|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
15-495 |
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: 1009.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 15 DLKIQHTKIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLAD 94
Cdd:cd07141 1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 95 LMERDRLLLATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPML 174
Cdd:cd07141 81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 175 MFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLI 254
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 255 KEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGN 334
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 335 PLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSV 414
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 415 DDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
.
gi 1371543638 495 K 495
Cdd:cd07141 481 K 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
19-492 |
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: 896.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 19 QHTKIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSpWRTMDASERGRLLNKLADLMER 98
Cdd:cd07091 2 QPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 99 DRLLLATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIW 178
Cdd:cd07091 81 DRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 179 KIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAA 258
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 259 GKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTP 338
Cdd:cd07091 241 AKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 339 GINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVI 418
Cdd:cd07091 321 DTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371543638 419 KRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
18-494 |
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: 735.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 18 IQHTKIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLME 97
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 98 RDRLLLATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFI 177
Cdd:cd07142 80 KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 178 WKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEA 257
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 258 AGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLT 337
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 338 PGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDV 417
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371543638 418 IKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVVM 476
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
18-492 |
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: 704.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 18 IQHTKIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPW-RTMDASERGRLLNKLADLM 96
Cdd:cd07143 4 EQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWgLKVSGSKRGRCLSKLADLM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 97 ERDRLLLATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMF 176
Cdd:cd07143 82 ERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 177 IWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKE 256
Cdd:cd07143 162 AWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVME 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 257 AAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPL 336
Cdd:cd07143 242 AAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 337 TPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDD 416
Cdd:cd07143 322 AEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371543638 417 VIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07143 402 AIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
4-492 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 699.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 4 PAQPAVpapladlKIQHTKIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDAS 83
Cdd:PLN02466 48 PITPPV-------QVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTAY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 84 ERGRLLNKLADLMERDRLLLATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVC 163
Cdd:PLN02466 120 ERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 164 GQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVA 243
Cdd:PLN02466 200 GQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 244 FTGSTQVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRS 323
Cdd:PLN02466 280 FTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 324 VERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFG 403
Cdd:PLN02466 360 KARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 404 PVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGL 483
Cdd:PLN02466 440 PVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSL 519
|
....*....
gi 1371543638 484 YEYTELKTV 492
Cdd:PLN02466 520 NNYLQVKAV 528
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
19-495 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 686.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 19 QHTKIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMER 98
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 99 DRLLLATMEALNGGKVFANAyLSDLGGCIKALKYCAGWADKIHGQTIPSD-GDIFTYTRREPIGVCGQIIPWNFPMLMFI 177
Cdd:COG1012 81 RREELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 178 WKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEA 257
Cdd:COG1012 160 WKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 258 AGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLT 337
Cdd:COG1012 240 AAE-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 338 PGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW-GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDD 416
Cdd:COG1012 319 PGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 417 VIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMM-LSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMK 495
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
19-492 |
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: 677.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 19 QHTKIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMER 98
Cdd:cd07144 6 QPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 99 DRLLLATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIW 178
Cdd:cd07144 84 NRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 179 KIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAA 258
Cdd:cd07144 164 KLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 259 GkSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKK-YVLGNPLT 337
Cdd:cd07144 244 A-QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 338 PGINQGPQIDKEQHDKILDLIESGKKEGAKLECGG---GRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSV 414
Cdd:cd07144 323 DDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTY 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371543638 415 DDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
34-492 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 674.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 34 SGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGK 113
Cdd:pfam00171 5 ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELETLENGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 114 VFANAyLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVK 193
Cdd:pfam00171 82 PLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 194 PAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGK 273
Cdd:pfam00171 161 PSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 274 SPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDK 353
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 354 ILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLF 433
Cdd:pfam00171 320 VLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVF 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 434 TKDLDKAITVSSALQAGVVWVNCYMMLSA-QCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:pfam00171 400 TSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
17-496 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 668.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 17 KIQHTKIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLM 96
Cdd:PLN02766 17 EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 97 ERDRLLLATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMF 176
Cdd:PLN02766 96 EEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 177 IWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKE 256
Cdd:PLN02766 176 FMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 257 AAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPL 336
Cdd:PLN02766 256 AAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 337 TPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDD 416
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 417 VIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMKI 496
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPL 495
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
24-492 |
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: 622.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 24 FINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFD-SGEWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 104 ATMEALNGGKVFANAYlSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPA 183
Cdd:cd07119 80 ARLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 184 LSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNL 263
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 264 KRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQG 343
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 344 PQIDKEQHDKILDLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIK 419
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371543638 420 RANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
35-492 |
0e+00 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 620.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 35 GKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSpWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKV 114
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 115 FANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKP 194
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 195 AEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTLELGGKS 274
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 275 PCIVFADA-DLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDK 353
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 354 ILDLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAG 431
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371543638 432 LFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
61-494 |
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: 619.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 61 DKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFAnAYLSDLGGCIKALKYCAGWADKI 140
Cdd:cd07078 1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 141 HGQTIPS-DGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVV 219
Cdd:cd07078 77 HGEVIPSpDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 220 NIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQ 299
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 300 GQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGN-K 378
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 379 GFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYM 458
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 1371543638 459 M-LSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07078 396 VgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
40-496 |
0e+00 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 596.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAY 119
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 120 LSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07115 78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 200 LTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkSNLKRVTLELGGKSPCIVF 279
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 280 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIE 359
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 360 SGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDK 439
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1371543638 440 AITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMKI 496
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
40-492 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 594.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFAnAY 119
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFE-GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIR-ET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 120 LSDLGGCIKALKYCAGWADKIHGQTIPSD-GDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQT 198
Cdd:cd07114 79 RAQVRYLAEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 199 PLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIV 278
Cdd:cd07114 159 PASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 279 FADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLI 358
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 359 ESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFT 434
Cdd:cd07114 318 ARAREEGARVLTGGERpsgaDLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1371543638 435 KDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07114 398 RDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
15-495 |
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 [Multi-domain] Cd Length: 486 Bit Score: 572.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 15 DLKIQHtKIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTMDASERGRLLNKLAD 94
Cdd:cd07140 1 TLKMPH-QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFE-NGEWGKMNARDRGRLMYRLAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 95 LMERDRLLLATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSD----GDIFTYTRREPIGVCGQIIPWN 170
Cdd:cd07140 79 LMEEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 171 FPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQV 250
Cdd:cd07140 159 YPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 251 GKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKY 330
Cdd:cd07140 239 GKHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 331 VLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMK 410
Cdd:cd07140 319 KIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 411 FKS--VDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTE 488
Cdd:cd07140 399 FDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLK 478
|
....*..
gi 1371543638 489 LKTVAMK 495
Cdd:cd07140 479 TKTVTIE 485
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
40-494 |
0e+00 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 566.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAY 119
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG---WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 120 LSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 200 LTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 280 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIE 359
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 360 SGKKEGAKLECGGGRWG----NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTK 435
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1371543638 436 DLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
40-494 |
0e+00 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 550.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAy 119
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 120 LSDLGGCIKALKYCAGWADKIHGQTIPS-DGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQT 198
Cdd:cd07103 77 RGEVDYAASFLEWFAEEARRIYGRTIPSpAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 199 PLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGK-LIKEAAgkSNLKRVTLELGGKSPCI 277
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKlLMAQAA--DTVKRVSLELGGNAPFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 278 VFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDL 357
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 358 IESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDL 437
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1371543638 438 DKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07103 395 ARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
24-492 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 538.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 24 FINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLM-ERDRLL 102
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERNDEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 103 lATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGP 182
Cdd:PRK13252 87 -AALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 183 ALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSn 262
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 263 LKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQ 342
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 343 GPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVI 418
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371543638 419 KRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
41-494 |
0e+00 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 531.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAyL 120
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 121 SDLGGCIKALKYCAGWADKIHGQTIPSDG-DIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07118 80 GEIEGAADLWRYAASLARTLHGDSYNNLGdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 200 LTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07118 160 GTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 280 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIE 359
Cdd:cd07118 239 ADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 360 SGKKEGAKLECGGGRW-GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLD 438
Cdd:cd07118 319 AGRAEGATLLLGGERLaSAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDID 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1371543638 439 KAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07118 399 TALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
23-493 |
0e+00 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 529.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 23 IFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMER--DR 100
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAF---PAWSATSVEERAALLERIAEAYEAraDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 101 LLLATMEALNGGKVFANAY-----LSDLGGCIKALKYCAgWADKIHGQTIpsdgdiftytRREPIGVCGQIIPWNFPMLM 175
Cdd:cd07138 78 LAQAITLEMGAPITLARAAqvglgIGHLRAAADALKDFE-FEERRGNSLV----------VREPIGVCGLITPWNWPLNQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 176 FIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIK 255
Cdd:cd07138 147 IVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 256 EAAGKSnLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNP 335
Cdd:cd07138 227 EAAADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 336 LTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGG-GR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:cd07138 306 RDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpGRpeGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 413 SVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNcYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07138 386 DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
.
gi 1371543638 493 A 493
Cdd:cd07138 465 Q 465
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
40-492 |
0e+00 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 527.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAy 119
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 120 LSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07090 77 RVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 200 LTALHLASLIKEAGFPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAK-GIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 280 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIE 359
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 360 SGKKEGAKLECGGGRWGNK-----GFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFT 434
Cdd:cd07090 315 SAKQEGAKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1371543638 435 KDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
24-490 |
0e+00 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 525.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 24 FINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGE---WAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 104 ATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPA 183
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 184 LSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkSNL 263
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 264 KRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQG 343
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 344 PQIDKEQHDKILDLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIK 419
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371543638 420 RANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELK 490
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
22-490 |
0e+00 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 523.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 22 KIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRL 101
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 102 LLATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIG 181
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 182 PALSCGNTVVVKPAEQTPLTALHLASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKs 261
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 262 NLKRVTLELGGKSPCIVFADA-----DLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPL 336
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 337 TPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW----GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371543638 413 SVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELK 490
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
40-493 |
0e+00 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 521.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAY 119
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFE--SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 120 lSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07109 79 -ADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 200 LTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 280 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTpGINQGPQIDKEQHDKILDLIE 359
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 360 SGKKEGAKLECGGGRWGN---KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKD 436
Cdd:cd07109 316 RARARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1371543638 437 LDKAITVSSALQAGVVWVNCYMMLSA-QCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07109 396 GDRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
40-492 |
5.00e-176 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 502.65 E-value: 5.00e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAY 119
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAF---PRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 120 LsDLGGCIKALKYCAGWADKIH---GQTIPSDGDIFT-YTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPA 195
Cdd:cd07110 78 W-DVDDVAGCFEYYADLAEQLDakaERAVPLPSEDFKaRVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 196 EQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSP 275
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 276 CIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKIL 355
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 356 DLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLF 433
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1371543638 434 TKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
40-494 |
9.14e-175 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 499.46 E-value: 9.14e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRtMDASERGRLLNKLADLMERDR-LLLATMEALNGGKVfANA 118
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFD-TGDWS-TDAEERARCLRQLHEALEARKeELRALLVAEVGAPV-MTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 119 YLSDLGGCIKALKYCAGWADKIHG-QTIPSDGDIFTYT----RREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVK 193
Cdd:cd07089 78 RAMQVDGPIGHLRYFADLADSFPWeFDLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 194 PAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkSNLKRVTLELGGK 273
Cdd:cd07089 158 PAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 274 SPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDK 353
Cdd:cd07089 237 SANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 354 ILDLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAG 431
Cdd:cd07089 317 VEGYIARGRDEGARLVTGGGRpaGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371543638 432 LFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07089 397 VWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
65-494 |
9.54e-173 |
|
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: 490.59 E-value: 9.54e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 65 KAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFAnAYLSDLGGCIKALKYCAGWADKIHGQT 144
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKPIE-EALGEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 145 IPS-DGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVP 223
Cdd:cd06534 77 LPSpDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 224 GYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCC 303
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 304 VAASRIFVEESVYDEFVKRSVerakkyvlgnpltpginqgpqidkeqhdkildliesgkkegaklecgggrwgnkgffvq 383
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 384 pTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMML-SA 462
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGvGP 335
|
410 420 430
....*....|....*....|....*....|..
