159 AAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKH 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    287 VTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQ 366
Cdd:TIGR01804 239 VTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    367 TSQMQLNKILKYVDIGKNEGATLITGGERLG----SKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMA 442
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGRPEnvglQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324950    443 NDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVK 511
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
64-513 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  Cd Length: 457  Bit Score: 519.17  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   64 VINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSRG 143
Cdd:cd07090   1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK--EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  144 DVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAESTPLS 223
Cdd:cd07090  79 DIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  224 ALYVSKYIPQAGIPPGVINIVSGFGKiVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIVFADA 303
Cdd:cd07090 159 ALLLAEILTEAGLPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  304 ELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKILKYVDIGK 383
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  384 NEGATLITGGERLGSK-----GYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTSNI 458
Cdd:cd07090 318 QEGAKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6324950  459 NTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07090 398 QRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
64-513 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  Cd Length: 451  Bit Score: 517.76  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   64 VINPSTEEEICHIYEGREDDVEEAVQAADRAFsnGSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSRG 143
Cdd:cd07103   1 VINPATGEVIGEVPDAGAADADAAIDAAAAAF--KTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  144 DVDLVINYLKSSAGFADKIDGRMI---DTGRTHFsyTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAEST 220
Cdd:cd07103  79 EVDYAASFLEWFAEEARRIYGRTIpspAPGKRIL--VIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  221 PLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIVF 300
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVF 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  301 ADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKILKYVD 380
Cdd:cd07103 237 DDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVE 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  381 IGKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTSNINT 460
Cdd:cd07103 317 DAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLAR 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 6324950  461 ALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07103 397 AWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
65-513 2.62e-175

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  Cd Length: 454  Bit Score: 501.48  E-value: 2.62e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   65 INPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSRGD 144
Cdd:cd07118   2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  145 VDLVINYLKSSAGFADKIDGRMIDT-GRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAESTPLS 223
Cdd:cd07118  82 IEGAADLWRYAASLARTLHGDSYNNlGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  224 ALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIVFADA 303
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADA 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  304 ELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKILKYVDIGK 383
Cdd:cd07118 242 DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGR 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  384 NEGATLITGGERLGS-KGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTSNINTAL 462
Cdd:cd07118 322 AEGATLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTAL 401
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 6324950  463 KVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07118 402 TVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
47-513 5.39e-175

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  Cd Length: 466  Bit Score: 500.88  E-value: 5.39e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   47 LFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFsnGSWNGIDPIDRGKALYRLAELIEQDKDVI 126
Cdd:cd07138   1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAF--PAWSATSVEERAALLERIAEAYEARADEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  127 ASIETLDNGKAISSSRGD-VDLVINYLKSSAGFADKIDGRmIDTGRTHFSytkRQPLGVCGQIIPWNFPLLMWAWKIAPA 205
Cdd:cd07138  79 AQAITLEMGAPITLARAAqVGLGIGHLRAAADALKDFEFE-ERRGNSLVV---REPIGVCGLITPWNWPLNQIVLKVAPA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  206 LVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLK 285
Cdd:cd07138 155 LAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVK 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  286 KVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGA 365
Cdd:cd07138 235 RVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGP 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  366 QTSQMQLNKILKYVDIGKNEGATLITGG----ERLgSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINM 441
Cdd:cd07138 315 LASAAQFDRVQGYIQKGIEEGARLVAGGpgrpEGL-ERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAI 393
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324950  442 ANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINtYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07138 394 ANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
64-513 1.61e-174

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  Cd Length: 446  Bit Score: 498.98  E-value: 1.61e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   64 VINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSRG 143
Cdd:cd07106   1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFP--GWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  144 DVDLVINYLKSSAGFAdkIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAESTPLS 223
Cdd:cd07106  79 EVGGAVAWLRYTASLD--LPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  224 ALYVSKYIPQAgIPPGVINIVSGfGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIVFADA 303
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDV 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  304 ELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKILKYVDIGK 383
Cdd:cd07106 235 DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAK 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  384 NEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTSNINTALK 463
Cdd:cd07106 315 AKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEA 394
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 6324950  464 VADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07106 395 VARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
44-517 3.76e-174

