|
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 ... |
26-506 |
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: 951.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 26 NLEVKFTKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSPWRRLDALSRGQLLHQLAD 105
Cdd:cd07141 1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 106 LVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLL 185
Cdd:cd07141 81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 186 MLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLV 265
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 266 REAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGD 345
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 346 PFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNL 425
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 426 EEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
.
gi 170650621 506 K 506
Cdd:cd07141 481 K 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
32-505 |
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: 844.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 32 TKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSpWRRLDALSRGQLLHQLADLVERDR 111
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 112 AILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKL 191
Cdd:cd07091 83 DELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 192 APALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASR 271
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 272 SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKT 351
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 352 EQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKR 431
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170650621 432 ANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07091 403 ANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
29-503 |
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: 703.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 29 VKFTKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVE 108
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 109 RDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLA 188
Cdd:cd07142 80 KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 189 WKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREA 268
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 269 ASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFD 348
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 349 AKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEV 428
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170650621 429 IKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
32-507 |
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: 688.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 32 TKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDR 111
Cdd:COG1012 6 YPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 112 AILATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWK 190
Cdd:COG1012 83 EELAALLTLETGKPLAEARG-EVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 191 LAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAAS 270
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 271 RsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAK 350
Cdd:COG1012 242 E-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 351 TEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMED-RGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVI 429
Cdd:COG1012 321 TDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170650621 430 KRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFY-AQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
45-503 |
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: 679.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 45 SGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGK 124
Cdd:pfam00171 5 ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELETLENGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 125 PFLHAFFvDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLK 204
Cdd:pfam00171 82 PLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 205 PAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGK 284
Cdd:pfam00171 161 PSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 285 NPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDK 364
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 365 ILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVF 444
Cdd:pfam00171 320 VLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVF 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 445 TKNLDKALKLAAALESGTVWINCYNAFYA-QAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:pfam00171 400 TSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
32-507 |
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: 677.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 32 TKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgSPWRR-LDALSRGQLLHQLADLVERD 110
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWGLkVSGSKRGRCLSKLADLMERN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 111 RAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWK 190
Cdd:cd07143 85 LDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 191 LAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAAS 270
Cdd:cd07143 165 IAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 271 RSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAK 350
Cdd:cd07143 245 KSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 351 TEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIK 430
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170650621 431 RANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
19-512 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 677.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 19 ALPRPIR-NLEVKFTKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRG 97
Cdd:PLN02466 44 AVEEPITpPVQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTAYERS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 98 QLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAI 177
Cdd:PLN02466 123 RILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 178 TPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTG 257
Cdd:PLN02466 203 IPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 258 STEVGKLVREAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEF 337
Cdd:PLN02466 283 STDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKAR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 338 AKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQ 417
Cdd:PLN02466 363 ALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQ 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 418 PILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEY 497
Cdd:PLN02466 443 SILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNY 522
|
490
....*....|....*
gi 170650621 498 TEVKTVTIKLeeKNP 512
Cdd:PLN02466 523 LQVKAVVTPL--KNP 535
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
32-507 |
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: 663.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 32 TKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgSPWRRLDALSRGQLLHQLADLVERDR 111
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 112 AILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKL 191
Cdd:cd07144 86 DLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 192 APALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASr 271
Cdd:cd07144 166 APALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 272 SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKR-PVGDPFDAK 350
Cdd:cd07144 245 QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 351 TEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMED---RGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEE 427
Cdd:cd07144 325 TVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 428 VIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07144 405 AIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHINL 484
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
72-505 |
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: 630.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 72 DKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFFVDLEGCIKTFRYFAGWADKI 151
Cdd:cd07078 1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 152 QGRTIPTDD-NVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVV 230
Cdd:cd07078 77 HGEVIPSPDpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 231 NIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQ 310
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 311 GQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAME-DR 389
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEgGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 390 GLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYN 469
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 170650621 470 AF-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07078 396 VGaEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
35-510 |
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: 616.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVERDRAIL 114
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSG-EWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 115 ATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPA 194
Cdd:cd07119 80 ARLETLNTGKTLRESEI-DIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 195 LCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNL 274
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQG 354
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 355 PQIDQKQFDKILELIESGKKEGAKLECGGSAMED----RGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIK 430
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 431 RANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLEEK 510
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLSPQ 477
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
28-507 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 607.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 28 EVKFTKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLV 107
Cdd:PLN02766 17 EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 108 ERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLML 187
Cdd:PLN02766 96 EEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 188 AWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVRE 267
Cdd:PLN02766 176 FMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 268 AASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPF 347
Cdd:PLN02766 256 AAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 348 DAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEE 427
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 428 VIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPL 495
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
46-505 |
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: 600.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 46 GRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSpWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKP 125
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 126 FLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKP 205
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 206 AEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRSNLKRVTLELGGKN 285
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 286 PCIVCADA-DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDK 364
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 365 ILELIESGKKEGAKLECGGSA--MEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAA 442
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 170650621 443 VFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
51-505 |
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: 594.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 51 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFqRGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAF 130
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAF-EGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKL-IRET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 131 FVDLEGCIKTFRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQT 209
Cdd:cd07114 79 RAQVRYLAEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 210 PLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIV 289
Cdd:cd07114 159 PASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 290 CADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELI 369
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 370 ESGKKEGAKLECGGSAME----DRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFT 445
Cdd:cd07114 318 ARAREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 446 KNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07114 398 RDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
51-507 |
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: 579.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 51 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF 130
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 131 FVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTP 210
Cdd:cd07115 78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 211 LTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASrSNLKRVTLELGGKNPCIVC 290
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIE 370
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 371 SGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDK 450
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 170650621 451 ALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
51-505 |
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: 578.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 51 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF 130
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG---WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 131 FVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTP 210
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 211 LTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVC 290
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIE 370
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 371 SGKKEGAKLECGGSAME----DRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTK 446
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 170650621 447 NLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
28-506 |
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: 570.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 28 EVKF-TKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADL 106
Cdd:cd07140 1 TLKMpHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENG-EWGKMNARDRGRLMYRLADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 107 VERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTD----DNVVCFTRHEPIGVCGAITPWNF 182
Cdd:cd07140 80 MEEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 183 PLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVG 262
Cdd:cd07140 160 PLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 263 KLVREAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRP 342
Cdd:cd07140 240 KHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 343 VGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKF 422
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 423 KN--LEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEV 500
Cdd:cd07140 400 DDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKT 479
|
....*.
gi 170650621 501 KTVTIK 506
Cdd:cd07140 480 KTVTIE 485
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
52-505 |
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: 543.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFf 131
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 132 VDLEGCIKTFRYFAGWADKIQGRTIPTDD-NVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTP 210
Cdd:cd07103 78 GEVDYAASFLEWFAEEARRIYGRTIPSPApGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 211 LTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASrSNLKRVTLELGGKNPCIVC 290
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIE 370
Cdd:cd07103 237 DDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 371 SGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDK 450
Cdd:cd07103 317 DAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 170650621 451 ALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07103 397 AWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
33-507 |
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: 537.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 33 KIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRA 112
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT---WGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 113 ILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLA 192
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 193 PALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRs 272
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 273 NLKRVTLELGGKNPCIVCADA-----DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPF 347
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 348 DAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGG----SAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFK 423
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGerltLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 424 NLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
....
gi 170650621 504 TIKL 507
Cdd:cd07559 477 LVSY 480
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
34-504 |
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: 530.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 34 IFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAF---QRGSPWRRLDALSRgqllhqLADLVERD 110
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFpawSATSVEERAALLER------IAEAYEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 111 RAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVcftrHEPIGVCGAITPWNFPLLMLAWK 190
Cdd:cd07138 75 ADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEERRGNSLVV----REPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 191 LAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAAS 270
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 271 RSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAK 350
Cdd:cd07138 231 DT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 351 TEQGPQIDQKQFDKILELIESGKKEGAKLECGGS---AMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEE 427
Cdd:cd07138 310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170650621 428 VIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINcYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
35-509 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 519.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLV-ERDRAi 113
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERNDE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 114 LATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAP 193
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 194 ALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPtVGAAISSHPQINKIAFTGSTEVGKLVREAASRSn 273
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 274 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQ 353
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 354 GPQIDQKQFDKILELIESGKKEGAKLECGGSAME----DRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVI 429
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTeggfANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 430 KRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLEE 509
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEMGP 483
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
51-503 |
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: 519.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 51 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF 130
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 131 fVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTP 210
Cdd:cd07090 78 -VDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 211 LTALYLASLIKEVGFPPGVVNIVPGFGPTvGAAISSHPQINKIAFTGSTEVGKLVREAASrSNLKRVTLELGGKNPCIVC 290
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIE 370
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 371 SGKKEGAKLECGGS--AMED---RGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFT 445
Cdd:cd07090 315 SAKQEGAKVLCGGErvVPEDgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 170650621 446 KNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
52-505 |
0e+00 |
|
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: 516.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF 131
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG---WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 132 vDLEGCIKTFRYFAGWAdkIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPL 211
Cdd:cd07106 79 -EVGGAVAWLRYTASLD--LPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 212 TALYLASLIKEVgFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASrSNLKRVTLELGGKNPCIVCA 291
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 292 DADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIES 371
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 372 GKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKA 451
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 170650621 452 LKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
35-501 |
5.97e-178 |
|
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: 508.20 E-value: 5.97e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAIL 114
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGE---WAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 115 ATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPA 194
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 195 LCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASrSNL 274
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQG 354
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 355 PQIDQKQFDKILELIESGKKEGAKLECGGSAME----DRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIK 430
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPEnvglQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170650621 431 RANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVK 501
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
65-505 |
7.18e-178 |
|
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: 507.65 E-value: 7.18e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 65 EGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYF 144
Cdd:cd07118 15 EGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQAR-GEIEGAADLWRYA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 145 AGWADKIQGRTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 223
Cdd:cd07118 93 ASLARTLHGDSYNNlGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 224 GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAH 303
Cdd:cd07118 173 GLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFADADLDAAADAVV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 304 QGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGG 383
Cdd:cd07118 252 FGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 384 SAMEDR-GLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGT 462
Cdd:cd07118 332 ERLASAaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGT 411
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 170650621 463 VWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07118 412 VWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
76-505 |
1.05e-177 |
|
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: 503.69 E-value: 1.05e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 76 EAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFFVDLEGCIKTFRYFAGWADKIQGRT 155
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKP-IEEALGEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 156 IP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVP 234
Cdd:cd06534 77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 235 GFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCC 314
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 315 TAASRVFVEEQVYGEFVRRSVefakkrpvgdpfdakteqgpqidqkqfdkileliesgkkegaklecggsamedrglfik 394
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 395 pTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFY-A 473
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVgP 335
|
410 420 430
....*....|....*....|....*....|..