gi 1371543638 463 QCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
22-492 |
3.43e-171 |
|
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: 491.20 E-value: 3.43e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 22 KIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRL 101
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 102 LLATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIG 181
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 182 PALSCGNTVVVKPAEQTPLTALHLASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKs 261
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 262 NLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGIN 341
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 342 QGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWG----NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDV 417
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTenglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371543638 418 IKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
40-492 |
8.37e-170 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 486.27 E-value: 8.37e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAY 119
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFP---GWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 120 LsDLGGCIKALKYCAGWADKIHgqTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07106 78 F-EVGGAVAWLRYTASLDLPDE--VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 200 LTALHLASLIKEAgFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAK-TLKRVTLELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 280 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIE 359
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 360 SGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDK 439
Cdd:cd07106 312 DAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1371543638 440 AITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
8-499 |
8.22e-168 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 483.47 E-value: 8.22e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 8 AVPAPLADLkiqhtkiFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAF--QIGSPWRTMDASER 85
Cdd:PLN02467 2 AIPVPRRQL-------FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrNKGKDWARTTGAVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 86 GRLLNKLADLMERDRLLLATMEALNGGKVFANAY--LSDLGGCikaLKYCAGWADKIHG-QTIPSD--GDIF-TYTRREP 159
Cdd:PLN02467 75 AKYLRAIAAKITERKSELAKLETLDCGKPLDEAAwdMDDVAGC---FEYYADLAEALDAkQKAPVSlpMETFkGYVLKEP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 160 IGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDV 239
Cdd:PLN02467 152 LGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 240 DKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEF 319
Cdd:PLN02467 232 DKIAFTGSTATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 320 VKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWG--NKGFFVQPTVFSNVTDEMRIA 397
Cdd:PLN02467 311 LEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIW 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 398 KEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRE 477
Cdd:PLN02467 391 REEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRE 470
|
490 500
....*....|....*....|..
gi 1371543638 478 LGEHGLYEYTELKTVAMKISQK 499
Cdd:PLN02467 471 LGEWGLENYLSVKQVTKYISDE 492
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
40-492 |
8.12e-167 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 478.74 E-value: 8.12e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAY 119
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPS---WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 120 LSDLGGCIKALKYCAGWADKIHGqtiPSDGDIF----TYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPA 195
Cdd:cd07092 78 DDELPGAVDNFRFFAGAARTLEG---PAAGEYLpghtSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 196 EQTPLTALHLASLIKEaGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSP 275
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 276 CIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKIL 355
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 356 DLIEsGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTK 435
Cdd:cd07092 313 GFVE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1371543638 436 DLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
24-492 |
1.57e-166 |
|
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 [Multi-domain] Cd Length: 478 Bit Score: 479.15 E-value: 1.57e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 24 FINNEWHNSVSGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLL 102
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 103 LATMEALNGGKVFANAyLSDLGGCIKALKYCAGWADKIHGQTIPSD-GDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIG 181
Cdd:cd07131 79 LARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 182 PALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKS 261
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 262 NlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGIN 341
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 342 QGPQIDKEQHDKILDLIESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDV 417
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERltggGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371543638 418 IKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMM-LSAQCPFGGFKMSGNG-RELGEHGLYEYTELKTV 492
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
24-492 |
1.97e-166 |
|
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 [Multi-domain] Cd Length: 473 Bit Score: 478.67 E-value: 1.97e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 24 FINNEWHNSVSGKkfPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLL 102
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAF---PAWRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 103 LATMEALNGGKVFANAyLSDLGGCIKALKYCAGWADKIHGQTIPS-DGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIG 181
Cdd:cd07097 79 LARLLTREEGKTLPEA-RGEVTRAGQIFRYYAGEALRLSGETLPStRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 182 PALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkS 261
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 262 NLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGIN 341
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 342 QGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW--GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIK 419
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371543638 420 RANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMM-LSAQCPFGGFKMSGNG-RELGEHGLYEYTELKTV 492
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
24-494 |
1.98e-166 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 478.68 E-value: 1.98e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 24 FINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK---AWERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 104 ATMEALNGGKVFANAYLsDLGGCIKALKYCAGWADKIHGQTIPSDG---DIFTYtrREPIGVCGQIIPWNFPMLMFIWKI 180
Cdd:cd07088 78 AKLIVEEQGKTLSLARV-EVEFTADYIDYMAEWARRIEGEIIPSDRpneNIFIF--KVPIGVVAGILPWNFPFFLIARKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 181 GPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGK 260
Cdd:cd07088 155 APALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 261 sNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGI 340
Cdd:cd07088 235 -NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 341 NQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW-GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIK 419
Cdd:cd07088 314 DMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371543638 420 RANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
20-497 |
3.60e-166 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 478.25 E-value: 3.60e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 20 HTKIFINNEWHNSvSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERD 99
Cdd:PRK13473 2 QTKLLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAF---PEWSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 100 RLLLATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGqtiPSDG----DIFTYTRREPIGVCGQIIPWNFPMLM 175
Cdd:PRK13473 78 ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEG---KAAGeyleGHTSMIRRDPVGVVASIAPWNYPLMM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 176 FIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIK 255
Cdd:PRK13473 155 AAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 256 EAAGKSnLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNP 335
Cdd:PRK13473 234 SAAADS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 336 LTPGINQGPQIDKEQHDKILDLIESGKKEG-AKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSV 414
Cdd:PRK13473 313 DDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 415 DDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMV 472
|
...
gi 1371543638 495 KIS 497
Cdd:PRK13473 473 KHT 475
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
23-494 |
5.68e-165 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 475.14 E-value: 5.68e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 23 IFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLMERDRLL 102
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 103 LATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKI-HGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIG 181
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFpFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 182 PALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkS 261
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG-E 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 262 NLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGIN 341
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 342 QGPQIDKEQHDKILDLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIK 419
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371543638 420 RANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNcYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07139 398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
4-486 |
1.06e-163 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 472.27 E-value: 1.06e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 4 PAQPAVPAPLADLKIQHTKI--FINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMD 81
Cdd:cd07111 3 PAPESAACALAWLDAHDRSFghFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 82 ASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADK----IHGqtipsdgdiftytrR 157
Cdd:cd07111 80 GHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLldteLAG--------------W 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 158 EPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTaGAAISSHM 237
Cdd:cd07111 146 KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 238 DVDKVAFTGSTQVGKLIKEA-AGKSnlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVY 316
Cdd:cd07111 225 GVDKVAFTGSTEVGRALRRAtAGTG--KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 317 DEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRI 396
Cdd:cd07111 303 EELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 397 AKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGR 476
Cdd:cd07111 383 AQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGR 462
|
490
....*....|
gi 1371543638 477 ELGEHGLYEY 486
Cdd:cd07111 463 EGGKEGLYEY 472
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
40-492 |
2.36e-163 |
|
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: 470.30 E-value: 2.36e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAY 119
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 120 LSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07108 78 RPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 200 LTALHLASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 280 ADADLDIAVEFAHHGV-FYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLI 358
Cdd:cd07108 236 PDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 359 ESGKKE-GAK-LECG---GGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLF 433
Cdd:cd07108 316 DLGLSTsGATvLRGGplpGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 434 TKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYE-YTELKTV 492
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMLEhFTQKKTV 455
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
38-494 |
3.82e-163 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 469.50 E-value: 3.82e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 38 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFAN 117
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 118 AYLsDLGGCIKALKYCAGWADKIHGQTIPSDG-DIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAE 196
Cdd:cd07150 78 AWF-ETTFTPELLRAAAGECRRVRGETLPSDSpGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 197 QTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPC 276
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 277 IVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILD 356
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 357 LIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKD 436
Cdd:cd07150 316 QVEDAVAKGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1371543638 437 LDKAITVSSALQAGVVWVNCYMMLS-AQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07150 393 LQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
59-494 |
1.59e-160 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 462.00 E-value: 1.59e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 59 DVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAYLsDLGGCIKALKYCAGWAD 138
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAF-EVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 139 KIHGQTIPSDGD-IFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLT-ALHLASLIKEAGFPP 216
Cdd:cd07104 77 RPEGEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 217 GVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVF 296
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 297 YHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWG 376
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 377 NkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNC 456
Cdd:cd07104 316 L---FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 1371543638 457 YMML-SAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07104 393 QTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
2-494 |
1.81e-157 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 456.84 E-value: 1.81e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 2 SSPAQPAVPAPLADLKIQHTKIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMD 81
Cdd:PLN02278 6 SSMDAQSALVKLRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 82 ASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAYLSDLGGcIKALKYCAGWADKIHGQTIPS---DGDIFTYtrRE 158
Cdd:PLN02278 83 ASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYG-ASFLEYFAEEAKRVYGDIIPSpfpDRRLLVL--KQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 159 PIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMD 238
Cdd:PLN02278 160 PVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 239 VDKVAFTGSTQVGKLIKEAAGKSnLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDE 318
Cdd:PLN02278 240 VRKITFTGSTAVGKKLMAGAAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 319 FVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAK 398
Cdd:PLN02278 319 FAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 399 EEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGREL 478
Cdd:PLN02278 399 EEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREG 478
|
490
....*....|....*.
gi 1371543638 479 GEHGLYEYTELKTVAM 494
Cdd:PLN02278 479 SKYGIDEYLEIKYVCL 494
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
24-495 |
2.20e-156 |
|
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: 453.44 E-value: 2.20e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 24 FINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 104 ATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQT----IPS-DGDIFT-YTRREPIGVCGQIIPWNFPMLMFI 177
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsIPSmQGERYTaFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 178 WKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVGKLIKEA 257
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 258 AgKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLT 337
Cdd:cd07113 240 A-ASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 338 PGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDV 417
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371543638 418 IKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMK 495
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
14-496 |
6.88e-156 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 452.81 E-value: 6.88e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 14 ADLKIQhTKIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSpWRTMDASERGRLLNKLA 93
Cdd:PRK09847 14 LSLAIE-NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 94 DLMERDRLLLATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPM 173
Cdd:PRK09847 92 DLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 174 LMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKL 253
Cdd:PRK09847 172 LLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 254 IKEAAGKSNLKRVTLELGGKSPCIVFADA-DLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVL 332
Cdd:PRK09847 252 LLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 333 GNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLEcgGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:PRK09847 332 GHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLL--DGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 413 SVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK09847 410 SEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
....
gi 1371543638 493 AMKI 496
Cdd:PRK09847 490 WISL 493
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
24-496 |
2.01e-155 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 451.57 E-value: 2.01e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 24 FINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:TIGR02299 4 FIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFK---RWAELKAAERKRYLHKIADLIEQHADEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 104 ATMEALNGGKVFANAYLSdlggCIKALKYCAGWADK----IHGQTIPSDgDIFTYTRREPIGVCGQIIPWNFPMLMFIWK 179
Cdd:TIGR02299 81 AVLECLDCGQPLRQTRQQ----VIRAAENFRFFADKceeaMDGRTYPVD-THLNYTVRVPVGPVGLITPWNAPFMLSTWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 180 IGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKeAAG 259
Cdd:TIGR02299 156 IAPALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIM-RNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 260 KSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPG 339
Cdd:TIGR02299 235 ADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 340 INQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWG-------NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:TIGR02299 315 TEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPtfrgedlGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 413 SVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:TIGR02299 395 DEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNV 474
|
....
gi 1371543638 493 AMKI 496
Cdd:TIGR02299 475 ALAL 478
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
40-492 |
9.51e-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 [Multi-domain] Cd Length: 456 Bit Score: 448.36 E-value: 9.51e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFAnAY 119
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE---WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 120 LSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 200 LTALHLASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSnLKRVTLELGGKSPCIVF 279
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 280 ADADLDIAVEFAHHGVFYH-QGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLI 358
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 359 ESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFT 434
Cdd:cd07107 315 DSAKREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1371543638 435 KDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
38-494 |
3.79e-152 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 441.65 E-value: 3.79e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 38 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGspwRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFAN 117
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 118 AyLSDLGGCIKALKYCAGWADKIHGQTIPSDG-----DIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVV 192
Cdd:cd07149 78 A-RKEVDRAIETLRLSAEEAKRLAGETIPFDAspggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 193 KPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGksnLKRVTLELGG 272
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 273 KSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHD 352
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 353 KILDLIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGL 432
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGKRDGA---ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371543638 433 FTKDLDKAITVSSALQAGVVWVN------CYMMlsaqcPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMINdsstfrVDHM-----PYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
18-496 |
1.44e-148 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 433.76 E-value: 1.44e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 18 IQHtkiFINNEWhnSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLME 97
Cdd:TIGR03216 1 IRN---FINGAF--VESGKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAALK--GPWGKMTVAERADLLYAVADEIE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 98 R--DRLLLAtmEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQ----TIPSDGDIFTYTRREPIGVCGQIIPWNF 171
Cdd:TIGR03216 74 RrfDDFLAA--EVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTEcfemATPDGKGALNYAVRKPLGVVGVISPWNL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 172 PMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGP-TAGAAISSHMDVDKVAFTGSTQV 250
Cdd:TIGR03216 152 PLLLMTWKVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGETRT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 251 GKLIKEAAGKSnLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKY 330
Cdd:TIGR03216 232 GSAIMKAAADG-VKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 331 VLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGG--RWGNK---GFFVQPTVFSNVTDEMRIAKEEIFGPV 405
Cdd:TIGR03216 311 KIGVPDDPATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGGvpDFGDAlagGAWVQPTIWTGLPDSARVVTEEIFGPC 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 406 QQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYE 485
Cdd:TIGR03216 391 CHIAPFDSEEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEF 470
|
490
....*....|.