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 499.05  E-value: 3.76e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    44 PTGLFINNKFVPSkQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFsnGSWNGIDPIDRGKALYRLAELIEQDK 123
Cdd:PRK13473   2 QTKLLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAF--PEWSQTTPKERAEALLKLADAIEENA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   124 DVIASIETLDNGKAISSSRGD-VDLVINYLKSSAGFADKIDGRMidTG---RTHFSYTKRQPLGVCGQIIPWNFPLLMWA 199
Cdd:PRK13473  79 DEFARLESLNCGKPLHLALNDeIPAIVDVFRFFAGAARCLEGKA--AGeylEGHTSMIRRDPVGVVASIAPWNYPLMMAA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   200 WKIAPALVTGNTVVLKTAESTPLSALYVSKYIPQAgIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQS 279
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   280 AAAGLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDE 359
Cdd:PRK13473 236 AADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDE 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   360 STFQGAQTSQMQLNKILKYVDIGKNEG-ATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEV 438
Cdd:PRK13473 316 DTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQA 395
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324950   439 INMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAVRAKL 517
Cdd:PRK13473 396 VRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKH 474
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
64-513 1.00e-173

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  Cd Length: 454  Bit Score: 497.14  E-value: 1.00e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   64 VINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNgIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSRG 143
Cdd:cd07109   1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLR-LSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  144 DVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAESTPLS 223
Cdd:cd07109  80 DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  224 ALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIVFADA 303
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  304 ELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFqGAQTSQMQLNKILKYVDIGK 383
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDL-GPLISAKQLDRVEGFVARAR 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  384 NEGATLITGGERL---GSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTSNINT 460
Cdd:cd07109 319 ARGARIVAGGRIAegaPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6324950  461 ALKVADRVNAGTVWINTYndFHHA---VPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07109 399 ALRVARRLRAGQVFVNNY--GAGGgieLPFGGVKKSGHGREKGLEALYNYTQTKTV 452
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
46-515 2.96e-173

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  Cd Length: 480  Bit Score: 496.92  E-value: 2.96e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   46 GLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDV 125
Cdd:cd07111  23 GHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE--SWSALPGHVRARHLYRIARHIQKHQRL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  126 IASIETLDNGKAISSSR-GDVDLVINYLKSSAGFADKIDGRMidtgrthfsyTKRQPLGVCGQIIPWNFPLLMWAWKIAP 204
Cdd:cd07111 101 FAVLESLDNGKPIRESRdCDIPLVARHFYHHAGWAQLLDTEL----------AGWKPVGVVGQIVPWNFPLLMLAWKICP 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  205 ALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKiVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGL 284
Cdd:cd07111 171 ALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAGTG 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  285 KKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQG 364
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMG 329
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  365 AQTSQMQLNKILKYVDIGKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMAND 444
Cdd:cd07111 330 AIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANN 409
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324950  445 SEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAVRA 515
Cdd:cd07111 410 TPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPSWEPA 480
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
64-513 1.71e-172

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  Cd Length: 456  Bit Score: 494.18  E-value: 1.71e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   64 VINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSRG 143
Cdd:cd07110   1 VINPATEATIGEIPAATAEDVDAAVRAARRAFP--RWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  144 DVDLVINYLKSSAGFADKID---GRMIDTGRTHFS-YTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAES 219
Cdd:cd07110  79 DVDDVAGCFEYYADLAEQLDakaERAVPLPSEDFKaRVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  220 TPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIV 299
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIV 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  300 FADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKILKYV 379
Cdd:cd07110 239 FDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  380 DIGKNEGATLITGGER--LGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTSN 457
Cdd:cd07110 319 ARGKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRD 398
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6324950  458 INTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07110 399 AERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
64-513 1.70e-169