gi 170650621 474 QAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
33-507 |
4.04e-177 |
|
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: 506.61 E-value: 4.04e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 33 KIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRA 112
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT---WRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 113 ILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLA 192
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 193 PALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRs 272
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 273 NLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTE 352
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 353 QGPQIDQKQFDKILELIESGKKEGAKLECGG----SAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEV 428
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGhrltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170650621 429 IKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
52-505 |
3.66e-176 |
|
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: 503.31 E-value: 3.66e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFf 131
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESG--WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 132 VDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPL 211
Cdd:cd07109 79 ADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 212 TALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCA 291
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 292 DADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGdPFDAKTEQGPQIDQKQFDKILELIES 371
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 372 GKKEGAKLECGGSAMEDR---GLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNL 448
Cdd:cd07109 317 ARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 449 DKALKLAAALESGTVWINCYnaFYA---QAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNY--GAGggiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
51-504 |
7.52e-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: 7.52e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 51 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAF 130
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR---WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKP-LDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 131 FVDLEGCIKTFRYFAGWADKI---QGRTIPTDDN-VVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPA 206
Cdd:cd07110 77 AWDVDDVAGCFEYYADLAEQLdakAERAVPLPSEdFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 207 EQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNP 286
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKIL 366
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 367 ELIESGKKEGAKLECGGSAME--DRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVF 444
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 445 TKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
35-505 |
2.57e-175 |
|
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: 501.80 E-value: 2.57e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAIL 114
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAA-QKA--WERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 115 ATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAP 193
Cdd:cd07088 78 AKLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDrPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 194 ALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsN 273
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-N 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 274 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQ 353
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 354 GPQIDQKQFDKILELIESGKKEGAKLECGGSAME-DRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRA 432
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 170650621 433 NSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
35-503 |
1.01e-174 |
|
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: 500.24 E-value: 1.01e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWHESKSGRkfATYNPSTL-EKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAI 113
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSDTsDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 114 LATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWADKIQGRTIP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLA 192
Cdd:cd07097 79 LARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 193 PALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASrS 272
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 273 NLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTE 352
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 353 QGPQIDQKQFDKILELIESGKKEGAKLECGGSA--MEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIK 430
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170650621 431 RANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYA-QAPFGGFKMSGNG-RELGEYALAEYTEVKTV 503
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDyHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
52-505 |
1.87e-172 |
|
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: 493.77 E-value: 1.87e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF 131
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPS---WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 132 VDLEGCIKTFRYFAGWADKIQGRT----IPtddNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAE 207
Cdd:cd07092 79 DELPGAVDNFRFFAGAARTLEGPAageyLP---GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 208 QTPLTALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPC 287
Cdd:cd07092 156 TTPLTTLLLAELAAEV-LPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILE 367
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 368 LIEsGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKN 447
Cdd:cd07092 314 FVE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 170650621 448 LDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
31-508 |
1.53e-169 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 487.11 E-value: 1.53e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 31 FTKIFINNDWhESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERD 110
Cdd:PRK13473 2 QTKLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE---WSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 111 RAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTipTDDNVVCFT---RHEPIGVCGAITPWNFPLLML 187
Cdd:PRK13473 78 ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKA--AGEYLEGHTsmiRRDPVGVVASIAPWNYPLMMA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 188 AWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVRE 267
Cdd:PRK13473 156 AWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 268 AASRSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPF 347
Cdd:PRK13473 235 AAADS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 348 DAKTEQGPQIDQKQFDKILELIESGKKEG-AKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLE 426
Cdd:PRK13473 314 DEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 427 EVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
|
..
gi 170650621 507 LE 508
Cdd:PRK13473 474 HT 475
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
35-505 |
4.59e-169 |
|
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: 486.08 E-value: 4.59e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWHESKSGRKFATYNPSTLEKIC-EVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAI 113
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVVgTFPLSTASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 114 LATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLA 192
Cdd:cd07131 79 LARLVTREMGKPLAEGR-GDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 193 PALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRS 272
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 273 NlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTE 352
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 353 QGPQIDQKQFDKILELIESGKKEGAKLECGGSAME----DRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEV 428
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTgggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 429 IKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWIN--CYNAfYAQAPFGGFKMSGNG-RELGEYALAEYTEVKTVTI 505
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIGA-EVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
52-503 |
2.36e-166 |
|
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: 478.66 E-value: 2.36e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRlDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF 131
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTG-DWST-DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 132 VDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVC-----FTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPA 206
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEFDLPVPALRGgpgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 207 EQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNP 286
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKIL 366
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 367 ELIESGKKEGAKLECGGSAME--DRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVF 444
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAglDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 170650621 445 TKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
19-504 |
1.14e-165 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 478.46 E-value: 1.14e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 19 ALPRPIRNLevkftkiFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQR--GSPWRRLDALSR 96
Cdd:PLN02467 2 AIPVPRRQL-------FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkGKDWARTTGAVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 97 GQLLHQLADLVERDRAILATLETMDTGKPFLHAFF--VDLEGCiktFRYFAGWADKIQGR-----TIPtDDNVVCFTRHE 169
Cdd:PLN02467 75 AKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWdmDDVAGC---FEYYADLAEALDAKqkapvSLP-METFKGYVLKE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 170 PIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQ 249
Cdd:PLN02467 151 PLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 250 INKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGE 329
Cdd:PLN02467 231 VDKIAFTGSTATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 330 FVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMED--RGLFIKPTVFSDVTDNMRI 407
Cdd:PLN02467 310 FLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 408 AKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGR 487
Cdd:PLN02467 390 WREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGR 469
|
490
....*....|....*..
gi 170650621 488 ELGEYALAEYTEVKTVT 504
Cdd:PLN02467 470 ELGEWGLENYLSVKQVT 486
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
70-505 |
1.80e-165 |
|
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: 475.10 E-value: 1.80e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 70 DVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWAD 149
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAF-EVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 150 KIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLmLAWK-LAPALCCGNTVVLKPAEQTPLT-ALYLASLIKEVGFP 226
Cdd:cd07104 77 RPEGEILPSDvPGKESMVRRVPLGVVGVISPFNFPLI-LAMRsVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 227 PGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGV 306
Cdd:cd07104 156 KGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 307 FFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAm 386
Cdd:cd07104 235 FLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 387 edRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWIN 466
Cdd:cd07104 314 --EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIN 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 170650621 467 CYNAF-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07104 392 DQTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
34-505 |
2.66e-164 |
|
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: 473.60 E-value: 2.66e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 34 IFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVERDRAI 113
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 114 LATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADK---IQGRTIPTDDNVVcfTRHEPIGVCGAITPWNFPLLMLAWK 190
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDfpfEERRPGSGGGHVL--VRREPVGVVAAIVPWNAPLFLAALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 191 LAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVREAAS 270
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 271 RsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAK 350
Cdd:cd07139 237 E-RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 351 TEQGPQIDQKQFDKILELIESGKKEGAKLECGGS--AMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEV 428
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170650621 429 IKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAqAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFG-APFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
51-507 |
5.18e-164 |
|
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: 472.63 E-value: 5.18e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 51 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAF 130
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE---WRATTPLERARMLRELATRLREHAEELALIDALDCGNP-VSAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 131 FVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTP 210
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 211 LTALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRSnLKRVTLELGGKNPCIVC 290
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 291 ADADLDLAVECAHQGVFFN-QGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELI 369
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 370 ESGKKEGAKLECGGSAMED----RGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFT 445
Cdd:cd07107 315 DSAKREGARLVTGGGRPEGpaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170650621 446 KNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
53-505 |
4.65e-162 |
|
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: 467.61 E-value: 4.65e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 53 NPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFV 132
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 133 DLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLT 212
Cdd:cd07108 80 EAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 213 ALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLV-REAASRsnLKRVTLELGGKNPCIVCA 291
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIyRAAADR--LIPVSLELGGKSPMIVFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 292 DADLDLAVECAHQGV-FFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIE 370
Cdd:cd07108 237 DADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 371 SGKKE-GAKLECGGSAMED----RGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFT 445
Cdd:cd07108 317 LGLSTsGATVLRGGPLPGEgplaDGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170650621 446 KNLDKALKLAAALESGTVWIncyNAFYAQAP---FGGFKMSGNGRELG-EYALAEYTEVKTVTI 505
Cdd:cd07108 397 RDLGRALRAAHALEAGWVQV---NQGGGQQPgqsYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
35-497 |
7.32e-162 |
|
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: 468.03 E-value: 7.32e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAIL 114
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES---WSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 115 ATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQgrtipTDdnvvcFTRHEPIGVCGAITPWNFPLLMLAWKLAPA 194
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLD-----TE-----LAGWKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 195 LCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRSNl 274
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTG- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQG 354
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 355 PQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANS 434
Cdd:cd07111 330 AIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANN 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 170650621 435 TDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEY 497
Cdd:cd07111 410 TPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
49-505 |
2.51e-158 |
|
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: 457.95 E-value: 2.51e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 49 FATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLH 128
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 129 AFFvDLEGCIKTFRYFAGWADKIQGRTIPTDDN-VVCFTRHEPIGVCGAITPWNFPLLmLAWK-LAPALCCGNTVVLKPA 206
Cdd:cd07150 78 AWF-ETTFTPELLRAAAGECRRVRGETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLI-LATKkVAFALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 207 EQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNP 286
Cdd:cd07150 156 EETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKIL 366
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 367 ELIESGKKEGAKLECGGsamEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTK 446
Cdd:cd07150 315 RQVEDAVAKGAKLLTGG---KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170650621 447 NLDKALKLAAALESGTVWINCyNAFY--AQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07150 392 DLQRAFKLAERLESGMVHIND-PTILdeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
16-503 |
5.41e-156 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 453.76 E-value: 5.41e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 16 KPPALPRPIRNLEVKFTKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALS 95
Cdd:PLN02278 9 DAQSALVKLRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLTASE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 96 RGQLLHQLADLVERDRAILATLETMDTGKPFLHAF--------FVDlegciktfrYFAGWADKIQGRTIPTDD-NVVCFT 166
Cdd:PLN02278 86 RSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIgevaygasFLE---------YFAEEAKRVYGDIIPSPFpDRRLLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 167 RHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISS 246
Cdd:PLN02278 157 LKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 247 HPQINKIAFTGSTEVGKLVREAASRSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQV 326
Cdd:PLN02278 237 SPKVRKITFTGSTAVGKKLMAGAAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 327 YGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMR 406
Cdd:PLN02278 316 YDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDML 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 407 IAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNG 486
Cdd:PLN02278 396 IFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLG 475
|
490
....*....|....*..
gi 170650621 487 RELGEYALAEYTEVKTV 503
Cdd:PLN02278 476 REGSKYGIDEYLEIKYV 492
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
49-505 |
1.13e-154 |
|
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: 448.72 E-value: 1.13e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 49 FATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLH 128
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV---MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 129 AFfVDLEGCIKTFRYFAGWADKIQGRTIPTDD-----NVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVL 203
Cdd:cd07145 78 SR-VEVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 204 KPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRSnLKRVTLELGG 283
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT-GKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 284 KNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFD 363
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 364 KILELIESGKKEGAKLECGGSAMEdrGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAV 443
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 170650621 444 FTKNLDKALKLAAALESGTVWINCYNAF-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFrWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
52-505 |
4.34e-154 |
|
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: 447.04 E-value: 4.34e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGspwRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFF 131
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKP-IKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 132 VDLEGCIKTFRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPA 206
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKRLAGETIPFDaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 207 EQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASrsnLKRVTLELGGKNP 286
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGSNAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKIL 366
Cdd:cd07149 237 VIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 367 ELIESGKKEGAKLECGGSAmedRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTK 446
Cdd:cd07149 317 EWVEEAVEGGARLLTGGKR---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTN 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 447 NLDKALKLAAALESGTVWINCYNAFYAQA-PFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07149 394 DLQKALKAARELEVGGVMINDSSTFRVDHmPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
32-508 |
1.91e-153 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 447.04 E-value: 1.91e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 32 TKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSpWRRLDALSRGQLLHQLADLVERDR 111
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLADLMEAHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 112 AILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKL 191
Cdd:PRK09847 99 EELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 192 APALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASR 271
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 272 SNLKRVTLELGGKNPCIVCADA-DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAK 350
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 351 TEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAmeDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIK 430
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNA--GLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170650621 431 RANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLE 508
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISLE 494
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
35-505 |
1.02e-152 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 444.31 E-value: 1.02e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWHESKSGRkFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAIL 114
Cdd:cd07086 2 VIGGEWVGSGGET-FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 115 ATLETMDTGKPFLHAF-----FVDLegCIktfrYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLA 188
Cdd:cd07086 78 GRLVSLEMGKILPEGLgevqeMIDI--CD----YAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 189 WKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV----GFPPGVVNIVPGFGPtVGAAISSHPQINKIAFTGSTEVGKL 264
Cdd:cd07086 152 WNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 265 VREAASRSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVG 344
Cdd:cd07086 231 VGETVARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 345 DPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAME--DRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKF 422
Cdd:cd07086 310 DPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDggEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 423 KNLEEVIKRANSTDYGLTAAVFTKNLDKALKL--AAALESGTVWIN--CYNAfYAQAPFGGFKMSGNGRELGEYALAEYT 498
Cdd:cd07086 390 DSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNipTSGA-EIGGAFGGEKETGGGRESGSDAWKQYM 468
|
....*..