gi 1371543638 486 YTELKTVAMKI 496
Cdd:TIGR03216 471 YTELTNVCIKL 481
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
19-496 |
2.66e-143 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 421.25 E-value: 2.66e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 19 QHTKIFINNEWHnsVSGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLME 97
Cdd:cd07124 31 REYPLVIGGKEV--RTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFP---TWRRTPPEERARLLLRAAALLR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 98 RDRLLLATMEALNGGKVFANAyLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFI 177
Cdd:cd07124 106 RRRFELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 178 WKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEA 257
Cdd:cd07124 185 GMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYER 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 258 AGK-----SNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVL 332
Cdd:cd07124 265 AAKvqpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 333 GNPLTPGINQGPQIDKEQHDKILDLIESGKKEGaKLECGGGRWGN--KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMK 410
Cdd:cd07124 345 GDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 411 FKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVN--CYMMLSAQCPFGGFKMSG-NGRELGEHGLYEYT 487
Cdd:cd07124 424 AKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGtGSKAGGPDYLLQFM 503
|
....*....
gi 1371543638 488 ELKTVAMKI 496
Cdd:cd07124 504 QPKTVTENF 512
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
24-492 |
6.13e-143 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 419.28 E-value: 6.13e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 24 FINNEWHNSvSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 104 ATMEALNGGKVFANAyLSDLGGCIKALKYCAGWADKIHGQTIPSD-GDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGP 182
Cdd:cd07086 78 GRLVSLEMGKILPEG-LGEVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 183 ALSCGNTVVVKPAEQTPLTALHLASLIKEA----GFPPGVVNIVPGYGPtAGAAISSHMDVDKVAFTGSTQVGKLIKEAA 258
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 259 GKSNlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTP 338
Cdd:cd07086 236 ARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 339 GINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW--GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDD 416
Cdd:cd07086 315 GTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 417 VIKRANNTTYGLAAGLFTKDLDKAITVSSA--LQAGVVWVNcymmLS-----AQCPFGGFKMSGNGRELGEHGLYEYTEL 489
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVN----IPtsgaeIGGAFGGEKETGGGRESGSDAWKQYMRR 470
|
...
gi 1371543638 490 KTV 492
Cdd:cd07086 471 STC 473
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
38-493 |
7.72e-143 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 417.90 E-value: 7.72e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 38 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFAN 117
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV---MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 118 AYLsDLGGCIKALKYCAGWADKIHGQTIPSDGDIFT-----YTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVV 192
Cdd:cd07145 78 SRV-EVERTIRLFKLAAEEAKVLRGETIPVDAYEYNerriaFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 193 KPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGkSNLKRVTLELGG 272
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 273 KSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHD 352
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 353 KILDLIESGKKEGAKLECGGGRwgNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGL 432
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGKR--DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371543638 433 FTKDLDKAITVSSALQAGVVWVNCYMMLSA-QCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFRWdNLPFGGFKKSGIGREGVRYTMLEMTEEKTIV 455
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
24-490 |
3.99e-141 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 414.54 E-value: 3.99e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 24 FINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE---AWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 104 ATMEALNGGKVFANAYLSDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPA 183
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 184 LSCGNTVVVKPAEQTPLTALHLASLIKEAgFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNL 263
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 264 KRVTLELGGKSPCIVFA------DADLDIAVE----FAhhgvfYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLG 333
Cdd:cd07116 239 IPVTLELGGKSPNIFFAdvmdadDAFFDKALEgfvmFA-----LNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 334 NPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRW----GNKGFFVQPTVFSNvTDEMRIAKEEIFGPVQQIM 409
Cdd:cd07116 314 NPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNelggLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 410 KFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTEL 489
Cdd:cd07116 393 TFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQT 472
|
.
gi 1371543638 490 K 490
Cdd:cd07116 473 K 473
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
41-494 |
5.42e-140 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 410.97 E-value: 5.42e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTmDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAYL 120
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFD-ETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 121 sDLGGCIKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPL 200
Cdd:cd07120 80 -EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 201 TALHLASLIKEA-GFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAP-TLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 280 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIE 359
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 360 SGKKEGAKLECGGGRWG---NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKD 436
Cdd:cd07120 318 RAIAAGAEVVLRGGPVTeglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1371543638 437 LDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
27-495 |
3.54e-133 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 393.59 E-value: 3.54e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 27 NEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAfqiGSPWRTMDASERGRLLNKLADLME--RDRLLLA 104
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA---QKEWAATLPQERAEILEKAAQILEerRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 105 TMEALNGGKVFANAylsDLGGCIKALKYCAGWADKIHGQTIPSDGD-----IFtytrREPIGVCGQIIPWNFPMLMFIWK 179
Cdd:cd07151 78 LIRESGSTRIKANI---EWGAAMAITREAATFPLRMEGRILPSDVPgkenrVY----REPLGVVGVISPWNFPLHLSMRS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 180 IGPALSCGNTVVVKPAEQTPLTA-LHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAA 258
Cdd:cd07151 151 VAPALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 259 GKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTP 338
Cdd:cd07151 231 GR-HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 339 GINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVI 418
Cdd:cd07151 310 DTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEAEGN---VLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEAL 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371543638 419 KRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMML-SAQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMK 495
Cdd:cd07151 387 ELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
60-492 |
5.36e-129 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 381.81 E-value: 5.36e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 60 VDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAyLSDLGGCIKALKYcagWADK 139
Cdd:cd07100 1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRY---YAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 140 IHG----QTIPSDGDIfTYTRREPIGVCGQIIPWNFPmlmfIWKI----GPALSCGNTVVVKPAEQTPLTALHLASLIKE 211
Cdd:cd07100 74 AEAfladEPIETDAGK-AYVRYEPLGVVLGIMPWNFP----FWQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 212 AGFPPGVVNIVPGYGPTAGAAISSHMdVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFA 291
Cdd:cd07100 149 AGFPEGVFQNLLIDSDQVEAIIADPR-VRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 292 HHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECG 371
Cdd:cd07100 227 VKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 372 GGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGV 451
Cdd:cd07100 307 GKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGM 386
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1371543638 452 VWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07100 387 VFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
40-494 |
5.33e-127 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 377.54 E-value: 5.33e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAy 119
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 120 LSDLGGCIKALKYCAGWADKIHGQTIPSD-----GDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKP 194
Cdd:cd07094 79 RVEVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 195 AEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsnlKRVTLELGGKS 274
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG---KRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 275 PCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKI 354
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 355 LDLIESGKKEGAKLECGGGRwgnKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFT 434
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371543638 435 KDLDKAITVSSALQAGVVWVNCYMMLSAQ-CPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07094 393 RDLNVAFKAAEKLEVGGVMVNDSSAFRTDwMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
47-479 |
4.64e-125 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 372.01 E-value: 4.64e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 47 EVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAyLSDLGGC 126
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQR---AWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKA-GFEVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 127 IKALKYCAGWADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTA-LHL 205
Cdd:cd07152 78 IGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 206 ASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLD 285
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 286 IAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEG 365
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 366 AKLECGGGRwgnKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSS 445
Cdd:cd07152 316 ARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430
....*....|....*....|....*....|....*
gi 1371543638 446 ALQAGVVWVNCYMML-SAQCPFGGFKMSGNGRELG 479
Cdd:cd07152 393 RLRTGMLHINDQTVNdEPHNPFGGMGASGNGSRFG 427
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
41-493 |
1.35e-124 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 371.17 E-value: 1.35e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAYL 120
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRA---WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 121 sDLGGCIKALKYCAGWADKIHGQTIPSDGDIF----TYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAE 196
Cdd:cd07099 78 -EVLLALEAIDWAARNAPRVLAPRKVPTGLLMpnkkATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 197 QTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISShmDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPC 276
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA--GVDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 277 IVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILD 356
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 357 LIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKD 436
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1371543638 437 LDKAITVSSALQAGVVWVNCYMMLSAQC--PFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLLTAGIPalPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
19-496 |
1.75e-123 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 370.80 E-value: 1.75e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 19 QHTKIFINNEWHNSvsGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLME 97
Cdd:PRK03137 35 QDYPLIIGGERITT--EDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE---TWKKWSPEDRARILLRAAAIIR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 98 RDRLLLATMEALNGGKVFANAyLSDLGGCIKALKYCA----GWADKIHGQTIPSDGDIFTYtrrEPIGVCGQIIPWNFPM 173
Cdd:PRK03137 110 RRKHEFSAWLVKEAGKPWAEA-DADTAEAIDFLEYYArqmlKLADGKPVESRPGEHNRYFY---IPLGVGVVISPWNFPF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 174 LMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKL 253
Cdd:PRK03137 186 AIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 254 IKEAAGKSN-----LKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAK 328
Cdd:PRK03137 266 IYERAAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 329 KYVLGNPLTPGiNQGPQIDKEQHDKILDLIESGKKEGaKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQI 408
Cdd:PRK03137 346 ELTVGNPEDNA-YMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAF 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 409 MKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVN--CYMMLSAQCPFGGFKMSG-NGRELGEHGLYE 485
Cdd:PRK03137 424 IKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGFNMSGtDSKAGGPDYLLL 503
|
490
....*....|.