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  Cd Length: 450  Bit Score: 486.45  E-value: 1.70e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   64 VINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSRG 143
Cdd:cd07092   1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFP--SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  144 D-VDLVINYLKSSAGFADKIDGRMI-DTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAESTP 221
Cdd:cd07092  79 DeLPGAVDNFRFFAGAARTLEGPAAgEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  222 LSALYVSKyIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIVFA 301
Cdd:cd07092 159 LTTLLLAE-LAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFD 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  302 DAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKILKYVDi 381
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE- 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  382 GKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTSNINTA 461
Cdd:cd07092 317 RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRA 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 6324950  462 LKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07092 397 MRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
48-513 3.06e-167

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  Cd Length: 468  Bit Score: 481.38  E-value: 3.06e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   48 FINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVIA 127
Cdd:cd07088   1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK--AWERLPAIERAAYLRKLADLIRENADELA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  128 SIETLDNGKAISSSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFS-YTKRQPLGVCGQIIPWNFPLLMWAWKIAPAL 206
Cdd:cd07088  79 KLIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENiFIFKVPIGVVAGILPWNFPFFLIARKLAPAL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  207 VTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKK 286
Cdd:cd07088 159 VTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITK 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  287 VTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQ 366
Cdd:cd07088 239 VSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPL 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  367 TSQMQLNKILKYVDIGKNEGATLITGGERL-GSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDS 445
Cdd:cd07088 319 VNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDS 398
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324950  446 EYGLAAGIHTSNINTALKVADRVNAGTVWIN-----TYNDFHHavpfgGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07088 399 EYGLTSYIYTENLNTAMRATNELEFGETYINrenfeAMQGFHA-----GWKKSGLGGADGKHGLEEYLQTKVV 466
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
47-513 2.71e-166

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  Cd Length: 471  Bit Score: 478.99  E-value: 2.71e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   47 LFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNGIDPIDRGKALYRLAELIEQDKDVI 126
Cdd:cd07139   1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  127 ASIETLDNGKAISSSR-GDVDLVINYLKSSAGFADKI------DGRMIDTGRTHfsytkRQPLGVCGQIIPWNFPLLMWA 199
Cdd:cd07139  81 ARLWTAENGMPISWSRrAQGPGPAALLRYYAALARDFpfeerrPGSGGGHVLVR-----REPVGVVAAIVPWNAPLFLAA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  200 WKIAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGfGKIVGEAITNHPKIKKVAFTGSTATGRHIYQS 279
Cdd:cd07139 156 LKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAV 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  280 AAAGLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDE 359
Cdd:cd07139 235 CGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  360 STFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERLG--SKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADE 437
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAglDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDD 394
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324950  438 VINMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTY-NDFHhaVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07139 395 AVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFrLDFG--APFGGFKQSGIGREGGPEGLDAYLETKSI 469
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
64-513 1.17e-165

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: 476.85  E-value: 1.17e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   64 VINPSTEEEICHIYEGREDDVEEAVQAADRAFsnGSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAI-SSSR 142
Cdd:cd07108   1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQAR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  143 GDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAESTPL 222
Cdd:cd07108  79 PEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  223 SALYVSKyIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIVFAD 302
Cdd:cd07108 159 AVLLLAE-ILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  303 AELKKAVQNIILGI-YYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKILKYVDI 381
Cdd:cd07108 238 ADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  382 GKNE-GATLITGG----ERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTS 456
Cdd:cd07108 318 GLSTsGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6324950  457 NINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDA-LQNYLQVKAV 513
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
64-513 2.24e-165

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  Cd Length: 459  Bit Score: 476.35  E-value: 2.24e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   64 VINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWnGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSRG 143
Cdd:cd07089   1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  144 -DVDLVINYLKSSAGFADK------IDGRMIDTGRTHfSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKT 216
Cdd:cd07089  80 mQVDGPIGHLRYFADLADSfpwefdLPVPALRGGPGR-RVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  217 AESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSP 296
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  297 NIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKIL 376
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  377 KYVDIGKNEGATLITGGERL--GSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIH 454
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPagLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6324950  455 TSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
46-513 1.19e-164