gi 170650621 499 EVKTVTI 505
Cdd:cd07086 469 RRSTCTI 475
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
35-506 |
2.16e-147 |
|
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: 431.09 E-value: 2.16e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgSPWRRLDALSRGQLLHQLADLVERDRAIL 114
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 115 ATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTI------PTDDNVVCFTRHEPIGVCGAITPWNFPLLMLA 188
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLapsipsMQGERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 189 WKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGpTVGAAISSHPQINKIAFTGSTEVGKLVREA 268
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 269 ASrSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFD 348
Cdd:cd07113 240 AA-SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 349 AKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEV 428
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170650621 429 IKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
34-504 |
2.39e-145 |
|
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: 427.02 E-value: 2.39e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 34 IFINNDwhESKSGRKFATYNPS-TLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRA 112
Cdd:cd07124 35 LVIGGK--EVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPT---WRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 113 ILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLA 192
Cdd:cd07124 110 ELAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 193 PALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASR- 271
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 272 ----SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPF 347
Cdd:cd07124 269 qpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 348 DAKTEQGPQIDQKQFDKILELIESGKKEGaKLECGGSAMED--RGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNL 425
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 426 EEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWIN--CYNAFYAQAPFGGFKMSG-NGRELGEYALAEYTEVKT 502
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGtGSKAGGPDYLLQFMQPKT 507
|
..
gi 170650621 503 VT 504
Cdd:cd07124 508 VT 509
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
35-505 |
4.44e-144 |
|
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: 422.63 E-value: 4.44e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAIL 114
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA---WGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 115 ATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPA 194
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 195 LCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNL 274
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 275 KRVTLELGGKNPCIVCA------DADLDLAVECAhqGVF-FNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPF 347
Cdd:cd07116 239 IPVTLELGGKSPNIFFAdvmdadDAFFDKALEGF--VMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 348 DAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGL----FIKPTVFSDvTDNMRIAKEEIFGPVQPILKFK 423
Cdd:cd07116 317 DTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 424 NLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07116 396 DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNL 475
|
..
gi 170650621 504 TI 505
Cdd:cd07116 476 LV 477
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
35-507 |
1.82e-139 |
|
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: 410.65 E-value: 1.82e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWHESksGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGsPWRRLDALSRGQLLHQLADLVERDRAIL 114
Cdd:TIGR03216 4 FINGAFVES--GKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAA-LKG-PWGKMTVAERADLLYAVADEIERRFDDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 115 ATLETMDTGKPFLHAFFVDLEGCIKTFRYFAgwaDKIqgRTIPTD---------DNVVCFTRHEPIGVCGAITPWNFPLL 185
Cdd:TIGR03216 80 LAAEVADTGKPRSLASHLDIPRGAANFRVFA---DVV--KNAPTEcfematpdgKGALNYAVRKPLGVVGVISPWNLPLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 186 MLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGP-TVGAAISSHPQINKIAFTGSTEVGKL 264
Cdd:TIGR03216 155 LMTWKVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGETRTGSA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 265 VREAASRSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVG 344
Cdd:TIGR03216 235 IMKAAADG-VKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 345 DPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGG-----SAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPI 419
Cdd:TIGR03216 314 VPDDPATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGgvpdfGDALAGGAWVQPTIWTGLPDSARVVTEEIFGPCCHI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 420 LKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTE 499
Cdd:TIGR03216 394 APFDSEEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTE 473
|
....*...
gi 170650621 500 VKTVTIKL 507
Cdd:TIGR03216 474 LTNVCIKL 481
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
38-506 |
4.23e-139 |
|
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: 409.39 E-value: 4.23e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 38 NDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRgsPWRRLDALSRGQLLHQLADLVERDRAILATL 117
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA-QK--EWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 118 ETMDTGKPFLHAFFvDLEGCIKTFRYFAGWADKIQGRTIPTD----DNVVcftRHEPIGVCGAITPWNFPLLMLAWKLAP 193
Cdd:cd07151 78 LIRESGSTRIKANI-EWGAAMAITREAATFPLRMEGRILPSDvpgkENRV---YREPLGVVGVISPWNFPLHLSMRSVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 194 ALCCGNTVVLKPAEQTPLTA-LYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRs 272
Cdd:cd07151 154 ALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 273 NLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTE 352
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 353 QGPQIDQKQFDKILELIESGKKEGAKLECGGSAmedRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRA 432
Cdd:cd07151 313 VGPLINESQVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELA 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170650621 433 NSTDYGLTAAVFTKNLDKALKLAAALESGTVWIN--CYNAfYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:cd07151 390 NDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINdqPVND-EPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
53-505 |
5.00e-138 |
|
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: 406.05 E-value: 5.00e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 53 NPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfV 132
Cdd:cd07094 5 NPYDGEVIGKVPADDRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR-V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 133 DLEGCIKTFRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAE 207
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 208 QTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASrsnLKRVTLELGGKNPC 287
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILE 367
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 368 LIESGKKEGAKLECGGsamEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKN 447
Cdd:cd07094 318 WVEEAVEAGARLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 170650621 448 LDKALKLAAALESGTVWINCYNAFYAQA-PFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
71-505 |
2.51e-136 |
|
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: 400.68 E-value: 2.51e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 71 VDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF-VDLegCIKTFRYFAGWAD 149
Cdd:cd07100 1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAeVEK--CAWICRYYAENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 150 K-IQGRTIPTDDNVvCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPG 228
Cdd:cd07100 76 AfLADEPIETDAGK-AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 229 VVNIVPGFGPTVGAAISsHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFF 308
Cdd:cd07100 155 VFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 309 NQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMED 388
Cdd:cd07100 233 NAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 389 RGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCY 468
Cdd:cd07100 313 PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGM 392
|
410 420 430
....*....|....*....|....*....|....*..
gi 170650621 469 NAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07100 393 VKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
52-501 |
7.29e-136 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 400.27 E-value: 7.29e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAff 131
Cdd:TIGR01780 2 YNPATGEIIGSVPDQGVDETEAAIRAAYEAFKT---WRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 132 vdlEGCIKT----FRYFAGWADKIQGRTIPT--DDNVVCFTRhEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKP 205
Cdd:TIGR01780 77 ---KGEILYaasfLEWFAEEAKRVYGDTIPSpqSDKRLIVIK-QPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 206 AEQTPLTALYLASLIKEVGFPPGVVNIVPG-FGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASrSNLKRVTLELGGK 284
Cdd:TIGR01780 153 AEQTPLSALALARLAEQAGIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSA-STVKKVSMELGGN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 285 NPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDK 364
Cdd:TIGR01780 232 APFIVFDDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 365 ILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVF 444
Cdd:TIGR01780 312 VEKHIADAVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFF 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 170650621 445 TKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVK 501
Cdd:TIGR01780 392 SRDLSRIWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
51-504 |
1.33e-133 |
|
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: 394.79 E-value: 1.33e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 51 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFqRGSPWRRlDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF 130
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAF-DETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 131 FvDLEGCIKTFRYFAGWADKIQGRTI-PTDDNVVCFTRhEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQT 209
Cdd:cd07120 79 F-EISGAISELRYYAGLARTEAGRMIePEPGSFSLVLR-EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 210 PLTALYLASLIKEV-GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASrSNLKRVTLELGGKNPCI 288
Cdd:cd07120 157 AQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPCI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 289 VCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILEL 368
Cdd:cd07120 236 VFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 369 IESGKKEGAK-LECGGSAMED--RGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFT 445
Cdd:cd07120 316 VERAIAAGAEvVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 170650621 446 KNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07120 396 RDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
58-505 |
1.23e-132 |
|
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: 392.04 E-value: 1.23e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 58 EKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGC 137
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAA-QRA--WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGF-EVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 138 IKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTA-LYL 216
Cdd:cd07152 78 IGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 217 ASLIKEVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLD 296
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 297 LAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEG 376
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 377 AKLECGGSAmedRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAA 456
Cdd:cd07152 316 ARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 170650621 457 ALESGTVWIN-------CYNafyaqaPFGGFKMSGNGRELGEYA-LAEYTEVKTVTI 505
Cdd:cd07152 393 RLRTGMLHINdqtvndePHN------PFGGMGASGNGSRFGGPAnWEEFTQWQWVTV 443
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
52-505 |
2.36e-131 |
|
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: 388.89 E-value: 2.36e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFF 131
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAA-QRA--WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 132 VDLEGCIKTFRYFAGWADKI-QGRTIPTDD---NVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAE 207
Cdd:cd07099 77 LEVLLALEAIDWAARNAPRVlAPRKVPTGLlmpNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 208 QTPLTALYLASLIKEVGFPPGVVNIVPGFGPTvGAAISSHPqINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPC 287
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILE 367
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 368 LIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKN 447
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 448 LDKALKLAAALESGTVWINC--YNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
70-505 |
5.30e-131 |
|
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: 387.32 E-value: 5.30e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 70 DVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWAD 149
Cdd:cd07105 1 DADQAVEAAAAAFP---AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGF-NVDLAAGMLREAASLIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 150 KIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPG 228
Cdd:cd07105 77 QIIGGSIPSDkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 229 VVNIV---PGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQG 305
Cdd:cd07105 157 VLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 306 VFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDpfdakTEQGPQIDQKQFDKILELIESGKKEGAKLECGG-S 384
Cdd:cd07105 236 AFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGlA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 385 AMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVW 464
Cdd:cd07105 311 DESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 170650621 465 IN---CYNAfyAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07105 391 INgmtVHDE--PTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
33-506 |
9.87e-131 |
|
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: 388.08 E-value: 9.87e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 33 KIFINNDWHESkSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGSpWRRLDALSRGQLLHQLADLVERDRA 112
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDA-GRGW-WPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 113 ILATLETMDTGKPflhaffvdLEGCIKTF-------RYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPW 180
Cdd:cd07082 80 EVANLLMWEIGKT--------LKDALKEVdrtidyiRDTIEELKRLDGDSLPGDwfpgtKGKIAQVRREPLGVVLAIGPF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 181 NFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTE 260
Cdd:cd07082 152 NYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 261 VGKLVREAASRsnlKRVTLELGGKNPCIVCADADLDLAV-ECAHQGVFFNqGQCCTAASRVFVEEQVYGEFVRRSVEFAK 339
Cdd:cd07082 232 VGNRLKKQHPM---KRLVLELGGKDPAIVLPDADLELAAkEIVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEEVA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 340 KRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEdrGLFIKPTVFSDVTDNMRIAKEEIFGPVQPI 419
Cdd:cd07082 308 KLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 420 LKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNA-----FyaqaPFGGFKMSGNGRELGEYAL 494
Cdd:cd07082 386 IRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrgpdhF----PFLGRKDSGIGTQGIGDAL 461
|
490
....*....|..