gi 1371543638 486 YTELKTVAMKI 496
Cdd:PRK03137 504 FLQAKTVSEMF 514
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
21-495 |
1.77e-123 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 369.15 E-value: 1.77e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 21 TKIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDR 100
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP---AWSATPVLKRQQVMFKFRQLLEENL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 101 LLLATMEALNGGKVFANAYlSDLGGCIKALKYCAGWADKIHGQTIP-SDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWK 179
Cdd:cd07085 78 DELARLITLEHGKTLADAR-GDVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 180 IGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAG 259
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 260 KSNlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPG 339
Cdd:cd07085 236 ANG-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 340 INQGPQIDKEQHDKILDLIESGKKEGAKLECgGGRwGNK------GFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKS 413
Cdd:cd07085 315 ADMGPVISPAAKERIEGLIESGVEEGAKLVL-DGR-GVKvpgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 414 VDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMML-SAQCPFGGFKMS--GNGRELGEHGLYEYTELK 490
Cdd:cd07085 393 LDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVpLAFFSFGGWKGSffGDLHFYGKDGVRFYTQTK 472
|
....*
gi 1371543638 491 TVAMK 495
Cdd:cd07085 473 TVTSR 477
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
22-477 |
5.85e-122 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 365.36 E-value: 5.85e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 22 KIFINNEWHNSvSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMERDRL 101
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR--GWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 102 LLATMEALNGGKVFANA---------YLSDlggCIKALKycagwadKIHGQTIPSDGDIFT-----YTRREPIGVCGQII 167
Cdd:cd07082 80 EVANLLMWEIGKTLKDAlkevdrtidYIRD---TIEELK-------RLDGDSLPGDWFPGTkgkiaQVRREPLGVVLAIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 168 PWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGS 247
Cdd:cd07082 150 PFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 248 TQVGKLIKEAAGKsnlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERA 327
Cdd:cd07082 230 TEVGNRLKKQHPM---KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 328 KKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRwgNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQ 407
Cdd:cd07082 307 AKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLP 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371543638 408 IMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYmmlsaqC-------PFGGFKMSGNGRE 477
Cdd:cd07082 385 IIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSK------CqrgpdhfPFLGRKDSGIGTQ 455
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
59-492 |
1.18e-119 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 358.04 E-value: 1.18e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 59 DVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLME--RDRLLLATMEALNGGKVFANaylSDLGGCIKALKYCAGW 136
Cdd:cd07105 1 DADQAVEAAAAAFPA---WSKTPPSERRDILLKAADLLEsrRDEFIEAMMEETGATAAWAG---FNVDLAAGMLREAASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 137 ADKIHGQTIPSD-GDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFP 215
Cdd:cd07105 75 ITQIIGGSIPSDkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 216 PGVVNIV---PGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAH 292
Cdd:cd07105 155 KGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 293 HGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTpginqGPQIDKEQHDKILDLIESGKKEGAKLECGG 372
Cdd:cd07105 234 FGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL-----GSLVSAAAADRVKELVDDALSKGAKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 373 -GRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGV 451
Cdd:cd07105 309 lADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1371543638 452 VWVN-CYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07105 389 VHINgMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
34-493 |
1.22e-117 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 356.11 E-value: 1.22e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 34 SGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAfQIGspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGK 113
Cdd:PRK09407 30 AGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QRA--WAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 114 VFANAY--LSDLGGCI-----KALKYCAgwaDKIHGQTIPsdgdIFTYTR--REPIGVCGQIIPWNFPMLMFIWKIGPAL 184
Cdd:PRK09407 107 ARRHAFeeVLDVALTAryyarRAPKLLA---PRRRAGALP----VLTKTTelRQPKGVVGVISPWNYPLTLAVSDAIPAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 185 SCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHmdVDKVAFTGSTQVGKLIKEAAGkSNLK 264
Cdd:PRK09407 180 LAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAG-RRLI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 265 RVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGP 344
Cdd:PRK09407 257 GFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 345 QIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKG-FFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANN 423
Cdd:PRK09407 337 LISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERAND 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371543638 424 TTYGLAAGLFTKDLDKAITVSSALQAGVVWVN-CYMML--SAQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:PRK09407 417 TPYGLNASVWTGDTARGRAIAARIRAGTVNVNeGYAAAwgSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
13-496 |
1.38e-116 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 351.90 E-value: 1.38e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 13 LADLKIQHTKIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKL 92
Cdd:PRK11241 3 LNDSTLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 93 ADLMERDRLLLATMEALNGGKVFANAYlSDLGGCIKALKYCAGWADKIHGQTIPS-DGDIFTYTRREPIGVCGQIIPWNF 171
Cdd:PRK11241 80 FNLMMEHQDDLARLMTLEQGKPLAEAK-GEISYAASFIEWFAEEGKRIYGDTIPGhQADKRLIVIKQPIGVTAAITPWNF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 172 PMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVG 251
Cdd:PRK11241 159 PAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 252 KLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYV 331
Cdd:PRK11241 239 RQLMEQCAK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 332 LGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKF 411
Cdd:PRK11241 318 IGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 412 KSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKT 491
Cdd:PRK11241 398 KDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKY 477
|
....*
gi 1371543638 492 VAMKI 496
Cdd:PRK11241 478 MCIGL 482
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
38-494 |
2.46e-116 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 350.01 E-value: 2.46e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 38 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFAN 117
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 118 AYlSDLGGCIKALKYCAGWADKIHGQTIPSDGD-----IFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVV 192
Cdd:cd07147 78 AR-GEVARAIDTFRIAAEEATRIYGEVLPLDISargegRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 193 KPAEQTPLTALHLASLIKEAGFPPGVVNIVPGygPTAGAAI-SSHMDVDKVAFTGSTQVGKLIKEAAGKsnlKRVTLELG 271
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 272 GKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQH 351
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 352 DKILDLIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAG 431
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLLTGGKRDGA---LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371543638 432 LFTKDLDKAITVSSALQAGVVWVN---CYMMLSAqcPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVINdvpTFRVDHM--PYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
40-492 |
6.02e-115 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 346.65 E-value: 6.02e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 40 VLNPATEEVICHVEEGDKADVDKAVKAArqafqiGSPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAy 119
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALA------ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDT- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 120 LSDLGGCIKALKYCAGWADKIHGQTIPSD-----GDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKP 194
Cdd:cd07146 76 RYEVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 195 AEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGksnLKRVTLELGGKS 274
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 275 PCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKI 354
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 355 LDLIESGKKEGAKLECGGGRwgnKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFT 434
Cdd:cd07146 313 ENRVEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371543638 435 KDLDKAITVSSALQAGVVWVN---CYMmlSAQCPFGGFKMSGNG-RELGEHGLYEYTELKTV 492
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNevpGFR--SELSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
41-492 |
8.31e-112 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 338.45 E-value: 8.31e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFAnAYL 120
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG---WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIA-QAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 121 SDLGGCIKALKYCAGWADKIHGQTIPSDGDIFT-YTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTP 199
Cdd:cd07102 77 GEIRGMLERARYMISIAEEALADIRVPEKDGFErYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 200 LTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHmDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07102 157 LCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP-RIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYVR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 280 ADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIE 359
Cdd:cd07102 235 PDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 360 SGKKEGAKLECGGGRWGN---KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKD 436
Cdd:cd07102 315 DAIAKGARALIDGALFPEdkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1371543638 437 LDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07102 395 IARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
43-493 |
9.22e-112 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 338.51 E-value: 9.22e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 43 PATEEVICHVEEGDKADVDKAVKAARQAfQIGspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAYLSD 122
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA-QRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 123 LGGCIKALKYC----AGWADKIHGQTIPsdgdIFTYTR--REPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAE 196
Cdd:cd07101 80 LDVAIVARYYArraeRLLKPRRRRGAIP----VLTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 197 QTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHmdVDKVAFTGSTQVGKLIKEAAGkSNLKRVTLELGGKSPC 276
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAG-RRLIGCSLELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 277 IVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILD 356
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 357 LIESGKKEGAKLECGGGRWGNKG-FFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTK 435
Cdd:cd07101 313 HVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371543638 436 DLDKAITVSSALQAGVVWVN-CYMML--SAQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNeGYAAAwaSIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
130-492 |
3.12e-106 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 322.84 E-value: 3.12e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 130 LKYCAGWADKIHGQTIPSD---GDIFTYTRrePIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLA 206
Cdd:PRK10090 41 IDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 207 SLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDI 286
Cdd:PRK10090 119 KIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 287 AVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLT-PGINQGPQIDKEQHDKILDLIESGKKEG 365
Cdd:PRK10090 198 AVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 366 AKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSS 445
Cdd:PRK10090 278 ARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIK 357
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1371543638 446 ALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK10090 358 GLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVV 404
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
42-493 |
1.12e-101 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 313.08 E-value: 1.12e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 42 NPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAYLS 121
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQ---REWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 122 DLGGCIKALKYCAGWADKiHGQTIPSDGDIFTYTRR-----EPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAE 196
Cdd:cd07098 79 EILVTCEKIRWTLKHGEK-ALRPESRPGGLLMFYKRarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 197 QTPLTALHLASLIKEA----GFPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSnLKRVTLELGG 272
Cdd:cd07098 158 QVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVVLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 273 KSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHD 352
Cdd:cd07098 236 KDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 353 KILDLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGL 428
Cdd:cd07098 316 RLEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371543638 429 AAGLFTKDLDKAITVSSALQAGVVWVNCY--MMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07098 396 GASVFGKDIKRARRIASQLETGMVAINDFgvNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
41-492 |
1.03e-94 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 294.72 E-value: 1.03e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAYl 120
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFR---DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 121 SDLGGCIKALKYCAGWADKIHGQTiPSD----GDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAE 196
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAEALLADE-PADaaavGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 197 QTPLTALHLASLIKEAGFPPGVVNIVPgYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSnLKRVTLELGGKSPC 276
Cdd:PRK09406 161 NVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 277 IVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILD 356
Cdd:PRK09406 239 IVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 357 LIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKD 436
Cdd:PRK09406 319 QVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1371543638 437 LDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK09406 399 EAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
8-496 |
4.29e-89 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 281.77 E-value: 4.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 8 AVPAPLADLK---IQHTKIFINNEWHNSvsGKKFPVLNP-ATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDAS 83
Cdd:cd07083 3 AMREALRRVKeefGRAYPLVIGGEWVDT--KERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFK---TWKDWPQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 84 ERGRLLNKLADLMERDRLLLATMEALNGGKVFANAyLSDLGGCIKALKYCAGWADKIHGQTI------PSDGDIFTytrr 157
Cdd:cd07083 78 DRARLLLKAADLLRRRRRELIATLTYEVGKNWVEA-IDDVAEAIDFIRYYARAALRLRYPAVevvpypGEDNESFY---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 158 EPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHM 237
Cdd:cd07083 153 VGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 238 DVDKVAFTGSTQVGKLIKEAAGK-----SNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVE 312
Cdd:cd07083 233 RIRGINFTGSLETGKKIYEAAARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 313 ESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGaKLECGGGRWGNKGFFVQPTVFSNVTD 392
Cdd:cd07083 313 QGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 393 EMRIAKEEIFGPVQQIMKFKSVD--DVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYMM--LSAQCPFGG 468
Cdd:cd07083 392 KARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITgaLVGVQPFGG 471
|
490 500
....*....|....*....|....*....
gi 1371543638 469 FKMSG-NGRELGEHGLYEYTELKTVAMKI 496
Cdd:cd07083 472 FKLSGtNAKTGGPHYLRRFLEMKAVAERF 500
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
26-479 |
5.88e-89 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 280.25 E-value: 5.88e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 26 NNEWhnSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLAT 105
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 106 MEALNGGKVFANAyLSDLGGCIKALKYCAGWADKIHGQTIPSD-GDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPAL 184
Cdd:cd07130 79 LVSLEMGKILPEG-LGEVQEMIDICDFAVGLSRQLYGLTIPSErPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 185 SCGNTVVVKPAEQTPLTALH----LASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGK 260
Cdd:cd07130 158 VCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 261 sNLKRVTLELGGKSPCIVFADADLDIAVE---FAHHGVfyhQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLT 337
Cdd:cd07130 237 -RFGRSLLELGGNNAIIVMEDADLDLAVRavlFAAVGT---AGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 338 PGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDeMRIAKEEIFGPVQQIMKFKSVDDV 417
Cdd:cd07130 313 DGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSD-APIVKEETFAPILYVLKFDTLEEA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371543638 418 IKRANNTTYGLAAGLFTKDLDKAITVSSALQA--GVVWVNcymmlsaqCP---------FGGFKMSGNGRELG 479
Cdd:cd07130 392 IAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVN--------IGtsgaeiggaFGGEKETGGGRESG 456
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
40-475 |
8.18e-83 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 263.90 E-value: 8.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWrtMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAy 119
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 120 LSDLGGCIKALKYCAGWADKIHGQTIP------SDGDIfTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVK 193
Cdd:cd07148 80 KVEVTRAIDGVELAADELGQLGGREIPmgltpaSAGRI-AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 194 PAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHmdvdKVA---FTGSTQVGKLI--KEAAGKsnlkRVTL 268
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDP----RVAffsFIGSARVGWMLrsKLAPGT----RCAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 269 ELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDK 348
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 349 EQHDKILDLIESGKKEGAKLECGGGRWGNKGFfvQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGL 428
Cdd:cd07148 311 REVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAF 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1371543638 429 AAGLFTKDLDKAITVSSALQAGVVWVNCYMMLSAQ-CPFGGFKMSGNG 475
Cdd:cd07148 389 QAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
12-479 |
8.66e-83 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 265.60 E-value: 8.66e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 12 PLADLKIQHTKiFINNEWHNS--VSGKKF------PVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDA 82
Cdd:cd07125 15 PLEALADALKA-FDEKEWEAIpiINGEETetgegaPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAF---AGWSATPV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 83 SERGRLLNKLADLMERDR---LLLATMEAlngGKVFANAyLSDLGGCIKALKYCAGWADKI--HGQTIPSDG--DIFTYT 155
Cdd:cd07125 91 EERAEILEKAADLLEANRgelIALAAAEA---GKTLADA-DAEVREAIDFCRYYAAQARELfsDPELPGPTGelNGLELH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 156 RREpIGVCgqIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISS 235
Cdd:cd07125 167 GRG-VFVC--ISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 236 HMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTL--ELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEE 313
Cdd:cd07125 244 HPRIDGVIFTGSTETAKLINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 314 SVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEgAKLECGGGRWGNKGFFVQPTVFSNVTDE 393
Cdd:cd07125 324 EIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGIF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 394 MRiaKEEIFGPVQQIMKFKS--VDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNcYMMLSA----QcPFG 467
Cdd:cd07125 403 DL--TTEVFGPILHVIRFKAedLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN-RNITGAivgrQ-PFG 478
|
490
....*....|..