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: 475.01  E-value: 1.19e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   46 GLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFsNGSWNGIDPIDRGKALYRLAELIEQDKDV 125
Cdd:cd07113   1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAF-VSAWAKTTPAERGRILLRLADLIEQHGEE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  126 IASIETLDNGKAISSSRG-DVDLVINYLKSSAGFADKIDGRMID------TGRTHFSYTKRQPLGVCGQIIPWNFPLLMW 198
Cdd:cd07113  80 LAQLETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETLApsipsmQGERYTAFTRREPVGVVAGIVPWNFSVMIA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  199 AWKIAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKiVGEAITNHPKIKKVAFTGSTATGRHIYQ 278
Cdd:cd07113 160 VWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGR 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  279 SAAAGLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFD 358
Cdd:cd07113 239 QAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  359 ESTFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEV 438
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324950  439 INMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
48-513 2.78e-164

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: 474.04  E-value: 2.78e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   48 FINNKFVPSkqNKTFEVINPS-TEEEICHIYEGREDDVEEAVQAADRAFSNgsWNGIDPIDRGKALYRLAELIEQDKDVI 126
Cdd:cd07097   4 YIDGEWVAG--GDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  127 ASIETLDNGKAISSSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTH-FSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPA 205
Cdd:cd07097  80 ARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGvEVETTREPLGVVGLITPWNFPIAIPAWKIAPA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  206 LVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLK 285
Cdd:cd07097 160 LAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  286 KVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGA 365
Cdd:cd07097 240 RVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  366 QTSQMQLNKILKYVDIGKNEGATLITGGERL--GSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMAN 443
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324950  444 DSEYGLAAGIHTSNINTALKVADRVNAGTVWIN---TYNDFHhaVPFGGFNASGLG-REMSVDALQNYLQVKAV 513
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlptAGVDYH--VPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
89-513 2.67e-163

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: 467.48  E-value: 2.67e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   89 QAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSRGDVDLVINYLKSSAGFADKIDGRMI- 167
Cdd:cd06534   1 AAARAAFK--AWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELp 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  168 DTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGF 247
Cdd:cd06534  79 SPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  248 GKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAG 327
Cdd:cd06534 159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  328 SRVYVEESIYDKFIEEFKaasesikvgdpfdestfqgaqtsqmqlnkilkyvdigknegatlitggerlgskgyfikpTV 407
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV------------------------------------------------------------TV 258
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  408 FGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHA-VP 486
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPeAP 338
                       410       420
                ....*....|....*....|....*..
gi 6324950  487 FGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd06534 339 FGGVKNSGIGREGGPYGLEEYTRTKTV 365
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
48-513 6.72e-157

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: 455.27  E-value: 6.72e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   48 FINNKFVPSKQNKTFEVINPSTEEEICHIY-EGREDDVEEAVQAADRAFsnGSWNGIDPIDRGKALYRLAELIEQDKDVI 126
Cdd:cd07131   2 YIGGEWVDSASGETFDSRNPADLEEVVGTFpLSTASDVDAAVEAAREAF--PEWRKVPAPRRAEYLFRAAELLKKRKEEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  127 ASIETLDNGKAISSSRGDVDLVINYLKSSAG-----FADKIDGRMIDTgrthFSYTKRQPLGVCGQIIPWNFPLLMWAWK 201
Cdd:cd07131  80 ARLVTREMGKPLAEGRGDVQEAIDMAQYAAGegrrlFGETVPSELPNK----DAMTRRQPIGVVALITPWNFPVAIPSWK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  202 IAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAA 281
Cdd:cd07131 156 IFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  282 AGLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDEST 361
Cdd:cd07131 236 RPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEET 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  362 FQGAQTSQMQLNKILKYVDIGKNEGATLITGGERL----GSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADE 437
Cdd:cd07131 316 DMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLtgggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEE 395
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324950  438 VINMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWIN--TYNDFHHaVPFGGFNASGLG-REMSVDALQNYLQVKAV 513
Cdd:cd07131 396 AIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIGAEVH-LPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
48-511 4.16e-155