gi 170650621 495 AEYTEVKTVTIK 506
Cdd:cd07082 462 RSMTRRKGIVIN 473
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
48-507 |
6.79e-127 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 379.66 E-value: 6.79e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 48 KFATYNPS-TLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPF 126
Cdd:PRK03137 51 KIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFET---WKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPW 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 127 LHAFfVDLEGCIKTFRYFA----GWADKIQGRTIPTDDNvvcFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVV 202
Cdd:PRK03137 128 AEAD-ADTAEAIDFLEYYArqmlKLADGKPVESRPGEHN---RYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 203 LKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRSN-----LKRV 277
Cdd:PRK03137 204 LKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQpgqiwLKRV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 278 TLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAkTEQGPQI 357
Cdd:PRK03137 284 IAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN-AYMGPVI 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 358 DQKQFDKILELIESGKKEGaKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDY 437
Cdd:PRK03137 363 NQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEY 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170650621 438 GLTAAVFTKNLDKALKLAAALESGTVWIN--CYNAFYAQAPFGGFKMSGNGRELG--EYaLAEYTEVKTVTIKL 507
Cdd:PRK03137 442 GLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGFNMSGTDSKAGgpDY-LLLFLQAKTVSEMF 514
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
42-504 |
1.44e-126 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 379.22 E-value: 1.44e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 42 ESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMD 121
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QRA--WAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 122 TGKPFLHAF--FVDLEGCIktfRYFAGWADKI------QGrTIPTDDNVVcfTRHEPIGVCGAITPWNFPLLMLAWKLAP 193
Cdd:PRK09407 104 TGKARRHAFeeVLDVALTA---RYYARRAPKLlaprrrAG-ALPVLTKTT--ELRQPKGVVGVISPWNYPLTLAVSDAIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 194 ALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHpqINKIAFTGSTEVGKLVREAASRsN 273
Cdd:PRK09407 178 ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGR-R 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 274 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQ 353
Cdd:PRK09407 255 LIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 354 GPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRG-LFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRA 432
Cdd:PRK09407 335 GSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170650621 433 NSTDYGLTAAVFTKNLDKALKLAAALESGTVWIN-CYNAFYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:PRK09407 415 NDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNeGYAAAWGsvDAPMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
53-505 |
2.29e-123 |
|
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: 368.61 E-value: 2.29e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 53 NPSTLEKICEVEEGDKPDVDKAVEAAqaafqrGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfV 132
Cdd:cd07146 5 NPYTGEVVGTVPAGTEEALREALALA------ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR-Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 133 DLEGCIKTFRYFAGWADKIQGRTIPTDDNV-----VCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAE 207
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFSCDLTAngkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 208 QTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASrsnLKRVTLELGGKNPC 287
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILE 367
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 368 LIESGKKEGAKLECGGsamEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKN 447
Cdd:cd07146 315 RVEEAIAQGARVLLGN---QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 448 LDKALKLAAALESGTVWINCYNAFYAQ-APFGGFKMSGNG-RELGEYALAEYTEVKTVTI 505
Cdd:cd07146 392 LDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
54-504 |
5.83e-122 |
|
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: 365.09 E-value: 5.83e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 54 PSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF--F 131
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA-QRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFeeV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 132 VDlegCIKTFRYFAGWADKI-----QGRTIPT-DDNVVCftrHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKP 205
Cdd:cd07101 80 LD---VAIVARYYARRAERLlkprrRRGAIPVlTRTTVN---RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 206 AEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHpqINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKN 285
Cdd:cd07101 154 DSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGR-RLIGCSLELGGKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 286 PCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKI 365
Cdd:cd07101 231 PMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 366 LELIESGKKEGAKLECGGSAMEDRG-LFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVF 444
Cdd:cd07101 311 TAHVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVW 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 170650621 445 TKNLDKALKLAAALESGTVWIN-CYNAFYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07101 391 TRDGARGRRIAARLRAGTVNVNeGYAAAWAsiDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
32-504 |
1.49e-120 |
|
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: 362.22 E-value: 1.49e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 32 TKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDR 111
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 112 AILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWADKIQGRTIP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWK 190
Cdd:cd07085 78 DELARLITLEHGKTLADAR-GDVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 191 LAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGaAISSHPQINKIAFTGSTEVGKLVREAAS 270
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVN-ALLDHPDIKAVSFVGSTPVGEYIYERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 271 RSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAK 350
Cdd:cd07085 236 ANG-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 351 TEQGPQIDQKQFDKILELIESGKKEGAKLECGG----SAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLE 426
Cdd:cd07085 315 ADMGPVISPAAKERIEGLIESGVEEGAKLVLDGrgvkVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 427 EVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWIN----CYNAFYaqaPFGGFKMS--GNGRELGEYALAEYTEV 500
Cdd:cd07085 395 EAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINvpipVPLAFF---SFGGWKGSffGDLHFYGKDGVRFYTQT 471
|
....
gi 170650621 501 KTVT 504
Cdd:cd07085 472 KTVT 475
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
52-505 |
4.11e-120 |
|
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: 360.41 E-value: 4.11e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF 131
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 132 vDLEGCIKTFRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPA 206
Cdd:cd07147 81 -EVARAIDTFRIAAEEATRIYGEVLPLDisargEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 207 EQTPLTALYLASLIKEVGFPPGVVNIVPGfgPTVGAAI-SSHPQINKIAFTGSTEVGKLVREAASRsnlKRVTLELGGKN 285
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 286 PCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKI 365
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 366 LELIESGKKEGAKLECGGsamEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFT 445
Cdd:cd07147 315 EGWVNEAVDAGAKLLTGG---KRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170650621 446 KNLDKALKLAAALESGTVWINCYNAFYA-QAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07147 392 RDLEKALRAWDELEVGGVVINDVPTFRVdHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
100-506 |
2.22e-115 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 346.72 E-value: 2.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 100 LHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWADKIQGRTIPTD---DNVVCFTRhePIGVCGA 176
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAE-VEVAFTADYIDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 177 ITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFT 256
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 257 GSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVE 336
Cdd:PRK10090 158 GSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 337 FAKKRPVGDPFDAKT-EQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGP 415
Cdd:PRK10090 237 AMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 416 VQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNaFYAQAPF-GGFKMSGNGRELGEYAL 494
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINREN-FEAMQGFhAGWRKSGIGGADGKHGL 395
|
410
....*....|..
gi 170650621 495 AEYTEVKTVTIK 506
Cdd:PRK10090 396 HEYLQTQVVYLQ 407
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
35-507 |
2.84e-115 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 348.82 E-value: 2.84e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAIL 114
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRWFNLMMEHQDDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 115 ATLETMDTGKPFLHAffvdlEGCIKTFRYFAGW----ADKIQGRTIP---TDDNVVCFTrhEPIGVCGAITPWNFPLLML 187
Cdd:PRK11241 91 ARLMTLEQGKPLAEA-----KGEISYAASFIEWfaeeGKRIYGDTIPghqADKRLIVIK--QPIGVTAAITPWNFPAAMI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 188 AWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVRE 267
Cdd:PRK11241 164 TRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLME 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 268 AASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPF 347
Cdd:PRK11241 244 QCAK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 348 DAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEE 427
Cdd:PRK11241 323 EKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEAD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 428 VIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:PRK11241 403 VIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
34-504 |
4.84e-115 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 349.16 E-value: 4.84e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 34 IFINNDWHESKSgrKFATYNPS-TLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRA 112
Cdd:TIGR01237 35 LVINGERVETEN--KIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEA---WKKTDPEERAAILFKAAAIVRRRRH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 113 ILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWADKIQGR----TIPTDDNVVCFTrhePIGVCGAITPWNFPLLMLA 188
Cdd:TIGR01237 110 EFSALLVKEVGKPWNEAD-AEVAEAIDFMEYYARQMIELAKGkpvnSREGETNQYVYT---PTGVTVVISPWNFPFAIMV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 189 WKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREA 268
Cdd:TIGR01237 186 GMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFER 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 269 ASR-----SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPV 343
Cdd:TIGR01237 266 AAKvqpgqKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 344 GDPFDAKTEQGPQIDQKQFDKILELIESGKKEGaKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFK 423
Cdd:TIGR01237 346 GPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRAS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 424 NLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWIN--CYNAFYAQAPFGGFKMSGNGRELG--EYaLAEYTE 499
Cdd:TIGR01237 425 DFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrnITGAIVGYQPFGGFKMSGTDSKAGgpDY-LALFMQ 503
|
....*
gi 170650621 500 VKTVT 504
Cdd:TIGR01237 504 AKTVT 508
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
52-503 |
1.29e-111 |
|
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: 1.29e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQ-LADLVERDRAILATLETMdTGKPFLHAf 130
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAA-QKG--WRAVPLEERKAIVTRaVELLAANTDEIAEELTWQ-MGRPIAQA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 131 fvdlEGCIKTF----RYFAGWADK-IQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKP 205
Cdd:cd07102 76 ----GGEIRGMleraRYMISIAEEaLADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 206 AEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTvGAAISSHPQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKN 285
Cdd:cd07102 152 SPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 286 PCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKI 365
Cdd:cd07102 230 PAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 366 LELIESGKKEGAKLECGG---SAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAA 442
Cdd:cd07102 310 RAQIADAIAKGARALIDGalfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTAS 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170650621 443 VFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07102 390 VWTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
52-504 |
5.90e-108 |
|
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: 329.65 E-value: 5.90e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF 131
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQRE---WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 132 vdleGCIKTFryfagwADKIQ-----G----RTIPTDDNVVCFTR-----HEPIGVCGAITPWNFPLLMLAWKLAPALCC 197
Cdd:cd07098 78 ----GEILVT------CEKIRwtlkhGekalRPESRPGGLLMFYKrarveYEPLGVVGAIVSWNYPFHNLLGPIIAALFA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 198 GNTVVLKPAEQTPLTALYLASLIKEV----GFPPGVVNIVPGFGPTvGAAISSHPQINKIAFTGSTEVGKLVREAASRSn 273
Cdd:cd07098 148 GNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 274 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQ 353
Cdd:cd07098 226 LTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 354 GPQIDQKQFDKILELIESGKKEGAKLECGGS----AMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVI 429
Cdd:cd07098 306 GAMISPARFDRLEELVADAVEKGARLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAV 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170650621 430 KRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCY-NAFYAQA-PFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07098 386 EIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFgVNYYVQQlPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
45-503 |
1.52e-106 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 326.34 E-value: 1.52e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 45 SGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgSPWRRLDALsRGQLLHQLADLVERDRAILATLETMDTGK 124
Cdd:TIGR04284 13 SAGTFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDE-TDWSRDTAL-RVRCLRQLRDALRAHVEELRELTIAEVGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 125 PFLHAFFVDLEGCIKTFRYFAGWADKIQGRT---------IPTDDNVvcftRHEPIGVCGAITPWNFPLLMLAWKLAPAL 195
Cdd:TIGR04284 91 PRMLTAGAQLEGPVDDLGFAADLAESYAWTTdlgvaspmgIPTRRTL----RREAVGVVGAITPWNFPHQINLAKLGPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 196 CCGNTVVLKPAEQTPLTALYLASLIKE-VGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRSnL 274
Cdd:TIGR04284 167 AAGNTVVLKPAPDTPWCAAVLGELIAEhTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRAVMADAAAT-L 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQG 354
Cdd:TIGR04284 246 KKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADPGTVCG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 355 PQIDQKQFDKILELIESGKKEGAKLECGGS--AMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRA 432
Cdd:TIGR04284 326 PVISARQRDRVQSYLDLAVAEGGRFACGGGrpADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRIA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170650621 433 NSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:TIGR04284 406 NDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETKLI 476
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
37-505 |
2.04e-97 |
|
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: 302.59 E-value: 2.04e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 37 NNDWheSKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILAT 116
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 117 LETMDTGKPFLHAF-----FVDLegCiktfRYFAGWADKIQGRTIPTD--DNVVCFTRHePIGVCGAITPWNFPLLMLAW 189
Cdd:cd07130 79 LVSLEMGKILPEGLgevqeMIDI--C----DFAVGLSRQLYGLTIPSErpGHRMMEQWN-PLGVVGVITAFNFPVAVWGW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 190 KLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV----GFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLV 265
Cdd:cd07130 152 NAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 266 REAASRsNLKRVTLELGGKNPCIVCADADLDLAVecahQGVFF----NQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKR 341
Cdd:cd07130 231 GQAVAA-RFGRSLLELGGNNAIIVMEDADLDLAV----RAVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 342 PVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSdVTDNMRIAKEEIFGPVQPILK 421
Cdd:cd07130 306 RIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 422 FKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCyNAFYAQA----PFGGFKMSGNGRELGEYALAEY 497
Cdd:cd07130 385 FDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNV-NIGTSGAeiggAFGGEKETGGGRESGSDAWKQY 463
|
....*...