gi 1371543638 468 GFKMSGNGRELG 479
Cdd:cd07125 479 GWGLSGTGPKAG 490
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
22-492 |
7.23e-82 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 262.12 E-value: 7.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 22 KIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRL 101
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 102 LLATMEALNGGKVFANAyLSDLGGCIKALKYCAGWADKIHGQTIPS-DGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKI 180
Cdd:TIGR01722 79 EIAELITAEHGKTHSDA-LGDVARGLEVVEHACGVNSLLKGETSTQvATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 181 GPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGK 260
Cdd:TIGR01722 158 PIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 261 SNlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVyDEFVKRSVERAKKYVLGNPLTPGI 340
Cdd:TIGR01722 237 HG-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 341 NQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGF----FVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDD 416
Cdd:TIGR01722 315 EMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 417 VIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNCYM-----MLSaqcpFGGFKMS--GNGRELGEHGLYEYTEL 489
Cdd:TIGR01722 395 AIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIpvplpYFS----FTGWKDSffGDHHIYGKQGTHFYTRG 470
|
...
gi 1371543638 490 KTV 492
Cdd:TIGR01722 471 KTV 473
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
59-476 |
4.24e-73 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 237.94 E-value: 4.24e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 59 DVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVF------ANAYLSDLGGCIKALKY 132
Cdd:cd07095 1 QVDAAVAAARAAF---PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLweaqteVAAMAGKIDISIKAYHE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 133 CAGWADKihgqtipSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEA 212
Cdd:cd07095 78 RTGERAT-------PMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 213 GFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAH 292
Cdd:cd07095 151 GLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 293 HGVFYHQGQCCVAASRIFVEES-VYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKIL----DLIESGKK---E 364
Cdd:cd07095 230 QSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLlaqqDLLALGGEpllA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 365 GAKLECGGGrwgnkgfFVQPTVFsNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVS 444
Cdd:cd07095 310 MERLVAGTA-------FLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFL 381
|
410 420 430
....*....|....*....|....*....|...
gi 1371543638 445 SALQAGVV-WVNCYMMLSAQCPFGGFKMSGNGR 476
Cdd:cd07095 382 ARIRAGIVnWNRPTTGASSTAPFGGVGLSGNHR 414
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
22-475 |
3.92e-71 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 234.65 E-value: 3.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 22 KIFINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRL 101
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA---WAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 102 LLATMEALNGGKVFANAyLSDLGGCIKALKYCA-------GWADKIHGQTIPSDG-DIFTYTRREPIGVCGQIIPWNFPM 173
Cdd:PLN00412 94 PIAECLVKEIAKPAKDA-VTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGNErNKYCLTSKIPLGVVLAIPPFNYPV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 174 LMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGStQVGKL 253
Cdd:PLN00412 173 NLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 254 IKEAAGKSNLKrvtLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLG 333
Cdd:PLN00412 252 ISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 334 NP-----LTPGINQgpqidkEQHDKILDLIESGKKEGAKLEcggGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQI 408
Cdd:PLN00412 329 PPeddcdITPVVSE------SSANFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371543638 409 MKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNcymmlSAQC------PFGGFKMSGNG 475
Cdd:PLN00412 400 IRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQIN-----SAPArgpdhfPFQGLKDSGIG 467
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
156-492 |
1.30e-70 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 231.35 E-value: 1.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 156 RREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAgFPPGVVNIVPGygptaGAAISS 235
Cdd:cd07134 97 RYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-----DAEVAQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 236 H---MDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVE 312
Cdd:cd07134 171 AlleLPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 313 ESVYDEFVKRSVERAKKYvLGNplTPGINQGPQ----IDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVqPTVFS 388
Cdd:cd07134 250 ESVKDAFVEHLKAEIEKF-YGK--DAARKASPDlariVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQRYIA-PTVLT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 389 NVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDlDKAI-TVSSALQAGVVWVNCYMM--LSAQCP 465
Cdd:cd07134 326 NVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKD-KANVnKVLARTSSGGVVVNDVVLhfLNPNLP 404
|
330 340
....*....|....*....|....*..
gi 1371543638 466 FGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07134 405 FGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
10-475 |
2.08e-70 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 243.62 E-value: 2.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 10 PAPLADLKIQHTKiFINNEWHN-------SVSGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMD 81
Cdd:PRK11905 535 EATLAALDEALNA-FAAKTWHAapllaggDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPE---WSATP 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 82 ASERGRLLNKLADLMERDR---LLLATMEAlngGKVFANAyLSDLGGCIKALKYCAGWADkihgqtipsdgDIFTYTRRE 158
Cdd:PRK11905 611 AAERAAILERAADLMEAHMpelFALAVREA---GKTLANA-IAEVREAVDFLRYYAAQAR-----------RLLNGPGHK 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 159 PIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMD 238
Cdd:PRK11905 676 PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPR 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 239 VDKVAFTGSTQVGKLIKEAAGKSNLKRVTL--ELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCvAASRI-FVEESV 315
Cdd:PRK11905 756 IAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRC-SALRVlCLQEDV 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 316 YDEFVKRSVERAKKYVLGNP--LTPGInqGPQIDKEQHDKILDLIESGKKEGAKL-ECGGGRWGNKGFFVQPTVFSnvTD 392
Cdd:PRK11905 835 ADRVLTMLKGAMDELRIGDPwrLSTDV--GPVIDAEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLIE--ID 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 393 EMRIAKEEIFGPVQQIMKFKS--VDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNcYMMLSA----QcPF 466
Cdd:PRK11905 911 SISDLEREVFGPVLHVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN-RNIIGAvvgvQ-PF 988
|
....*....
gi 1371543638 467 GGFKMSGNG 475
Cdd:PRK11905 989 GGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
31-475 |
4.80e-70 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 242.54 E-value: 4.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 31 NSVSGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLME--RDRLL-LATM 106
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPA---WSATPVEERAAILERAADLLEahRAELMaLLVR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 107 EAlngGKVFANAyLSDLGGCIKALKYCAGWADKIHGQTipsdgdiftyTRREPIGVCGQIIPWNFPMLMFIWKIGPALSC 186
Cdd:COG4230 642 EA---GKTLPDA-IAEVREAVDFCRYYAAQARRLFAAP----------TVLRGRGVFVCISPWNFPLAIFTGQVAAALAA 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 187 GNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEA-AGKSNlKR 265
Cdd:COG4230 708 GNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTlAARDG-PI 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 266 VTL--ELGGKSPCIVfaD---------ADldiAVEFAhhgvFYHQGQCCVAAsRI-FVEESVYDEFVKRSVERAKKYVLG 333
Cdd:COG4230 787 VPLiaETGGQNAMIV--DssalpeqvvDD---VLASA----FDSAGQRCSAL-RVlCVQEDIADRVLEMLKGAMAELRVG 856
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 334 NPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKL-ECGGGRWGNKGFFVQPTVFsnvtdEM-RIA--KEEIFGPVQQIM 409
Cdd:COG4230 857 DPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLI-----EIdSISdlEREVFGPVLHVV 931
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371543638 410 KFKS--VDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGvvwvNCYM---MLSA----QcPFGGFKMSGNG 475
Cdd:COG4230 932 RYKAdeLDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVG----NVYVnrnIIGAvvgvQ-PFGGEGLSGTG 1001
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
41-492 |
1.08e-69 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 229.75 E-value: 1.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAYl 120
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFR---DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 121 sdlGGCIKALKYCAGWADkiHGQT--------IPSDGDIFTYtrrEPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVV 192
Cdd:PRK13968 88 ---AEVAKSANLCDWYAE--HGPAmlkaeptlVENQQAVIEY---RPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 193 KPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMdVDKVAFTGSTQVGKLIKEAAGKSnLKRVTLELGG 272
Cdd:PRK13968 160 KHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 273 KSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHD 352
Cdd:PRK13968 238 SDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 353 KILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGL 432
Cdd:PRK13968 318 ELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 433 FTKDLDKAITVSSALQAGVVWVNCYMMLSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK13968 398 FTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
39-490 |
1.65e-69 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 230.57 E-value: 1.65e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 39 PVLNPAT-EEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFAN 117
Cdd:TIGR01238 54 PVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPT---WNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 118 AylsdLGGCIKALKYCAGWADKIHgqtipsdgDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQ 197
Cdd:TIGR01238 131 A----IAEVREAVDFCRYYAKQVR--------DVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 198 TPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKSNLKRVTL--ELGGKSP 275
Cdd:TIGR01238 199 TSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 276 CIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKIL 355
Cdd:TIGR01238 279 MIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 356 DLIESGKKEG---AKLECGGGRWGNKGFFVQPTVFSnvTDEMRIAKEEIFGPVQQIMKFKS--VDDVIKRANNTTYGLAA 430
Cdd:TIGR01238 359 AHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTM 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371543638 431 GLFTKDLDKAITVSSALQAGVVWVNCYM---MLSAQcPFGGFKMSGNG-RELGEHGLYEYTELK 490
Cdd:TIGR01238 437 GVHSRIETTYRWIEKHARVGNCYVNRNQvgaVVGVQ-PFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
2-495 |
1.79e-69 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 233.10 E-value: 1.79e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 2 SSP---AQPAVPAPLADLkiqhtkifINNEWHNSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWR 78
Cdd:PLN02419 100 TSPeqsTQPQMPPRVPNL--------IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL---WR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 79 TMDASERGRLLNKLADLMERDRLLLATMEALNGGKVFANAYlSDLGGCIKALKYCAGWADKIHGQTIP--SDGdIFTYTR 156
Cdd:PLN02419 169 NTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSH-GDIFRGLEVVEHACGMATLQMGEYLPnvSNG-VDTYSI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 157 REPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGaAISSH 236
Cdd:PLN02419 247 REPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 237 MDVDKVAFTGSTQVGKLI-KEAAGKSnlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASR-IFVEES 314
Cdd:PLN02419 326 EDIRAVSFVGSNTAGMHIyARAAAKG--KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 315 vyDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNV 390
Cdd:PLN02419 404 --KSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvpGYEKGNFIGPTILSGV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 391 TDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNcyMMLSAQCPFggFK 470
Cdd:PLN02419 482 TPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN--VPIPVPLPF--FS 557
|
490 500 510
....*....|....*....|....*....|..
gi 1371543638 471 MSGNGREL-------GEHGLYEYTELKTVAMK 495
Cdd:PLN02419 558 FTGNKASFagdlnfyGKAGVDFFTQIKLVTQK 589
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
68-492 |
3.66e-69 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 227.75 E-value: 3.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 68 RQAFQI-GSPwrtmDASERGRLLNKLADLMERDRLLLAtmEALN---GGKVFANAYLSDLGGCIKALKYC----AGW--A 137
Cdd:cd07133 8 KAAFLAnPPP----SLEERRDRLDRLKALLLDNQDALA--EAISadfGHRSRHETLLAEILPSIAGIKHArkhlKKWmkP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 138 DKIHG--QTIPSDGDIftytRREPIGVCGQIIPWNFPMLMfiwKIGP---ALSCGNTVVVKPAEQTPLTALHLASLIKEA 212
Cdd:cd07133 82 SRRHVglLFLPAKAEV----EYQPLGVVGIIVPWNYPLYL---ALGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 213 gFPPGVVNIVPGyGPTAGAAISShMDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAH 292
Cdd:cd07133 155 -FDEDEVAVVTG-GADVAAAFSS-LPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 293 HGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKY---VLGNP-LTPGINQGpqidkeQHDKILDLIESGKKEGAKL 368
Cdd:cd07133 231 FGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNPdYTSIINER------HYARLQGLLEDARAKGARV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 369 -ECG-GGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSA 446
Cdd:cd07133 305 iELNpAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRR 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1371543638 447 LQAGVVWVNCYMMLSAQ--CPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07133 385 THSGGVTINDTLLHVAQddLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
24-476 |
4.66e-69 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 228.69 E-value: 4.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 24 FINNEWHnSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:PRK09457 4 WINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 104 ATMEALNGGKVF------ANAYLSDLGGCIKALKycagwadKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFI 177
Cdd:PRK09457 80 AEVIARETGKPLweaateVTAMINKIAISIQAYH-------ERTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 178 WKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFTGSTQVGKLI-KE 256
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLhRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 257 AAGKSNlKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVY-DEFVKRSVERAKKYVLGNP 335
Cdd:PRK09457 232 FAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 336 L-TPGINQGPQIDKEQHDKILD----LIESGKK---EGAKLECGGGrwgnkgfFVQPTVFsNVTDEMRIAKEEIFGPVQQ 407
Cdd:PRK09457 311 DaEPQPFMGAVISEQAAQGLVAaqaqLLALGGKsllEMTQLQAGTG-------LLTPGII-DVTGVAELPDEEYFGPLLQ 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 408 IMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVV-WVNCYMMLSAQCPFGGFKMSGNGR 476
Cdd:PRK09457 383 VVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHR 452
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
62-492 |
1.93e-68 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 226.23 E-value: 1.93e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 62 KAVKAARQAFQIGspwRTMDASERGRLLNKLADLMERDRLLLatMEALNG--GKVFANAYLSDLGGCIKALKYC----AG 135
Cdd:cd07136 2 SLVEKQRAFFKTG---ATKDVEFRIEQLKKLKQAIKKYENEI--LEALKKdlGKSEFEAYMTEIGFVLSEINYAikhlKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 136 WADKIHGQT----IPSDGdiftYTRREPIGVCGQIIPWNFP-MLMFIWKIGpALSCGNTVVVKPAEQTPLTALHLASLIK 210
Cdd:cd07136 77 WMKPKRVKTpllnFPSKS----YIYYEPYGVVLIIAPWNYPfQLALAPLIG-AIAAGNTAVLKPSELTPNTSKVIAKIIE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 211 EAgFPPGVVNIVPGYGPTAGAAISSHMDvdKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEF 290
Cdd:cd07136 152 ET-FDEEYVAVVEGGVEENQELLDQKFD--YIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 291 AHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGinQGPQIDKEQH-DKILDLIESGKkegakLE 369
Cdd:cd07136 228 IVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESP--DYGRIINEKHfDRLAGLLDNGK-----IV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 370 CGGGrwGNKG-FFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQ 448
Cdd:cd07136 301 FGGN--TDREtLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLS 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1371543638 449 AGVVWVN-CYMML-SAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07136 379 FGGGCINdTIMHLaNPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
63-492 |
2.34e-68 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 225.10 E-value: 2.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 63 AVKAARQAFQIGspwRTMDASERGRLLNKLADLME--RDRLLLATMEALngGKVFANAYLSDLGGCIK----ALKYCAGW 136
Cdd:cd07087 3 LVARLRETFLTG---KTRSLEWRKAQLKALKRMLTenEEEIAAALYADL--GKPPAEAYLTEIAVVLGeidhALKHLKKW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 137 ADKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAgFPP 216
Cdd:cd07087 78 MKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 217 GVVNIVPGyGPTAGAAISSHmDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVF 296
Cdd:cd07087 157 EAVAVVEG-GVEVATALLAE-PFDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 297 YHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGiNQGPQIDKEQHDKILDLIESGKKEGaklecgGGRWG 376
Cdd:cd07087 234 LNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESP-DYGRIINERHFDRLASLLDDGKVVI------GGQVD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 377 NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVNC 456
Cdd:cd07087 307 KEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVND 386
|
410 420 430
....*....|....*....|....*....|....*...