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  Cd Length: 479  Bit Score: 450.75  E-value: 4.16e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   48 FINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVIA 127
Cdd:cd07116   4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE--AWGKTSVAERANILNKIADRMEANLEMLA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  128 SIETLDNGKAI-SSSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPAL 206
Cdd:cd07116  82 VAETWDNGKPVrETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  207 VTGNTVVLKTAESTPLSALYVSKYIPQAgIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKK 286
Cdd:cd07116 162 AAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  287 VTLELGGKSPNIVFA------DAELKKAVQNIILgIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDES 360
Cdd:cd07116 241 VTLELGGKSPNIFFAdvmdadDAFFDKALEGFVM-FALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTE 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  361 TFQGAQTSQMQLNKILKYVDIGKNEGATLITGGER-----LGSKGYFIKPTVFGDVKedMRIVKEEIFGPVVTVTKFKSA 435
Cdd:cd07116 320 TMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelggLLGGGYYVPTTFKGGNK--MRIFQEEIFGPVLAVTTFKDE 397
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324950  436 DEVINMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVK 511
Cdd:cd07116 398 EEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
64-517 4.48e-155

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  Cd Length: 456  Bit Score: 449.90  E-value: 4.48e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   64 VINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSRG 143
Cdd:cd07107   1 VINPATGQVLARVPAASAADVDRAVAAARAAFP--EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  144 DVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAESTPLS 223
Cdd:cd07107  79 DVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  224 ALYVSKYIpQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIVFADA 303
Cdd:cd07107 159 ALRLAELA-REVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  304 ELKKAVQNIILGIYYN-SGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKILKYVDIG 382
Cdd:cd07107 238 DPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  383 KNEGATLITGGER----LGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTSNI 458
Cdd:cd07107 318 KREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6324950  459 NTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAVRAKL 517
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
PLN02467 PLN02467
betaine aldehyde dehydrogenase
46-513 1.64e-154

betaine aldehyde dehydrogenase


Pssm-ID: 215260  Cd Length: 503  Bit Score: 450.34  E-value: 1.64e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    46 GLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSN---GSWNGIDPIDRGKALYRLAELIEQD 122
Cdd:PLN02467   9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgKDWARTTGAVRAKYLRAIAAKITER 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   123 KDVIASIETLDNGKAISSSRGDVDLVINYLKSSAGFADKIDGRM---IDTGRTHF-SYTKRQPLGVCGQIIPWNFPLLMW 198
Cdd:PLN02467  89 KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQkapVSLPMETFkGYVLKEPLGVVGLITPWNYPLLMA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   199 AWKIAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQ 278
Cdd:PLN02467 169 TWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMT 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   279 SAAAGLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFD 358
Cdd:PLN02467 249 AAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLE 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   359 ESTFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERLG--SKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSAD 436
Cdd:PLN02467 329 EGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTED 408
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324950   437 EVINMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:PLN02467 409 EAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
62-513 2.06e-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  Cd Length: 453  Bit Score: 437.80  E-value: 2.06e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   62 FEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSwnGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSS 141
Cdd:cd07149   1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMK--SLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  142 RGDVDLVINYLKSSAGFADKIDGRMIDT-----GRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKT 216
Cdd:cd07149  79 RKEVDRAIETLRLSAEEAKRLAGETIPFdaspgGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  217 AESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIyqSAAAGLKKVTLELGGKSP 296
Cdd:cd07149 159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAI--ARKAGLKKVTLELGSNAA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  297 NIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKIL 376
Cdd:cd07149 237 VIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIE 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  377 KYVDIGKNEGATLITGGERLGSkgyFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTS 456
Cdd:cd07149 317 EWVEEAVEGGARLLTGGKRDGA---ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTN 393
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6324950  457 NINTALKVADRVNAGTVWINTYNDFH-HAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:cd07149 394 DLQKALKAARELEVGGVMINDSSTFRvDHMPYGGVKESGTGREGPRYAIEEMTEIKLV 451
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
83-498 3.97e-148