gi 170650621 498 TEVKTVTI 505
Cdd:cd07130 464 MRRSTCTI 471
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
50-505 |
1.26e-96 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 300.12 E-value: 1.26e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 50 ATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHA 129
Cdd:PRK09406 4 ATINPATGETVKTFTALTDDEVDAAIARAHARFRD---YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 130 FFVDLEGCIKTFRYFAGWADKIQGRTiPTDDNVV----CFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKP 205
Cdd:PRK09406 80 AKAEALKCAKGFRYYAEHAEALLADE-PADAAAVgasrAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 206 AEQTPLTALYLASLIKEVGFPPGVVNIVpgfgpTVGA----AISSHPQINKIAFTGSTEVGKLVREAASRSnLKRVTLEL 281
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGFPDGCFQTL-----LVGSgaveAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 282 GGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQ 361
Cdd:PRK09406 233 GGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 362 FDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTA 441
Cdd:PRK09406 313 RDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170650621 442 AVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:PRK09406 393 NAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
53-504 |
4.86e-93 |
|
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: 292.18 E-value: 4.86e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 53 NPS-TLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFf 131
Cdd:cd07083 38 SPFaPSEVVGTTAKADKAEAEAALEAAWAAFKT---WKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAI- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 132 VDLEGCIKTFRYFAGWADKIQGR-----TIPTDDNVvcfTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPA 206
Cdd:cd07083 114 DDVAEAIDFIRYYARAALRLRYPavevvPYPGEDNE---SFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 207 EQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASR-----SNLKRVTLEL 281
Cdd:cd07083 191 EDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARlapgqTWFKRLYVET 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 282 GGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQ 361
Cdd:cd07083 271 GGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 362 FDKILELIESGKKEGaKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFK--NLEEVIKRANSTDYGL 439
Cdd:cd07083 351 EAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKddDFAEALEVANSTPYGL 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170650621 440 TAAVFTKNLDKALKLAAALESGTVWIN--CYNAFYAQAPFGGFKMSG-NGRELGEYALAEYTEVKTVT 504
Cdd:cd07083 430 TGGVYSRKREHLEEARREFHVGNLYINrkITGALVGVQPFGGFKLSGtNAKTGGPHYLRRFLEMKAVA 497
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
52-505 |
6.34e-86 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 274.07 E-value: 6.34e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 52 YNPSTLEK-ICEVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF 130
Cdd:cd07125 51 IDPADHERtIGEVSLADAEDVDAALAIAAAAF---AGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 131 -----FVDLegCiktfRYFAGWADKIQGRTI---PTD--DNVVCftrhEPIGVCGAITPWNFPLLMLAWKLAPALCCGNT 200
Cdd:cd07125 128 aevreAIDF--C----RYYAAQARELFSDPElpgPTGelNGLEL----HGRGVFVCISPWNFPLAIFTGQIAAALAAGNT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 201 VVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRSNLKRVTL- 279
Cdd:cd07125 198 VIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPILPLi 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 280 -ELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQID 358
Cdd:cd07125 278 aETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLID 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 359 QKQFDKILELIESGKKEgAKLECGGSAMEDRGLFIKPTVFSDVTDNMRiaKEEIFGPVQPILKFK--NLEEVIKRANSTD 436
Cdd:cd07125 358 KPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGIFDL--TTEVFGPILHVIRFKaeDLDEAIEDINATG 434
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170650621 437 YGLTAAVFTKNLDKALKLAAALESGTVWINcYN---AFYAQAPFGGFKMSGNGRELG--EYaLAEYTEVKTVTI 505
Cdd:cd07125 435 YGLTLGIHSRDEREIEYWRERVEAGNLYIN-RNitgAIVGRQPFGGWGLSGTGPKAGgpNY-LLRFGNEKTVSL 506
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
53-505 |
6.86e-85 |
|
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: 269.67 E-value: 6.86e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 53 NPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSPWrrLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfV 132
Cdd:cd07148 5 NPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK-V 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 133 DLEGCIKTFRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAE 207
Cdd:cd07148 82 EVTRAIDGVELAADELGQLGGREIPMGltpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 208 QTPLTALYLASLIKEVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVReaasrSNLK---RVTLELGGK 284
Cdd:cd07148 162 ATPLSCLAFVDLLHEAGLPEGWCQAVPC-ENAVAEKLVTDPRVAFFSFIGSARVGWMLR-----SKLApgtRCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 285 NPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDK 364
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 365 ILELIESGKKEGAKLECGGSAMEDRGLfiKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVF 444
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170650621 445 TKNLDKALKLAAALESGTVWINCYNAFYAQ-APFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07148 394 TKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
70-498 |
8.35e-84 |
|
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: 266.06 E-value: 8.35e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 70 DVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF--------VDLEgcIKTF 141
Cdd:cd07095 1 QVDAAVAAARAAF---PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDIS--IKAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 142 RYFAGwadkiqGRTIPTDdNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIK 221
Cdd:cd07095 76 HERTG------ERATPMA-QGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 222 EVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRSNLKRVTLELGGKNPCIVCADADLDLAVEC 301
Cdd:cd07095 149 EAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 302 AHQGVFFNQGQCCTAASRVFVEEQVYG-EFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLE 380
Cdd:cd07095 228 IVQSAFLTAGQRCTCARRLIVPDGAVGdAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 381 CGGSAMEDRGLFIKPTVFsDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALES 460
Cdd:cd07095 308 LAMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRA 386
|
410 420 430
....*....|....*....|....*....|....*....
gi 170650621 461 GTVWINCYNAFYA-QAPFGGFKMSGNGRELGEYAlAEYT 498
Cdd:cd07095 387 GIVNWNRPTTGASsTAPFGGVGLSGNHRPSAYYA-ADYC 424
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
74-505 |
2.43e-81 |
|
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: 259.38 E-value: 2.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 74 AVEAAQAAFQRGS----PWRR--LDALSRGqllhqladLVERDRAILATLETmDTGKPFLHAFFVDLEGCIKTFRY---- 143
Cdd:cd07087 3 LVARLRETFLTGKtrslEWRKaqLKALKRM--------LTENEEEIAAALYA-DLGKPPAEAYLTEIAVVLGEIDHalkh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 144 FAGWADKiqgRTIPTDDNVV---CFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLI 220
Cdd:cd07087 74 LKKWMKP---RRVSVPLLLQpakAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 221 KEVgFPPGVVNIVPGfGPTVGAAISSHPqINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLDLAVE 300
Cdd:cd07087 151 PKY-FDPEAVAVVEG-GVEVATALLAEP-FDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 301 CAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEfAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKkegakLE 380
Cdd:cd07087 227 RIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKK-AIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGK-----VV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 381 CGGSAMEDRgLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALES 460
Cdd:cd07087 301 IGGQVDKEE-RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSS 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 170650621 461 GTVwinCYNAFYAQA-----PFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07087 380 GGV---CVNDVLLHAaipnlPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
53-503 |
4.81e-81 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 259.79 E-value: 4.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 53 NPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVeRDRAI-LATLETMDTGKPFLHAff 131
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRD---WRETNIDYRAQKLRDIGKAL-RARSEeMAQMITREMGKPINQA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 132 vdlEGCIKTFRYFAGWADKiQG----RTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPA 206
Cdd:PRK13968 87 ---RAEVAKSANLCDWYAE-HGpamlKAEPTlVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 207 EQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISShPQINKIAFTGSTEVGKLVREAASRSnLKRVTLELGGKNP 286
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKIL 366
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 367 ELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTK 446
Cdd:PRK13968 321 HQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 170650621 447 NLDKALKLAAALESGTVWINCYNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:PRK13968 401 DETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
164-503 |
1.55e-80 |
|
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: 257.54 E-value: 1.55e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 164 CFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGfGPTVGAA 243
Cdd:cd07134 94 SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-DAEVAQA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 244 ISSHPqINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVE 323
Cdd:cd07134 172 LLELP-FDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 324 EQVYGEFVRRSVEFAKKRpVGDpfDAKTEQGPQ----IDQKQFDKILELIESGKKEGAKLECGGsAMEDRGLFIKPTVFS 399
Cdd:cd07134 250 ESVKDAFVEHLKAEIEKF-YGK--DAARKASPDlariVNDRHFDRLKGLLDDAVAKGAKVEFGG-QFDAAQRYIAPTVLT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 400 DVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYA--QAPF 477
Cdd:cd07134 326 NVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLnpNLPF 405
|
330 340
....*....|....*....|....*.
gi 170650621 478 GGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07134 406 GGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
33-508 |
1.61e-79 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 256.99 E-value: 1.61e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 33 KIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRA 112
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA-QKA--WAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 113 ILATLETMDTGKPFLHAFF-----VDL------EGCiktfRYFaGWADKIQGRTIP-TDDNVVCFTRHEPIGVCGAITPW 180
Cdd:PLN00412 94 PIAECLVKEIAKPAKDAVTevvrsGDLisytaeEGV----RIL-GEGKFLVSDSFPgNERNKYCLTSKIPLGVVLAIPPF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 181 NFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGStE 260
Cdd:PLN00412 169 NYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-D 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 261 VGKLVREAASRSNLKrvtLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKK 340
Cdd:PLN00412 248 TGIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 341 RPVGDPFDaKTEQGPQIDQKQFDKILELIESGKKEGAKLeCGGSAMEdrGLFIKPTVFSDVTDNMRIAKEEIFGPVQPIL 420
Cdd:PLN00412 325 LTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATF-CQEWKRE--GNLIWPLLLDNVRPDMRIAWEEPFGPVLPVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 421 KFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNA-----FyaqaPFGGFKMSGNGRELGEYALA 495
Cdd:PLN00412 401 RINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPArgpdhF----PFQGLKDSGIGSQGITNSIN 476
|
490
....*....|...
gi 170650621 496 EYTEVKTVTIKLE 508
Cdd:PLN00412 477 MMTKVKSTVINLP 489
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
33-504 |
8.94e-73 |
|
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: 238.63 E-value: 8.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 33 KIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRA 112
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 113 ILATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWADKIQGRTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKL 191
Cdd:TIGR01722 79 EIAELITAEHGKTHSDALG-DVARGLEVVEHACGVNSLLKGETSTQvATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 192 APALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGaAISSHPQINKIAFTGSTEVGKLVREAASR 271
Cdd:TIGR01722 158 PIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPIGRYIHTTGSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 272 SNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVyGEFVRRSVEFAKKRPVGDPFDAKT 351
Cdd:TIGR01722 237 HG-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 352 EQGPQIDQKQFDKILELIESGKKEGAKLECGGSAME----DRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEE 427
Cdd:TIGR01722 315 EMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKvdgyEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 428 VIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWIN----CYNAFYAqapFGGFKMS--GNGRELGEYALAEYTEVK 501
Cdd:TIGR01722 395 AIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNvpipVPLPYFS---FTGWKDSffGDHHIYGKQGTHFYTRGK 471
|
...
gi 170650621 502 TVT 504
Cdd:TIGR01722 472 TVT 474
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
70-503 |
2.90e-72 |
|
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: 235.96 E-value: 2.90e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 70 DVDKAVEAAQAAFQRGS----PWRRldalsrgQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFA 145
Cdd:cd07135 6 EIDSIHSRLRATFRSGKtkdlEYRL-------WQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 146 G----WA-DKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLI 220
Cdd:cd07135 79 KnlkkWAkDEKVKDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 221 KEvGFPPGVVNIVPGFGPTVGAAISSHpqINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLDLAVE 300
Cdd:cd07135 159 PK-YLDPDAFQVVQGGVPETTALLEQK--FDKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELAAK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 301 CAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPfDAKTEQGPQIDQKQFDKILELIESGKkegAKLE 380
Cdd:cd07135 235 RILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLLDTTK---GKVV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 381 CGGSaMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALES 460
Cdd:cd07135 311 IGGE-MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRS 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 170650621 461 GTVWIN-CYNAF-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07135 390 GGVVINdTLIHVgVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
169-492 |
7.70e-72 |
|
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: 235.48 E-value: 7.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 169 EPIGVCGAITPWNFPLLMLawkLAP---ALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGfGPTVGAAIS 245
Cdd:cd07136 99 EPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 246 SHPqINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQ 325
Cdd:cd07136 174 DQK-FDYIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 326 VYGEFVRRSVEFAKKRPVGDPFDAKtEQGPQIDQKQFDKILELIESGKkegakLECGGSAmEDRGLFIKPTVFSDVTDNM 405
Cdd:cd07136 252 VKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDNGK-----IVFGGNT-DRETLYIEPTILDNVTWDD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 406 RIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINcyNAFYAQA----PFGGFK 481
Cdd:cd07136 325 PVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN--DTIMHLAnpylPFGGVG 402
|
330
....*....|.