gi 1371543638 457 YMM--LSAQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07087 387 VLLhaAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
24-492 |
2.70e-68 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 236.63 E-value: 2.70e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 24 FINNEWHN----SVSGKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMER 98
Cdd:PRK11904 546 FLEKQWQAgpiiNGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPA---WSRTPVEERAAILERAADLLEA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 99 DR---LLLATMEAlngGKVFANAyLSDLGGCIKALKYCAGWADKIHGQTIPSDGdiFT----YTRREPIGV--CgqIIPW 169
Cdd:PRK11904 623 NRaelIALCVREA---GKTLQDA-IAEVREAVDFCRYYAAQARRLFGAPEKLPG--PTgesnELRLHGRGVfvC--ISPW 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 170 NFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQ 249
Cdd:PRK11904 695 NFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTE 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 250 VGKLIKEA-AGKSNlKRVTL--ELGGKSPCIVFADADL----DIAVEFAhhgvFYHQGQCCVAASRIFVEESVYDEFVKR 322
Cdd:PRK11904 775 TARIINRTlAARDG-PIVPLiaETGGQNAMIVDSTALPeqvvDDVVTSA----FRSAGQRCSALRVLFVQEDIADRVIEM 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 323 SVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEG---AKLECGGGrwGNKGFFVQPTVFSnvTDEMRIAKE 399
Cdd:PRK11904 850 LKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLPAG--TENGHFVAPTAFE--IDSISQLER 925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 400 EIFGPVQQIMKFKS--VDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGvvwvNCYM---MLSA----QcPFGGFK 470
Cdd:PRK11904 926 EVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVG----NVYVnrnQIGAvvgvQ-PFGGQG 1000
|
490 500
....*....|....*....|...
gi 1371543638 471 MSGNG-RELGEHGLYEYTELKTV 492
Cdd:PRK11904 1001 LSGTGpKAGGPHYLLRFATEKTV 1023
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
58-493 |
1.65e-67 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 223.25 E-value: 1.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 58 ADVDKAVKAARQAFQIGspwRTMDASERGRLLNKLADLM-ERDRLLLATMEALNGGKVFaNAYLSDLGG----CIKALKY 132
Cdd:cd07135 5 DEIDSIHSRLRATFRSG---KTKDLEYRLWQLKQLYWAVkDNEEAIVEALKKDLGRPPF-ETLLTEVSGvkndILHMLKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 133 CAGWA-DKIhgqtiPSDGDIF-----TYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLA 206
Cdd:cd07135 81 LKKWAkDEK-----VKDGPLAfmfgkPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 207 SLIKEAgFPPGVVNIVPGYGPTAGAAISSHMdvDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDI 286
Cdd:cd07135 156 ELVPKY-LDPDAFQVVQGGVPETTALLEQKF--DKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 287 AvefAHH---GVFYHQGQCCVAASRIFVEESVYDEFVKRSverakKYVLgNPLTPGINQGPQ-----IDKEQHDKILDLI 358
Cdd:cd07135 232 A---AKRilwGKFGNAGQICVAPDYVLVDPSVYDEFVEEL-----KKVL-DEFYPGGANASPdytriVNPRHFNRLKSLL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 359 ESGKkegAKLECGGGRwGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKD-- 436
Cdd:cd07135 303 DTTK---GKVVIGGEM-DEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDks 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1371543638 437 -LDKAITvsSALQAGVVWVNCYMMLSA-QCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07135 379 eIDHILT--RTRSGGVVINDTLIHVGVdNAPFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
39-486 |
5.79e-58 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 207.90 E-value: 5.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 39 PVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMErdrlllATMEALNG------ 111
Cdd:PRK11809 662 PVINPAdPRDIVGYVREATPAEVEQALESAVNAAPI---WFATPPAERAAILERAADLME------AQMQTLMGllvrea 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 112 GKVFANAyLSDLGGCIKALKYCAGWADkihgqtipsdgDIFTYTRREPIG--VCgqIIPWNFPMLMFIWKIGPALSCGNT 189
Cdd:PRK11809 733 GKTFSNA-IAEVREAVDFLRYYAGQVR-----------DDFDNDTHRPLGpvVC--ISPWNFPLAIFTGQVAAALAAGNS 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 190 VVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIK-------EAAGKSn 262
Cdd:PRK11809 799 VLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQrnlagrlDPQGRP- 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 263 lkrVTL--ELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNP--LTP 338
Cdd:PRK11809 878 ---IPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPdrLST 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 339 GInqGPQIDKEQHDKILDLIESGKKEGAK---LECGGGRWGNKGFFVQPTVFS-NVTDEMriaKEEIFGPVQQIMKFKS- 413
Cdd:PRK11809 955 DI--GPVIDAEAKANIERHIQAMRAKGRPvfqAARENSEDWQSGTFVPPTLIElDSFDEL---KREVFGPVLHVVRYNRn 1029
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371543638 414 -VDDVIKRANNTTYGLAAGLFTKdLDKAIT-VSSALQAGVVWVNCYM---MLSAQcPFGGFKMSGNGRELGehG-LYEY 486
Cdd:PRK11809 1030 qLDELIEQINASGYGLTLGVHTR-IDETIAqVTGSAHVGNLYVNRNMvgaVVGVQ-PFGGEGLSGTGPKAG--GpLYLY 1104
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
3-473 |
2.67e-56 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 195.88 E-value: 2.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 3 SPAQPAVPAPLADLKIQHTKI--FINNE--WhnsvSGKKFPVLNPAT-EEVICHVEEGDKADVDKAVKAARQAfqiGSPW 77
Cdd:cd07123 13 SPERAKLQEALAELKSLTVEIplVIGGKevR----TGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEA---RKEW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 78 RTMDASERGRLLNKLADLME---RDRLLLATMeaLNGGKvfaNAYLSDL-GGC--IKALKYCAGWADKI-HGQTIPSDGD 150
Cdd:cd07123 86 ARMPFEDRAAIFLKAADLLSgkyRYELNAATM--LGQGK---NVWQAEIdAACelIDFLRFNVKYAEELyAQQPLSSPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 151 IFTYTRREPI-GVCGQIIPWNFPmlmfiwKIG------PALsCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVP 223
Cdd:cd07123 161 VWNRLEYRPLeGFVYAVSPFNFT------AIGgnlagaPAL-MGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 224 GYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAGKS-----NLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYH 298
Cdd:cd07123 234 GDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENldryrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 299 QGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKE-GAKLECGGGRWGN 377
Cdd:cd07123 314 QGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 378 KGFFVQPTVFSnVTDEM-RIAKEEIFGPVQQIM-----KFKSVDDVIkraNNTT-YGLAAGLFTKDlDKAI-TVSSALQ- 448
Cdd:cd07123 394 VGYFVEPTVIE-TTDPKhKLMTEEIFGPVLTVYvypdsDFEETLELV---DTTSpYALTGAIFAQD-RKAIrEATDALRn 468
|
490 500
....*....|....*....|....*...
gi 1371543638 449 -AGVVWVN--CYMMLSAQCPFGGFKMSG 473
Cdd:cd07123 469 aAGNFYINdkPTGAVVGQQPFGGARASG 496
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
13-491 |
2.93e-55 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 192.74 E-value: 2.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 13 LADLKIQHTKI--FINNEWhnSVSGKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLN 90
Cdd:PLN02315 11 LSEIGLSSRNLgcYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI---WMQVPAPKRGEIVR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 91 KLADLMERDRLLLATMEALNGGKVFANAyLSDLGGCIKALKYCAGWADKIHGQTIPSD-GDIFTYTRREPIGVCGQIIPW 169
Cdd:PLN02315 86 QIGDALRAKLDYLGRLVSLEMGKILAEG-IGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 170 NFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEA----GFPPGVVNIVPGyGPTAGAAISSHMDVDKVAFT 245
Cdd:PLN02315 165 NFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 246 GSTQVGKLIKEAAgKSNLKRVTLELGGKSPCIVFADADLDIAVE---FAHHGVfyhQGQCCVAASRIFVEESVYDEFVKR 322
Cdd:PLN02315 244 GSSKVGLMVQQTV-NARFGKCLLELSGNNAIIVMDDADIQLAVRsvlFAAVGT---AGQRCTTCRRLLLHESIYDDVLEQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 323 SVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSnVTDEMRIAKEEIF 402
Cdd:PLN02315 320 LLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 403 GPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQA--GVVWVNCYMMlSAQC--PFGGFKMSGNGREL 478
Cdd:PLN02315 399 GPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVNIPTN-GAEIggAFGGEKATGGGREA 477
|
490
....*....|...
gi 1371543638 479 GEHGLYEYTELKT 491
Cdd:PLN02315 478 GSDSWKQYMRRST 490
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
153-495 |
8.18e-54 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 188.70 E-value: 8.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 153 TYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAgFPPGVVNIVPGYGPTAGAA 232
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 233 ISSHMDVdkVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHHGVFYHQGQCCVAASRIFVE 312
Cdd:PTZ00381 182 LKEPFDH--IFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 313 ESVYDEFVKRSVERAKKYVLGNPLTPgiNQGPQIDKEQH-DKILDLIESGKKEGAKlecgGGRWGNKGFFVQPTVFSNVT 391
Cdd:PTZ00381 259 RSIKDKFIEALKEAIKEFFGEDPKKS--EDYSRIVNEFHtKRLAELIKDHGGKVVY----GGEVDIENKYVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 392 DEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVVWVN-CYMMLSAQ-CPFGGF 469
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdCVFHLLNPnLPFGGV 412
|
330 340
....*....|....*....|....*.