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  Cd Length: 431  Bit Score: 431.18  E-value: 3.97e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   83 DVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSRGDVDLVINYLKSSAGFADKI 162
Cdd:cd07104   1 DVDRAYAAAAAAQK--AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  163 DGRMIDT---GRthFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAESTPLS-ALYVSKYIPQAGIPP 238
Cdd:cd07104  79 EGEILPSdvpGK--ESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  239 GVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYY 318
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  319 NSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERlgs 398
Cdd:cd07104 237 HQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY--- 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  399 KGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWIN-- 476
Cdd:cd07104 314 EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINdq 393
                       410       420
                ....*....|....*....|..
gi 6324950  477 TYNDFHHaVPFGGFNASGLGRE 498
Cdd:cd07104 394 TVNDEPH-VPFGGVKASGGGRF 414
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
48-513 1.58e-145

succinic semialdehyde dehydrogenase


Pssm-ID: 215157  Cd Length: 498  Bit Score: 427.18  E-value: 1.58e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    48 FINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVIA 127
Cdd:PLN02278  28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP--SWSKLTASERSKILRRWYDLIIANKEDLA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   128 SIETLDNGKAISSSRGDVDLVINYLKSSAGFADKIDGRMIDTgrtHFSYTK----RQPLGVCGQIIPWNFPLLMWAWKIA 203
Cdd:PLN02278 106 QLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPS---PFPDRRllvlKQPVGVVGAITPWNFPLAMITRKVG 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   204 PALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAG 283
Cdd:PLN02278 183 PALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   284 LKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQ 363
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQ 342
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   364 GAQTSQMQLNKILKYVDIGKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMAN 443
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAN 422
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   444 DSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAV 513
Cdd:PLN02278 423 DTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
45-518 4.72e-145

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108  Cd Length: 494  Bit Score: 425.85  E-value: 4.72e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950    45 TGLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNGIDPIDRGKALYRLAELIEQDKD 124
Cdd:PRK09847  20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   125 VIASIETLDNGKAISSS-RGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIA 203
Cdd:PRK09847 100 ELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLG 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   204 PALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAA-A 282
Cdd:PRK09847 180 PALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGdS 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   283 GLKKVTLELGGKSPNIVFADA-ELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDEST 361
Cdd:PRK09847 260 NMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPAT 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   362 FQGAQTSQMQLNKILKYVDIGKNEGaTLITGGERLGSKGYfIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINM 441
Cdd:PRK09847 340 TMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQL 417
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324950   442 ANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAVRAKLD 518
Cdd:PRK09847 418 ANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISLE 494
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
62-511 4.67e-142

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  Cd Length: 456  Bit Score: 416.75  E-value: 4.67e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950   62 FEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSngSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSS 141
Cdd:cd07145   1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKD--VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  142 RGDVDLVINYLKSSAGFADKIDGRMI-----DTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKT 216
Cdd:cd07145  79 RVEVERTIRLFKLAAEEAKVLRGETIpvdayEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  217 AESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSP 296
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDP 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  297 NIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKIL 376
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324950  377 KYVDIGKNEGATLITGGERLGskGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTS 456
Cdd:cd07145 319 NLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTN 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6324950  457 NINTALKVADRVNAGTVWINTYNDFH-HAVPFGGFNASGLGREMSVDALQNYLQVK 511
Cdd:cd07145 397 DINRALKVARELEAGGVVINDSTRFRwDNLPFGGFKKSGIGREGVRYTMLEMTEEK 452
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
48-513 3.07e-141

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 Ant