gi 170650621 482 MSGNGRELGEY 492
Cdd:cd07136 403 NSGMGSYHGKY 413
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
35-497 |
1.34e-71 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 236.01 E-value: 1.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWHESkSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAIL 114
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 115 ATLETMDTGKPFLHAffvdlegciKTfrYFAGWADKI-------QGRT----IPTDDNVVCFtRHEPIGVCGAITPWNFP 183
Cdd:PRK09457 80 AEVIARETGKPLWEA---------AT--EVTAMINKIaisiqayHERTgekrSEMADGAAVL-RHRPHGVVAVFGPYNFP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 184 LLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGK 263
Cdd:PRK09457 148 GHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 264 LV-REAASRSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGE-FVRRSVEFAKKR 341
Cdd:PRK09457 227 LLhRQFAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 342 PVGdPFDAKTE--QGPQIDQKQFDKILE----LIESGKK---EGAKLECGGSamedrglFIKPTVFsDVTDNMRIAKEEI 412
Cdd:PRK09457 306 TVG-RWDAEPQpfMGAVISEQAAQGLVAaqaqLLALGGKsllEMTQLQAGTG-------LLTPGII-DVTGVAELPDEEY 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 413 FGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTV-WINCYNAFYAQAPFGGFKMSGNGRELGE 491
Cdd:PRK09457 377 FGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHRPSAY 456
|
....*.
gi 170650621 492 YAlAEY 497
Cdd:PRK09457 457 YA-ADY 461
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
167-503 |
2.89e-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: 228.14 E-value: 2.89e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 167 RHEPIGVCGAITPWNFPLlMLAwkLAP---ALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGfGPTVGAA 243
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPL-YLA--LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTG-GADVAAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 244 ISSHPqINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVE 323
Cdd:cd07133 173 FSSLP-FDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVP 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 324 EQVYGEFVRRSVEFAKKR-PVGdpfdaktEQGPQ----IDQKQFDKILELIESGKKEGAKL-ECGGSAMEDRGL-FIKPT 396
Cdd:cd07133 251 EDKLEEFVAAAKAAVAKMyPTL-------ADNPDytsiINERHYARLQGLLEDARAKGARViELNPAGEDFAATrKLPPT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 397 VFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINcyNAFY--AQ 474
Cdd:cd07133 324 LVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN--DTLLhvAQ 401
|
330 340 350
....*....|....*....|....*....|.
gi 170650621 475 --APFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07133 402 ddLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
45-505 |
1.54e-67 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 234.71 E-value: 1.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 45 SGRKFATYNPSTLEK-ICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTG 123
Cdd:PRK11904 560 EGEARPVVSPADRRRvVGEVAFADAEQVEQALAAARAAFPA---WSRTPVEERAAILERAADLLEANRAELIALCVREAG 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 124 KPfLH--------AffVDLegCiktfRYFAGWADKIQGRTI----PT-DDNVVcftRHEPIGVCGAITPWNFPLLMLAWK 190
Cdd:PRK11904 637 KT-LQdaiaevreA--VDF--C----RYYAAQARRLFGAPEklpgPTgESNEL---RLHGRGVFVCISPWNFPLAIFLGQ 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 191 LAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLV-REAA 269
Cdd:PRK11904 705 VAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInRTLA 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 270 SRSNlKRVTL--ELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAAsRV-FVEEQVYG---EFVRRSVEFAKkrpV 343
Cdd:PRK11904 785 ARDG-PIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSAL-RVlFVQEDIADrviEMLKGAMAELK---V 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 344 GDPFDAKTEQGPQIDQKQFDKILELIESGKKEG---AKLECGGSAmeDRGLFIKPTVFSdvTDNMRIAKEEIFGPVQPIL 420
Cdd:PRK11904 860 GDPRLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLPAGT--ENGHFVAPTAFE--IDSISQLEREVFGPILHVI 935
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 421 KFK--NLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINcYN---AFYAQAPFGGFKMSGNG-RELGEYAL 494
Cdd:PRK11904 936 RYKasDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN-RNqigAVVGVQPFGGQGLSGTGpKAGGPHYL 1014
|
490
....*....|.
gi 170650621 495 AEYTEVKTVTI 505
Cdd:PRK11904 1015 LRFATEKTVTV 1025
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
60-490 |
3.91e-67 |
|
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: 224.40 E-value: 3.91e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 60 ICEVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFlHAFFVDLEGCIK 139
Cdd:TIGR01238 65 VGQVFHANLAHVQAAIDSAQQAF---PTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTI-HNAIAEVREAVD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 140 TFRYFAGWADKiqgrTIPTDDnvvcftrHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASL 219
Cdd:TIGR01238 141 FCRYYAKQVRD----VLGEFS-------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVEL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 220 IKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVREAASRSNLKRVTL--ELGGKNPCIVCADADLDL 297
Cdd:TIGR01238 210 MQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVDSTALPEQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 298 AVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEG- 376
Cdd:TIGR01238 290 VVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQk 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 377 --AKLECGGSAMEDRGLFIKPTVFSdvTDNMRIAKEEIFGPVQPILKFK--NLEEVIKRANSTDYGLTAAVFTKNLDKAL 452
Cdd:TIGR01238 370 kiAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVHSRIETTYR 447
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 170650621 453 KLAAALESGTVWIN--CYNAFYAQAPFGGFKMSGNGRELG 490
Cdd:TIGR01238 448 WIEKHARVGNCYVNrnQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
42-486 |
1.08e-66 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 233.29 E-value: 1.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 42 ESKSGRKFATYNPSTLEKIC-EVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETM 120
Cdd:COG4230 565 EAASGEARPVRNPADHSDVVgTVVEATAADVEAALAAAQAAFPA---WSATPVEERAAILERAADLLEAHRAELMALLVR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 121 DTGKPFLHAF-----FVDLegCiktfRYFAGwadkiQGRTIPTDDnvvcfTRHEPIGVCGAITPWNFPLLMLAWKLAPAL 195
Cdd:COG4230 642 EAGKTLPDAIaevreAVDF--C----RYYAA-----QARRLFAAP-----TVLRGRGVFVCISPWNFPLAIFTGQVAAAL 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 196 CCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLV-REAASRSNl 274
Cdd:COG4230 706 AAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLInRTLAARDG- 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 275 KRVTL--ELGGKNPCIV---------CADadldlAVECAhqgvFFNQGQCCTAAsRV-FVEEQVYGEFVRRSVEFAKKRP 342
Cdd:COG4230 785 PIVPLiaETGGQNAMIVdssalpeqvVDD-----VLASA----FDSAGQRCSAL-RVlCVQEDIADRVLEMLKGAMAELR 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 343 VGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKL-ECGGSAMEDRGLFIKPTVFSdvTDNMRIAKEEIFGPVQPILK 421
Cdd:COG4230 855 VGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLIE--IDSISDLEREVFGPVLHVVR 932
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170650621 422 FK--NLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINcYNAFYA----QaPFGGFKMSGNG 486
Cdd:COG4230 933 YKadELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN-RNIIGAvvgvQ-PFGGEGLSGTG 1001
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
35-505 |
1.26e-66 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 223.56 E-value: 1.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWheSKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfqrGSPWRRLDALSRGQLLHQLADLVERDRAIL 114
Cdd:PLN02315 24 YVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEA---AKIWMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 115 ATLETMDTGKpFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAP 193
Cdd:PLN02315 99 GRLVSLEMGK-ILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 194 ALCCGNTVVLKPAEQTPLTALYLASLIKEV----GFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVREAA 269
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 270 SrSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDA 349
Cdd:PLN02315 257 N-ARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 350 KTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFsDVTDNMRIAKEEIFGPVQPILKFKNLEEVI 429
Cdd:PLN02315 336 GTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAI 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170650621 430 KRANSTDYGLTAAVFTKNLDKALKLAAALES--GTVWINC-YNAFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:PLN02315 415 EINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTI 493
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
59-484 |
5.31e-66 |
|
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: 222.08 E-value: 5.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 59 KICEVEEGDKPDVDKAVEAAQAAfqRGSpWRRLDALSRGQLLHQLADLVE---RDRAILATLetMDTGKPFLHAffvdlE 135
Cdd:cd07123 59 VLATYHYADAALVEKAIEAALEA--RKE-WARMPFEDRAAIFLKAADLLSgkyRYELNAATM--LGQGKNVWQA-----E 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 136 ---GC--IKTFRYFAGWADKI-QGRTIPTDDNVVCFTRHEPI-GVCGAITPWNFPLLMLAWKLAPALCcGNTVVLKPAEQ 208
Cdd:cd07123 129 idaACelIDFLRFNVKYAEELyAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 209 TPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGK-LVREAASR----SNLKRVTLELGG 283
Cdd:cd07123 208 AVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKsLWKQIGENldryRTYPRIVGETGG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 284 KNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFD 363
Cdd:cd07123 288 KNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFD 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 364 KILELIESGKKE-GAKLECGGSAMEDRGLFIKPTVFsDVTD-NMRIAKEEIFGPVQPILKF--KNLEEVIKRANST-DYG 438
Cdd:cd07123 368 RIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVI-ETTDpKHKLMTEEIFGPVLTVYVYpdSDFEETLELVDTTsPYA 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 170650621 439 LTAAVF------TKNLDKALKLAAalesGTVWIN--CYNAFYAQAPFGGFKMSG 484
Cdd:cd07123 447 LTGAIFaqdrkaIREATDALRNAA----GNFYINdkPTGAVVGQQPFGGARASG 496
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
35-486 |
3.66e-65 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 228.98 E-value: 3.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWH-------ESKSGRKFATYNPS-TLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADL 106
Cdd:PRK11905 548 FAAKTWHaapllagGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPE---WSATPAAERAAILERAADL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 107 VERDRAILATLETMDTGKPFLHAF-----FVDlegciktF-RYFAGwadkiQGRTIPTDDnvvcftRHEPIGVCGAITPW 180
Cdd:PRK11905 625 MEAHMPELFALAVREAGKTLANAIaevreAVD-------FlRYYAA-----QARRLLNGP------GHKPLGPVVCISPW 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 181 NFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTE 260
Cdd:PRK11905 687 NFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTE 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 261 VGKLVREA-ASRSNlKRVTL--ELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAAsRV-FVEEQV--------YG 328
Cdd:PRK11905 767 VARLIQRTlAKRSG-PPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSAL-RVlCLQEDVadrvltmlKG 844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 329 ---EFVrrsvefakkrpVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKL-ECGGSAMEDRGLFIKPTVFSdvTDN 404
Cdd:PRK11905 845 amdELR-----------IGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLIE--IDS 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 405 MRIAKEEIFGPVQPILKFK--NLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINcYNAFYA----QaPFG 478
Cdd:PRK11905 912 ISDLEREVFGPVLHVVRFKadELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN-RNIIGAvvgvQ-PFG 989
|
....*...
gi 170650621 479 GFKMSGNG 486
Cdd:PRK11905 990 GEGLSGTG 997
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
164-506 |
2.08e-62 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 211.81 E-value: 2.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 164 CFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGfGPTVGAA 243
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 244 ISSHPqINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVE 323
Cdd:PTZ00381 181 LLKEP-FDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 324 EQVYGEFVrRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESgkkEGAKLECGGSA-MEDRglFIKPTVFSDVT 402
Cdd:PTZ00381 259 RSIKDKFI-EALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGEVdIENK--YVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 403 DNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWIN-CYNAFYAQA-PFGGF 480
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdCVFHLLNPNlPFGGV 412
|
330 340
....*....|....*....|....*.