gi 1371543638 470 KMSGNGRELGEHGLYEYTELKTVAMK 495
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
62-495 |
2.49e-49 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 175.10 E-value: 2.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 62 KAVKAARQAFQIGspwRTMDASERGRLLNKLADLME--RDRLLLATMEALNggKVFANAYLSDLGGCIK----ALKYCAG 135
Cdd:cd07132 2 EAVRRAREAFSSG---KTRPLEFRIQQLEALLRMLEenEDEIVEALAKDLR--KPKFEAVLSEILLVKNeikyAISNLPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 136 WAdkihgQTIPSDGDIFT-----YTRREPIGVCGQIIPWNFP-MLMFIWKIGpALSCGNTVVVKPAEQTPLTALHLASLI 209
Cdd:cd07132 77 WM-----KPEPVKKNLATllddvYIYKEPLGVVLIIGAWNYPlQLTLVPLVG-AIAAGNCVVIKPSEVSPATAKLLAELI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 210 -----KEAgFPpgVVnivpgygpTAGAAISSHM---DVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFAD 281
Cdd:cd07132 151 pkyldKEC-YP--VV--------LGGVEETTELlkqRFDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 282 ADLDIAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNP-LTPgiNQGPQIDKEQHDKILDLIES 360
Cdd:cd07132 219 CDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPkESP--DYGRIINDRHFQRLKKLLSG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 361 GKKegakleCGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFT---KDL 437
Cdd:cd07132 297 GKV------AIGGQTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSnnkKVI 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 438 DKAITVSSalqAGVVWVNCYMMLSA--QCPFGGFKMSGNGRELGEHGLYEYTELKTVAMK 495
Cdd:cd07132 371 NKILSNTS---SGGVCVNDTIMHYTldSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
64-486 |
3.33e-46 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 166.43 E-value: 3.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 64 VKAARQAFQIGspwRTMDASERGRLLNKLADLM--ERDRLLLATMEALngGKVFANAYLSDLG----GCIKALKYCAGWA 137
Cdd:cd07137 5 VRELRETFRSG---RTRSAEWRKSQLKGLLRLVdeNEDDIFAALRQDL--GKPSAESFRDEVSvlvsSCKLAIKELKKWM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 138 D----KIHGQTIPSDGDIFTytrrEPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAg 213
Cdd:cd07137 80 ApekvKTPLTTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 214 FPPGVVNIVPGyGPTAGAAISSHmDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDIAVEFAHH 293
Cdd:cd07137 155 LDTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 294 GVF-YHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGinQGPQIDKEQHDKILDLIESGKKEGAKLECGG 372
Cdd:cd07137 232 GKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESK--DLSRIVNSHHFQRLSRLLDDPSVADKIVHGG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 373 GRwGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITVSSALQAGVV 452
Cdd:cd07137 310 ER-DEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGV 388
|
410 420 430
....*....|....*....|....*....|....*.
gi 1371543638 453 WVNCYMM--LSAQCPFGGFKMSGNGRelgEHGLYEY 486
Cdd:cd07137 389 TFNDTVVqyAIDTLPFGGVGESGFGA---YHGKFSF 421
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
24-479 |
1.43e-35 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 139.07 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 24 FINNEWHNSvSGKKFPVLNPATEEVICHVEeGDKADVDKAVKAARQafQIGSPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:PRK11903 8 YVAGRWQAG-SGAGTPLFDPVTGEELVRVS-ATGLDLAAAFAFARE--QGGAALRALTYAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 104 ATMEALNGGKVFANAYLsDLGGCIKALKYCAGWADKIHGQTIPSDGD--------------IFTYTRrepiGVCGQIIPW 169
Cdd:PRK11903 84 YDIATANSGTTRNDSAV-DIDGGIFTLGYYAKLGAALGDARLLRDGEavqlgkdpafqgqhVLVPTR----GVALFINAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 170 NFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAG-FPPGVVNIVPGygptAGAAISSH---MDVdkVAFT 245
Cdd:PRK11903 159 NFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG----SSAGLLDHlqpFDV--VSFT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 246 GSTQVGKLIK-EAAGKSNLKRVTLELGGKSPCIVFADADLDIAvEFAhhgVFYHQ---------GQCCVAASRIFVEESV 315
Cdd:PRK11903 233 GSAETAAVLRsHPAVVQRSVRVNVEADSLNSALLGPDAAPGSE-AFD---LFVKEvvremtvksGQKCTAIRRIFVPEAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 316 YDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIEsGKKEGAKLECGGGRWG------NKGFFVQPTVF-- 387
Cdd:PRK11903 309 YDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLga 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 388 SNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKD---LDKAIT-----------VSSALQA---- 449
Cdd:PRK11903 388 SDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDaafLAAAALeladshgrvhvISPDVAAlhtg 467
|
490 500 510
....*....|....*....|....*....|.
gi 1371543638 450 -GVVwvncyMmlsAQCPFGGFKMSGNGRELG 479
Cdd:PRK11903 468 hGNV-----M---PQSLHGGPGRAGGGEELG 490
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
53-486 |
1.58e-35 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 138.32 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 53 EEGDKADVDKAVKAARQAFQIGspwRTMDASERGRLLNKLADLM--ERDRLLLATMEALngGKVFANAYLSDLGGCIKAL 130
Cdd:PLN02203 1 EEAPGETLEGSVAELRETYESG---RTRSLEWRKSQLKGLLRLLkdNEEAIFKALHQDL--GKHRVEAYRDEVGVLTKSA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 131 KY---CAG-WADKIHGQ----TIPSDGDIFTytrrEPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTA 202
Cdd:PLN02203 76 NLalsNLKkWMAPKKAKlplvAFPATAEVVP----EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 203 LHLASLIKeAGFPPGVVNIVPGyGPTAGAAISSHmDVDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIV---F 279
Cdd:PLN02203 152 AFLAANIP-KYLDSKAVKVIEG-GPAVGEQLLQH-KWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdslS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 280 ADADLDIAVEFAHHGVFYH-QGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGinQGPQIDKEQH-DKILDL 357
Cdd:PLN02203 228 SSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESK--SMARILNKKHfQRLSNL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 358 IESGKKEGAKLEcgGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDL 437
Cdd:PLN02203 306 LKDPRVAASIVH--GGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNE 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1371543638 438 DKAITVSSALQAGVVWVNCYMMLSA--QCPFGGFKMSGNGRelgEHGLYEY 486
Cdd:PLN02203 384 KLKRRILSETSSGSVTFNDAIIQYAcdSLPFGGVGESGFGR---YHGKYSF 431
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
24-440 |
7.27e-32 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 128.16 E-value: 7.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 24 FINNEWHNSvSGKKFPVLNPATEEVICHVEeGDKADVDKAVKAARQafqIGSP-WRTMDASERGRLLNKLAD-LMERDRL 101
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYARE---KGGPaLRALTFHERAAMLKALAKyLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 102 LLAtMEALNGGKVFANAYlsDLGGCIKALKYCAGWADK-IHGQTIPSDGDIFTYTRREPI----------GVCGQIIPWN 170
Cdd:cd07128 79 LYA-LSAATGATRRDSWI--DIDGGIGTLFAYASLGRReLPNAHFLVEGDVEPLSKDGTFvgqhiltprrGVAVHINAFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 171 FPmlmfIW----KIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAG-FPPGVVNIVPGygptAGAAISSHMDV-DKVAF 244
Cdd:cd07128 156 FP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG----SVGDLLDHLGEqDVVAF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 245 TGSTQVGKLIKEAAG-KSNLKRVTLELGGKSPCIVFADADLDIAvEFAhhgVFYHQ---------GQCCVAASRIFVEES 314
Cdd:cd07128 228 TGSAATAAKLRAHPNiVARSIRFNAEADSLNAAILGPDATPGTP-EFD---LFVKEvaremtvkaGQKCTAIRRAFVPEA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 315 VYDEFVKRSVERAKKYVLGNPLTPGINQGPQIDKEQHDKILDLIESGKKEgAKLECGG-------GRWGNKGFFVQPTVF 387
Cdd:cd07128 304 RVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGpdrfevvGADAEKGAFFPPTLL 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1371543638 388 -SNVTDEMRIAKE-EIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKA 440
Cdd:cd07128 383 lCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFA 437
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
129-492 |
1.90e-30 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 123.62 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 129 ALKYCAGW----ADKIHGQTIPSDGDIFTytrrEPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALH 204
Cdd:PLN02174 82 ALKQLKNWmapeKAKTSLTTFPASAEIVS----EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 205 LASLIkEAGFPPGVVNIVPGYGPTAGAAISSHMdvDKVAFTGSTQVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADL 284
Cdd:PLN02174 158 LAKLL-EQYLDSSAVRVVEGAVTETTALLEQKW--DKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDTDL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 285 DIAVEFAHHGVF-YHQGQCCVAASRIFVEESVYDEFVKRSVERAKKYVLGNPLTPGiNQGPQIDKEQHDKILDLIEsgKK 363
Cdd:PLN02174 234 KVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLD--EK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 364 EGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSVDDVIKRANNTTYGLAAGLFTKDLDKAITV 443
Cdd:PLN02174 311 EVSDKIVYGGEKDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERF 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1371543638 444 SSALQAGVVWVNCYMMLSA--QCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PLN02174 391 AATVSAGGIVVNDIAVHLAlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
60-436 |
9.64e-27 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 112.33 E-value: 9.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 60 VDKAVKAARQAfqiGSPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGGKvfANAYLSDLGGCIKALKYCA--GWA 137
Cdd:cd07084 1 PERALLAADIS---TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGK--GWMFAENICGDQVQLRARAfvIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 138 DKIH---GQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAG- 213
Cdd:cd07084 76 YRIPhepGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 214 FPPGVVNIVPGYGPTaGAAISSHMDVDKVAFTGSTQVG-KLIKEAAgksnLKRVTLELGGKSPCIVFADADL--DIAVEF 290
Cdd:cd07084 156 LPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAeKLALDAK----QARIYLELAGFNWKVLGPDAQAvdYVAWQC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 291 AHHGVFYhQGQCCVAASRIFVEES-----VYDEfVKRSVERAKkyVLGNPLTPGI--NQGPQIDKEQHDKILDLIESGKK 363
Cdd:cd07084 231 VQDMTAC-SGQKCTAQSMLFVPENwsktpLVEK-LKALLARRK--LEDLLLGPVQtfTTLAMIAHMENLLGSVLLFSGKE 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371543638 364 EGAKlecggGRWGNKGFFVQPTVFSNVTDEMRIAK---EEIFGPVQQIMKFK--SVDDVIKRANNTTYGLAAGLFTKD 436
Cdd:cd07084 307 LKNH-----SIPSIYGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKkdQLALVLELLERMHGSLTAAIYSND 379
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
60-422 |
1.93e-16 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 81.43 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 60 VDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLME--RDRLLLATM------EALNGG---------KVFANAYLSD 122
Cdd:cd07129 1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEalGDELVARAHaetglpEARLQGelgrttgqlRLFADLVREG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 123 lggcikalkycaGWADKI------HGQTIPSdGDIftYTRREPIGVCGQIIPWNFPmLMFIWKIG---PALSCGNTVVVK 193
Cdd:cd07129 78 ------------SWLDARidpadpDRQPLPR-PDL--RRMLVPLGPVAVFGASNFP-LAFSVAGGdtaSALAAGCPVVVK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 194 PAEQTPLTALHLASLI----KEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKLIKEAAgksnLKR---- 265
Cdd:cd07129 142 AHPAHPGTSELVARAIraalRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAA----AARpepi 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 266 -VTLELGGKSPCIVFADAdL-----DIAVEFAHH---GVfyhqGQCCVAASRIFVEESV-YDEFVKRSVERAKKYVLGNP 335
Cdd:cd07129 218 pFYAELGSVNPVFILPGA-LaergeAIAQGFVGSltlGA----GQFCTNPGLVLVPAGPaGDAFIAALAEALAAAPAQTM 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 336 LTPGINQGPQIDKEQ---HDKILDLIESGKKEGaklecgggrwgnkGFFVQPTVFsnVTDEMRIAK-----EEIFGPVQQ 407
Cdd:cd07129 293 LTPGIAEAYRQGVEAlaaAPGVRVLAGGAAAEG-------------GNQAAPTLF--KVDAAAFLAdpalqEEVFGPASL 357
|
410
....*....|....*
gi 1371543638 408 IMKFKSVDDVIKRAN 422
Cdd:cd07129 358 VVRYDDAAELLAVAE 372
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
60-357 |
9.88e-16 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 78.80 E-value: 9.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 60 VDKAVKAARQA-FQIGSPWRTMDASERGRLLNKLADLMERdRLLLATmealngGKVFANAYlsdlggcikALKYCAGWAD 138
Cdd:cd07077 18 RDLIINAIANAlYDTRQRLASEAVSERGAYIRSLIANWIA-MMGCSE------SKLYKNID---------TERGITASVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 139 KIHGQTIPSDGDifTYTRREPIGVCGQIIPWNFPMLMfIWKIGPALSCGNTVVVKPAEQTPLTAlHLASLIKEAGFPPGV 218
Cdd:cd07077 82 HIQDVLLPDNGE--TYVRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTN-RALALLFQAADAAHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 219 VNIVPGYGPTAGAAIS----SHMDVDKVAFTGSTQVgklIKEAAGKSNLKRVTLELGGKSPCIVFADADLDIAVEFAHHG 294
Cdd:cd07077 158 PKILVLYVPHPSDELAeellSHPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371543638 295 VFYHQGQCCVAASRIFVE---ESVYDEFVKRSVErAKKYVLGNPLTPGINQGPQIDKEQHDKILDL 357
Cdd:cd07077 235 KFFDQNACASEQNLYVVDdvlDPLYEEFKLKLVV-EGLKVPQETKPLSKETTPSFDDEALESMTPL 299
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
157-436 |
3.19e-08 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 55.96 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 157 REPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEAGFPPGVVNIVPGYGPTAGAAISSh 236
Cdd:cd07126 140 RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 237 MDVDKVAFTGSTQVG-KLIKEAAGKsnlkrVTLELGGKSPCIVFAD-ADLDIAVEFAHHGVFYHQGQCCVAASRIFVEES 314
Cdd:cd07126 219 ANPRMTLFTGSSKVAeRLALELHGK-----VKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHEN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 315 -VYDEFVKRSVERAKKYVLGNpLT--PGINQGPQIDKEQHDKILDLiesgkkEGAKLECGGGRWGNKGF-----FVQPT- 385
Cdd:cd07126 294 wVQAGILDKLKALAEQRKLED-LTigPVLTWTTERILDHVDKLLAI------PGAKVLFGGKPLTNHSIpsiygAYEPTa 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1371543638 386 VF-----SNVTDEMRIAKEEIFGPVQQIMKFK--SVDDVIKRANNTTYGLAAGLFTKD 436
Cdd:cd07126 367 VFvpleeIAIEENFELVTTEVFGPFQVVTEYKdeQLPLVLEALERMHAHLTAAVVSND 424
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
58-335 |
2.60e-07 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 53.01 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 58 ADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADlMERDRL-LLATMEALNGG------KVFANAYLSDLGGCIKAL 130
Cdd:cd07121 4 ATVDDAVAAAKAAQKQ---YRKCTLADREKIIEAIRE-ALLSNAeELAEMAVEETGmgrvedKIAKNHLAAEKTPGTEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 131 KYCAGWADkiHGQTIpsdgdiftyTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKP---AEQTPLTALHLAS 207
Cdd:cd07121 80 TTTAWSGD--NGLTL---------VEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKVSAYAVELIN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 208 -LIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTQVGKlikeAAGKSNlKRVTLELGGKSPCIVFADADLDI 286
Cdd:cd07121 149 kAIAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVK----AALSSG-KKAIGAGAGNPPVVVDETADIEK 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1371543638 287 AVEFAHHGVFYHQGQCCVAASRIFVEESVYDEFvKRSVERAKKYVLGNP 335
Cdd:cd07121 224 AARDIVQGASFDNNLPCIAEKEVIAVDSVADYL-IAAMQRNGAYVLNDE 271
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
56-455 |
3.49e-07 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 52.87 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 56 DKADVDKAVKAARQAFQigsPWRtmDASERGR------LLNKLADL-MERDRLLLAT-----MEALNGGkvfaNAYLSDL 123
Cdd:cd07127 82 PQCDPDALLAAARAAMP---GWR--DAGARARagvcleILQRLNARsFEMAHAVMHTtgqafMMAFQAG----GPHAQDR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 124 GgcIKALKYCAGWADKIHGQTI---PSDG-DIFTYTRR---EPIGV-----CGQIIPWN-FPMLMfiwkigPALSCGNTV 190
Cdd:cd07127 153 G--LEAVAYAWREMSRIPPTAEwekPQGKhDPLAMEKTftvVPRGValvigCSTFPTWNgYPGLF------ASLATGNPV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 191 VVKPAeqtPLTALHLASLIK-------EAGFPPGVVNIV--PGYGPTAGaAISSHMDVDKVAFTGSTQVGKLIKEAAGKs 261
Cdd:cd07127 225 IVKPH---PAAILPLAITVQvarevlaEAGFDPNLVTLAadTPEEPIAQ-TLATRPEVRIIDFTGSNAFGDWLEANARQ- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 262 nlKRVTLELGGKSPCIVFADADL-----DIAVEFAhhgvfYHQGQCCVAASRIFV---------EESVYDEfVKRSVERA 327
Cdd:cd07127 300 --AQVYTEKAGVNTVVVDSTDDLkamlrNLAFSLS-----LYSGQMCTTPQNIYVprdgiqtddGRKSFDE-VAADLAAA 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 328 KKYVLGNP-----LTPGInqgpqidkeQHDKILDLIESGKKEGAKLECGGGRwGNKGF---FVQPTVFSNVTDEMRIA-K 398
Cdd:cd07127 372 IDGLLADParaaaLLGAI---------QSPDTLARIAEARQLGEVLLASEAV-AHPEFpdaRVRTPLLLKLDASDEAAyA 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 399 EEIFGPVQQIMKFKSVDDVIKRANNT--TYG-LAAGLFTKDLDKA-ITVSSALQAGV---------VWVN 455
Cdd:cd07127 442 EERFGPIAFVVATDSTDHSIELARESvrEHGaMTVGVYSTDPEVVeRVQEAALDAGValsinltggVFVN 511
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
60-476 |
3.84e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 52.27 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 60 VDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMEALNGG----------KVFANAYLSDlggcika 129
Cdd:cd07081 1 LDDAVAAAKVAQQ---GLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGmgrvedkvikNHFAAEYIYN------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 130 lKYCagwaDKIHGQTIPSDGDIFTYTRREPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKP----AEQTPLTALHL 205
Cdd:cd07081 71 -VYK----DEKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 206 ASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGstqvGKLIKEAAGKSNlKRVTLELGGKSPCIVFADADLD 285
Cdd:cd07081 146 LQAAVAAGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSG-KPAIGVGAGNTPVVIDETADIK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 286 IAVEFAHHGVFYHQGQCCVAASRIFVEESVYDEfVKRSVERAKKYVLgnpltpginqgpqiDKEQHDKILDLIesgKKEG 365
Cdd:cd07081 221 RAVQSIVKSKTFDNGVICASEQSVIVVDSVYDE-VMRLFEGQGAYKL--------------TAEELQQVQPVI---LKNG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 366 AKLECGGGRWGNK-----GFFVQPT---VFSNVT--DEMRIAKEEIFGPVQQIMKFKSVDDVIKRA----NNTTYGLAAG 431
Cdd:cd07081 283 DVNRDIVGQDAYKiaaaaGLKVPQEtriLIGEVTslAEHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSA 362
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1371543638 432 LFT---KDLDKAITVSSALQAGVVWVNcymmlsAQCPFGGFKMSGNGR 476
Cdd:cd07081 363 MYSdniKAIENMNQFANAMKTSRFVKN------GPCSQGGLGDLYNFR 404
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
58-357 |
4.90e-07 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 52.21 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 58 ADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMEALNGG------KVFANAYLSDLGGCIKALK 131
Cdd:PRK15398 36 ASVDDAVAAAKVAQQR---YQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmgrvedKIAKNVAAAEKTPGVEDLT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 132 YCAGWADkiHGQTIpsdgdiFTYTrrePIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKP---AEQTPLTALHLAS- 207
Cdd:PRK15398 113 TEALTGD--NGLTL------IEYA---PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgAKKVSLRAIELLNe 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 208 LIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGstqvGKLIKEAAGKSNlKRVTLELGGKSPCIVFADADLDIA 287
Cdd:PRK15398 182 AIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTG----GPAVVKAAMKSG-KKAIGAGAGNPPVVVDETADIEKA 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 288 VEFAHHGVFYHQGQCCVAASRIFVEESVYDEFVkRSVERAKKYvlgnpltpginqgpQIDKEQHDKILDL 357
Cdd:PRK15398 257 ARDIVKGASFDNNLPCIAEKEVIVVDSVADELM-RLMEKNGAV--------------LLTAEQAEKLQKV 311
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
154-417 |
3.18e-06 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 49.36 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 154 YTRREPIGVCGQIIPWNFPMLMFiWKIGPALSCGNTVVVKPAEQTP-LTALHLASLIK--EAGFPPGVVNIVPGYGPTAG 230
Cdd:pfam05893 83 YEKAFPPGLVFHVLSGNVPLLPV-MSILMGLLVKNVNLLKVSSSDPfTAAALLASFADldPTHPLADSLSVVYWDGGSTQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 231 AAISSHMDVDKVAFTGSTQVGKLIKEAAGKSnlKRVTLELGGKSPCIVFADADLDIAVEFAHHGV-FYHQgQCCVAASRI 309
Cdd:pfam05893 162 LEDLIVANADVVIAWGGEDAINAIRECLKPG--KQWIDFGAKISFAVVDREAALDKAAERAADDIcVFDQ-QACLSPQTV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 310 FVE---ESVYDEFVKRSVERAKKYVLGNP-LTPGINQGPQI--DKEQHDKILDLIESGKKEGAKlecgGGRWgnkgffvq 383
Cdd:pfam05893 239 FVEsddKITPDEFAERLAAALAKRARILPkAVLDIDEAAKIssDRAECKLDYAFAGERGVWSDF----HQRW-------- 306
|
250 260 270
....*....|....*....|....*....|....*
gi 1371543638 384 pTV-FSNvtdemriAKEEIFGPVQQIMKFKSVDDV 417
Cdd:pfam05893 307 -TViWSD-------GQEELNSPLNRTVNVVPVPSL 333
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
158-456 |
1.83e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 47.10 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 158 EPIGVCGQIIPWNFPMLMFIWKIGPALSCGNTVVVKPAEQTPLTALHLASLIKEA----GFPPGVVNIVPgyGPT--AGA 231
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIE--EPSieLTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 232 AISSHMDVDKVAFTGStqvGKLIKEA--AGKSNlkrvtleLG---GKSPCIVFADADLDIAVE-------FAHhgvfyhq 299
Cdd:cd07122 172 ELMKHPDVDLILATGG---PGMVKAAysSGKPA-------IGvgpGNVPAYIDETADIKRAVKdiilsktFDN------- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 300 GQCCVAASRIFVEESVYDEFVKRsVERAKKYVLgnpltpginqgpqiDKEQHDKILDLIesgkkegakLECGGGRwgNK- 378
Cdd:cd07122 235 GTICASEQSVIVDDEIYDEVRAE-LKRRGAYFL--------------NEEEKEKLEKAL---------FDDGGTL--NPd 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 379 -------------GFFVQPTV------FSNVTDEMRIAKEEIFgPVQQIMKFKSVDDVIKRAN-NTTYGLA---AGLFTK 435
Cdd:cd07122 289 ivgksaqkiaelaGIEVPEDTkvlvaeETGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKAReLLEYGGAghtAVIHSN 367
|
330 340
....*....|....*....|.
gi 1371543638 436 DLDKAITVSSALQAGVVWVNC 456
Cdd:cd07122 368 DEEVIEEFALRMPVSRILVNT 388
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
154-314 |
2.83e-04 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 43.42 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 154 YTRREPIGVCGQIIPWNFPMLMFiWKIGPALSCGNTVVVKPAEQTPLTALHLA-SLIKEAGFPPGVVNI----VPGYGPT 228
Cdd:cd07080 107 YIRAQPRGLVVHIIAGNVPLLPV-WSIVRGLLVKNVNLLKMSSSDPLTATALLrSLADVDPNHPLTDSIsvvyWPGGDAE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371543638 229 AGAAISSHMDVdKVAFTGSTQVgKLIKEAAGKSnlKRvTLELGGK-SPCIV----FADADL-DIAVEFAHHGVFYHQgQC 302
Cdd:cd07080 186 LEERILASADA-VVAWGGEEAV-KAIRSLLPPG--CR-LIDFGPKySFAVIdreaLESEKLaEVADALAEDICRYDQ-QA 259
|
170
....*....|..
gi 1371543638 303 CVAASRIFVEES 314
Cdd:cd07080 260 CSSPQVVFVEKD 271
|
|
| DUF1487 |
pfam07368 |
Protein of unknown function (DUF1487); This family consists of several uncharacterized ... |
273-335 |
2.27e-03 |
|
Protein of unknown function (DUF1487); This family consists of several uncharacterized proteins from Drosophila melanogaster. The function of this family is unknown.
Pssm-ID: 254173 Cd Length: 215 Bit Score: 39.66 E-value: 2.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371543638 273 KSPC--IVFADADLDIAVEFAHHGVfyHQGQCCVAASRIFVEESVYDEFVKR---SVERAKKYVLGNP 335
Cdd:pfam07368 3 NSPRlmVIFEDGDVNSALHALVESL--HNPFAPGAVATVLVQESIRDEFVERvrsRLKPLSERVANHP 68
|
|
| |