gi 170650621 481 KMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
18-504 |
7.87e-61 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 210.37 E-value: 7.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 18 PALPRPIRNLevkftkifINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRG 97
Cdd:PLN02419 108 PQMPPRVPNL--------IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL---WRNTPITTRQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 98 QLLHQLADLVERDRAILATLETMDTGKPfLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVV-CFTRHEPIGVCGA 176
Cdd:PLN02419 177 RVMLKFQELIRKNMDKLAMNITTEQGKT-LKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVdTYSIREPLGVCAG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 177 ITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGaAISSHPQINKIAFT 256
Cdd:PLN02419 256 ICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 257 GSTEVGKLVREAASRSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASR-VFVEEQVYGEfvRRSV 335
Cdd:PLN02419 335 GSNTAGMHIYARAAAKG-KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDAKSWE--DKLV 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 336 EFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAM----EDRGLFIKPTVFSDVTDNMRIAKEE 411
Cdd:PLN02419 412 ERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMECYKEE 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 412 IFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCynafYAQAPFGGFKMSGNGREL-- 489
Cdd:PLN02419 492 IFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV----PIPVPLPFFSFTGNKASFag 567
|
490 500
....*....|....*....|
gi 170650621 490 -----GEYALAEYTEVKTVT 504
Cdd:PLN02419 568 dlnfyGKAGVDFFTQIKLVT 587
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
73-506 |
5.46e-60 |
|
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: 203.99 E-value: 5.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 73 KAVEAAQAAFQRGspwRRLDALSRGQLLHQLADLV-ERDRAILATLEtMDTGKPFLHAFFVDLEGCIKTFRY----FAGW 147
Cdd:cd07132 2 EAVRRAREAFSSG---KTRPLEFRIQQLEALLRMLeENEDEIVEALA-KDLRKPKFEAVLSEILLVKNEIKYaisnLPEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 148 A-DKIQGRTIPT--DDnvvCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLI---- 220
Cdd:cd07132 78 MkPEPVKKNLATllDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 221 -KEVgFPpgVVNivpgfgptvgAAISSHPQI-----NKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADAD 294
Cdd:cd07132 155 dKEC-YP--VVL----------GGVEETTELlkqrfDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSCD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 295 LDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVrrsvEFAK---KRPVGDpfDAKTEQ--GPQIDQKQFDKILELI 369
Cdd:cd07132 221 IDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFV----EALKktlKEFYGE--DPKESPdyGRIINDRHFQRLKKLL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 370 ESGKkegakLECGGSaMEDRGLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLD 449
Cdd:cd07132 295 SGGK-----VAIGGQ-TDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKK 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170650621 450 KALKLAAALESGTVwinCYN-----AFYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:cd07132 369 VINKILSNTSSGGV---CVNdtimhYTLDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
69-503 |
1.06e-53 |
|
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: 186.85 E-value: 1.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 69 PDVDKAVEAAQAAFQRGSPWRRldalsrgQLLHQLADLV-ERDRAILATLETmDTGKPFLHAFF----VDLEGCIKTFRY 143
Cdd:cd07137 3 RLVRELRETFRSGRTRSAEWRK-------SQLKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRdevsVLVSSCKLAIKE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 144 FAGWAD----KIQGRTIPTDDNVVCftrhEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASL 219
Cdd:cd07137 75 LKKWMApekvKTPLTTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 220 IKEVgFPPGVVNIVPGfGPTVGAAISSHpQINKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIVCADADLDLAV 299
Cdd:cd07137 151 IPEY-LDTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 300 ECAHQGVF-FNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKTEQgpQIDQKQFDKILELIESGKKEGAK 378
Cdd:cd07137 227 RRIAGGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLS--RIVNSHHFQRLSRLLDDPSVADK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 379 LECGGSAMEDRgLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAAL 458
Cdd:cd07137 305 IVHGGERDEKN-LYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAET 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 170650621 459 ESGTVWINCYNAFYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07137 384 SSGGVTFNDTVVQYAidTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
53-486 |
9.59e-51 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 187.10 E-value: 9.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 53 NPSTLEKIC-EVEEGDKPDVDKAVEAAQAAfqrGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF- 130
Cdd:PRK11809 665 NPADPRDIVgYVREATPAEVEQALESAVNA---APIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIa 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 131 ----FVDLegciktFRYFAGwadkiQGRTIPTDDNvvcftrHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPA 206
Cdd:PRK11809 742 evreAVDF------LRYYAG-----QVRDDFDNDT------HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 207 EQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLV-REAASR-SNLKRVT---LEL 281
Cdd:PRK11809 805 EQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLqRNLAGRlDPQGRPIpliAET 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 282 GGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVygefVRRSVEFAK----KRPVGDPFDAKTEQGPQI 357
Cdd:PRK11809 885 GGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDV----ADRTLKMLRgamaECRMGNPDRLSTDIGPVI 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 358 DQKQFDKILELIESGKKEGAK---LECGGSAMEDRGLFIKPTVFS-DVTDNMriaKEEIFGPVQPILKFK--NLEEVIKR 431
Cdd:PRK11809 961 DAEAKANIERHIQAMRAKGRPvfqAARENSEDWQSGTFVPPTLIElDSFDEL---KREVFGPVLHVVRYNrnQLDELIEQ 1037
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 170650621 432 ANSTDYGLTAAVFTKNLDKALKLAAALESGTVWI--NCYNAFYAQAPFGGFKMSGNG 486
Cdd:PRK11809 1038 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
77-490 |
5.31e-40 |
|
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: 150.08 E-value: 5.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 77 AAQAAFQRGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfvDLEGCIKTFRYFA--GWADKIQGR 154
Cdd:cd07084 4 ALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAE--NICGDQVQLRARAfvIYSYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 155 TIPTDDNVVCFTRHE---PIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG-FPPGVV 230
Cdd:cd07084 82 PGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 231 NIVPGFGPTvGAAISSHPQINKIAFTGSTEVGklvreAASRSNLK--RVTLELGGKNPCIVCADADL--DLAVECAhQGV 306
Cdd:cd07084 162 TLINGDGKT-MQALLLHPNPKMVLFTGSSRVA-----EKLALDAKqaRIYLELAGFNWKVLGPDAQAvdYVAWQCV-QDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 307 FFNQGQCCTAASRVFVEEQVYGE-FVRRSVEFAKKRPVGDpfdakTEQGPQIdqkQFDKILELIESGKKEGAKLECGGSA 385
Cdd:cd07084 235 TACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLED-----LLLGPVQ---TFTTLAMIAHMENLLGSVLLFSGKE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 386 M------EDRGLFIKPTVFSDVTDNMRIAK---EEIFGPVQPILKFKNLEE--VIKRANSTDYGLTAAVFTKNLDKALKL 454
Cdd:cd07084 307 LknhsipSIYGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPIFLQEL 386
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 170650621 455 AAALES-GTVWINCY---NAFYAQAPFGGFKMSGNGRELG 490
Cdd:cd07084 387 IGNLWVaGRTYAILRgrtGVAPNQNHGGGPAADPRGAGIG 426
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
169-504 |
2.20e-39 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 149.11 E-value: 2.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 169 EPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGfGPTVGAAISSHP 248
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEG-GPAVGEQLLQHK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 249 QiNKIAFTGSTEVGKLVREAASRsNLKRVTLELGGKNPCIV-CADA--DLDLAVE---------CAhqgvffnqGQCCTA 316
Cdd:PLN02203 185 W-DKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdSLSSsrDTKVAVNrivggkwgsCA--------GQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 317 ASRVFVEEQvygeFVRRSVEFAK---KRPVGDPFDAKTEQGPQIDQKQFDKILELIESgKKEGAKLECGGSAMEDRgLFI 393
Cdd:PLN02203 255 IDYVLVEER----FAPILIELLKstiKKFFGENPRESKSMARILNKKHFQRLSNLLKD-PRVAASIVHGGSIDEKK-LFI 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 394 KPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYA 473
Cdd:PLN02203 329 EPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYA 408
|
330 340 350
....*....|....*....|....*....|...
gi 170650621 474 --QAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:PLN02203 409 cdSLPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
121-503 |
2.01e-36 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 140.95 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 121 DTGKPFLHAFFVD---LEGCIK-TFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALC 196
Cdd:PLN02174 59 DLGKPELESSVYEvslLRNSIKlALKQLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAIS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 197 CGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISShpQINKIAFTGSTEVGKLVREAASRsNLKR 276
Cdd:PLN02174 139 AGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLEQ--KWDKIFYTGSSKIGRVIMAAAAK-HLTP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 277 VTLELGGKNPCIVCADADLDLAVECAHQGVF-FNQGQCCTAASRVFVEEQVYGEFVRRSVEFAKKRPVGDPFDAKtEQGP 355
Cdd:PLN02174 215 VVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMSR 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 356 QIDQKQFDKILELIESgKKEGAKLECGGSamEDR-GLFIKPTVFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANS 434
Cdd:PLN02174 294 IVNSTHFDRLSKLLDE-KEVSDKIVYGGE--KDReNLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRS 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170650621 435 TDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:PLN02174 371 RPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
35-459 |
7.33e-31 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 125.59 E-value: 7.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWHESkSGRKFATYNPSTLEKICEVeegDKPDVDKAVEAAQAAFQRGSPWRRLDALSRGQLLHQLADLVERDRAIL 114
Cdd:PRK11903 8 YVAGRWQAG-SGAGTPLFDPVTGEELVRV---SATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 115 ATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPI----------GVCGAITPWNFPL 184
Cdd:PRK11903 84 YDIATANSGTTRNDSAV-DIDGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKDPAFqgqhvlvptrGVALFINAFNFPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 185 LMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG-FPPGVVNIVPGfgptVGAAISSHPQ-INKIAFTGSTEVG 262
Cdd:PRK11903 163 WGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG----SSAGLLDHLQpFDVVSFTGSAETA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 263 KLVRE--AASRSNLkRVTLELGGKNPCIVCADAD-----LDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSV 335
Cdd:PRK11903 239 AVLRShpAVVQRSV-RVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 336 EFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIEsGKKEGAKLECGGSAME------DRGLFIKPTVF--SDVTDNMRI 407
Cdd:PRK11903 318 ARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLgaSDPDAATAV 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 170650621 408 AKEEIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKnlDKALKLAAALE 459
Cdd:PRK11903 397 HDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSD--DAAFLAAAALE 446
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
35-458 |
7.61e-26 |
|
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: 110.82 E-value: 7.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 35 FINNDWHESkSGRKFATYNPSTLEKICEVEeGDKPDVDKAVEAAQaafQRGSP-WRRLDALSRGQLLHQLAD-LVERDRA 112
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYAR---EKGGPaLRALTFHERAAMLKALAKyLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 113 ILATleTMDTGKPFLHAFfVDLEGCIKTFRYFAGwadkiQGRTIPTDDNV-------------------VCFTRHepiGV 173
Cdd:cd07128 79 LYAL--SAATGATRRDSW-IDIDGGIGTLFAYAS-----LGRRELPNAHFlvegdveplskdgtfvgqhILTPRR---GV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 174 CGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG-FPPGVVNIVPGfGPtvgAAISSH--PQi 250
Cdd:cd07128 148 AVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG-SV---GDLLDHlgEQ- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 251 NKIAFTGSTEVG-KLVREAASRSNLKRVTLELGGKNPCIVCADA-----DLDLAVECAHQGVFFNQGQCCTAASRVFVEE 324
Cdd:cd07128 223 DVVAFTGSAATAaKLRAHPNIVARSIRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRAFVPE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 325 QVYGEFVRRSVEFAKKRPVGDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAME------DRGLFIKPTVF 398
Cdd:cd07128 303 ARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEvvgadaEKGAFFPPTLL 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170650621 399 -SDVTDNMRIAKE-EIFGPVQPILKFKNLEEVIKRANSTDYGLTAAVFTKNLDKALKLAAAL 458
Cdd:cd07128 383 lCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGA 444
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
71-459 |
5.89e-21 |
|
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: 95.30 E-value: 5.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 71 VDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFlhaffVDLEGCI-KT---FRYFA- 145
Cdd:cd07129 1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPE-----ARLQGELgRTtgqLRLFAd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 146 -----GWADKI------QGRTIPTDDNVVCFTRHEPIGVCGAItpwNFPLlmlAWKL-----APALCCGNTVVLKPAEQT 209
Cdd:cd07129 73 lvregSWLDARidpadpDRQPLPRPDLRRMLVPLGPVAVFGAS---NFPL---AFSVaggdtASALAAGCPVVVKAHPAH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 210 PLTALYLASLIKEV----GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGK-LVREAASRSNLKRVTLELGGK 284
Cdd:cd07129 147 PGTSELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRaLFDAAAARPEPIPFYAELGSV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 285 NPCIVCADADLDLAVECAhQG----VFFNQGQCCTAASRVFVEEQVYGE-FVRRSVEFAKKRPVGDPFDAKTEQGpqidq 359
Cdd:cd07129 227 NPVFILPGALAERGEAIA-QGfvgsLTLGAGQFCTNPGLVLVPAGPAGDaFIAALAEALAAAPAQTMLTPGIAEA----- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 360 kqFDKILELIESGKkeGAKLECGGSAMEDRGLFiKPTVFS-DVTDNMRIAK--EEIFGPVQPILKFKNLEEVIKRANSTD 436
Cdd:cd07129 301 --YRQGVEALAAAP--GVRVLAGGAAAEGGNQA-APTLFKvDAAAFLADPAlqEEVFGPASLVVRYDDAAELLAVAEALE 375
|
410 420
....*....|....*....|....*
gi 170650621 437 YGLTAAVF--TKNLDKALKLAAALE 459
Cdd:cd07129 376 GQLTATIHgeEDDLALARELLPVLE 400
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
96-479 |
1.29e-17 |
|
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: 84.58 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 96 RGQLLHQLADLVERDRAILATLETMDTGKPF--LHAFFVDLEGCIK--------TFRYFAGWADKIQGRTIPtdDNVVCF 165
Cdd:cd07077 18 RDLIINAIANALYDTRQRLASEAVSERGAYIrsLIANWIAMMGCSEsklyknidTERGITASVGHIQDVLLP--DNGETY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 166 TRHEPIGVCGAITPWNFPLLMLAwKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV---GFPPGVVNIVPGFGPTVGA 242
Cdd:cd07077 96 VRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPSDELAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 243 AISSHPQINKIAFTGSTEVgklVREAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCctaasrvFV 322
Cdd:cd07077 175 ELLSHPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQNAC-------AS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 323 EEQVYgefvrrsvefakkrPVGDPFDAKTEQgpqidqkqfdkileLIESGKKEGAKLECGgsamedrglfIKPtVFSDVT 402
Cdd:cd07077 245 EQNLY--------------VVDDVLDPLYEE--------------FKLKLVVEGLKVPQE----------TKP-LSKETT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 403 DNMRIAKEEIFGPVQPILKFKNLEEVIKRA----NSTDYGLTAAVFTKNLDKALKLAAALESGTVWINCYNAFYAQAPFG 478
Cdd:cd07077 286 PSFDDEALESMTPLECQFRVLDVISAVENAwmiiESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAG 365
|
.
gi 170650621 479 G 479
Cdd:cd07077 366 K 366
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
170-443 |
3.12e-15 |
|
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: 77.92 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 170 PIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAIS-SHP 248
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 249 QInkIAFTGSTEVG-KLVREAASrsnlkRVTLELGGKNPCIVCAD-ADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQ- 325
Cdd:cd07126 222 RM--TLFTGSSKVAeRLALELHG-----KVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENw 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 326 VYGEFVRRSVEFAKKRPVGDpfdakTEQGP------QIDQKQFDKILELiesgkkEGAKLECGGS------------AME 387
Cdd:cd07126 295 VQAGILDKLKALAEQRKLED-----LTIGPvltwttERILDHVDKLLAI------PGAKVLFGGKpltnhsipsiygAYE 363
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 170650621 388 DRGLFIkPTVFSDVTDNMRIAKEEIFGPVQPILKFKN--LEEVIKRANSTDYGLTAAV 443
Cdd:cd07126 364 PTAVFV-PLEEIAIEENFELVTTEVFGPFQVVTEYKDeqLPLVLEALERMHAHLTAAV 420
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
70-459 |
2.33e-14 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 75.32 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 70 DVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKpflhaffvdleGciktfRYfagwAD 149
Cdd:PRK15398 37 SVDDAVAAAKVAQQR---YQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGM-----------G-----RV----ED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 150 KI-----QGRTIP----------TDDNVVCFTRHEPIGVCGAITPWNFP--------LLMLAwklapalcCGNTVVLKPA 206
Cdd:PRK15398 94 KIaknvaAAEKTPgvedlttealTGDNGLTLIEYAPFGVIGAVTPSTNPtetiinnaISMLA--------AGNSVVFSPH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 207 EQTPLTALYLASL----IKEVGFPPGVVNIVPGfgPTVGAA--ISSHPQINKIAFTGstevGKLVREAASRSNlKRVTLE 280
Cdd:PRK15398 166 PGAKKVSLRAIELlneaIVAAGGPENLVVTVAE--PTIETAqrLMKHPGIALLVVTG----GPAVVKAAMKSG-KKAIGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 281 LGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYGEFVRRSVEfakkrpvgdpfdaktEQGPQIDQK 360
Cdd:PRK15398 239 GAGNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEK---------------NGAVLLTAE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 361 QFDKILELIESGKKEGAKLECGGSA---MEDRGLFIKPTV---FSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANS 434
Cdd:PRK15398 304 QAEKLQKVVLKNGGTVNKKWVGKDAakiLEAAGINVPKDTrllIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVK 383
|
410 420
....*....|....*....|....*..
gi 170650621 435 TDYGL--TAAVFTKNLDKALKLAAALE 459
Cdd:PRK15398 384 LEHGNrhTAIMHSRNVDNLNKMARAIQ 410
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
170-459 |
7.65e-14 |
|
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: 73.43 E-value: 7.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 170 PIGVCGAITPWNFP--------LLMLAwklapalcCGNTVVLKPAEQTPLTALYLASL----IKEVGFPPGVVNIVPGfg 237
Cdd:cd07121 97 PFGVIGAITPSTNPtetiinnsISMLA--------AGNAVVFNPHPGAKKVSAYAVELinkaIAEAGGPDNLVVTVEE-- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 238 PTVGAA--ISSHPQINKIAFTGSTEVGKlvreaASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCT 315
Cdd:cd07121 167 PTIETTneLMAHPDINLLVVTGGPAVVK-----AALSSGKKAIGAGAGNPPVVVDETADIEKAARDIVQGASFDNNLPCI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 316 AASRVFVEEQVYGEFVRRSVEfakkrpvgdpfdaktEQGPQIDQKQFDKILELIESGKKEGA---KLEcGGSA---MEDR 389
Cdd:cd07121 242 AEKEVIAVDSVADYLIAAMQR---------------NGAYVLNDEQAEQLLEVVLLTNKGATpnkKWV-GKDAskiLKAA 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170650621 390 GLFIKPT---VFSDVTDNMRIAKEEIFGPVQPILKFKNLEEVIKRANSTDYGL--TAAVFTKNLDKALKLAAALE 459
Cdd:cd07121 306 GIEVPADirlIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENLTKMARAMQ 380
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
159-466 |
1.23e-08 |
|
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: 57.28 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 159 DDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKP----AEQTPLTALYLASLIKEVGFPPGVVNIVP 234
Cdd:cd07081 84 DENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWID 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 235 GFGPTVGAAISSHPQINKIAFTGSTEVGKlvreaASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCC 314
Cdd:cd07081 164 NPSIELAQRLMKFPGIGLLLATGGPAVVK-----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVIC 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 315 TAASRVFVEEQVYGEFVRRsvefakkrpvgdpfdAKTEQGPQIDQKQFDKILELIES---------GKKEGAKLECGGSA 385
Cdd:cd07081 239 ASEQSVIVVDSVYDEVMRL---------------FEGQGAYKLTAEELQQVQPVILKngdvnrdivGQDAYKIAAAAGLK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 386 M--EDRGLFIKPTVFsdvtDNMRIAKEEIFGPVQPILKFKNLEEVIKRA----NSTDYGLTAAVFTKNL---DKALKLAA 456
Cdd:cd07081 304 VpqETRILIGEVTSL----AEHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIkaiENMNQFAN 379
|
330
....*....|
gi 170650621 457 ALESGTVWIN 466
Cdd:cd07081 380 AMKTSRFVKN 389
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
169-467 |
3.85e-07 |
|
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: 52.49 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 169 EPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKE----VGFPPGVVNIVPgfGPTVGA-- 242
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREaavaAGAPEGLIQWIE--EPSIELtq 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 243 AISSHPQINKIAFTGStevGKLVREAASRSnlkrvTLELG---GKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASR 319
Cdd:cd07122 172 ELMKHPDVDLILATGG---PGMVKAAYSSG-----KPAIGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 320 VFVEEQVYGEFVRrsvEFAKkrpvgdpfdakteQGPQI----DQKQFDKILeLIESGK-------KEGAKL--ECGGSAM 386
Cdd:cd07122 244 VIVDDEIYDEVRA---ELKR-------------RGAYFlneeEKEKLEKAL-FDDGGTlnpdivgKSAQKIaeLAGIEVP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 387 EDRGLFIKPtvFSDVTDNMRIAKEEIFgPVQPILKFKNLEEVIKRANS-TDY---GLTAAVFTKNLDKALKLAAALESGT 462
Cdd:cd07122 307 EDTKVLVAE--ETGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKARElLEYggaGHTAVIHSNDEEVIEEFALRMPVSR 383
|
....*
gi 170650621 463 VWINC 467
Cdd:cd07122 384 ILVNT 388
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
67-471 |
4.12e-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: 52.48 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 67 DKPDVDKAVEAAQAAFQRgspWRRLDALSR-GQLLHQLADLVERDRAIL-ATLETmdTGKPFLHAFFVD----LEGCIKT 140
Cdd:cd07127 82 PQCDPDALLAAARAAMPG---WRDAGARARaGVCLEILQRLNARSFEMAhAVMHT--TGQAFMMAFQAGgphaQDRGLEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 141 FRYfagwADKIQGRTIPTDDNVVCFTRHEPI-----------GV-----CGAITPWN-FPLLMlawklaPALCCGNTVVL 203
Cdd:cd07127 157 VAY----AWREMSRIPPTAEWEKPQGKHDPLamektftvvprGValvigCSTFPTWNgYPGLF------ASLATGNPVIV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 204 KPAeqtPLTALYLASLIK-------EVGFPPGVVNIV---PGFGptVGAAISSHPQINKIAFTGSTEVGKLVREAASRsn 273
Cdd:cd07127 227 KPH---PAAILPLAITVQvarevlaEAGFDPNLVTLAadtPEEP--IAQTLATRPEVRIIDFTGSNAFGDWLEANARQ-- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 274 lKRVTLELGGKNPCIVcaDADLDLAVECAHQGVFFN--QGQCCTAASRVFV--------EEQVYGEFVRRSVEFAKKRPV 343
Cdd:cd07127 300 -AQVYTEKAGVNTVVV--DSTDDLKAMLRNLAFSLSlySGQMCTTPQNIYVprdgiqtdDGRKSFDEVAADLAAAIDGLL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170650621 344 GDPFDAKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDRGLFIKPTVFSDVTDNMRIAkEEIFGPVQPILKFK 423
Cdd:cd07127 377 ADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYA-EERFGPIAFVVATD 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170650621 424 NLEEVIKRANSTD----------YGLTAAVFTKNLDKALKLAAALE---SGTVWINCYNAF 471
Cdd:cd07127 456 STDHSIELARESVrehgamtvgvYSTDPEVVERVQEAALDAGVALSinlTGGVFVNQSAAF 516
|
|
| |
