|
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 ... |
27-506 |
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: 940.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 27 LEVKFTKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSPWRRLDALGRGRLLNQLADL 106
Cdd:cd07141 2 PEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLADL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 107 VERDRTVLATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLM 186
Cdd:cd07141 82 IERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 187 LVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVK 266
Cdd:cd07141 162 AAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 267 EAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDP 346
Cdd:cd07141 242 QAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 347 FDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIE 426
Cdd:cd07141 322 FDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTID 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 427 EVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 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: 836.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 32 TKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSpWRRLDALGRGRLLNQLADLVERDR 111
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 112 TVLATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKL 191
Cdd:cd07091 83 DELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 192 APALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASR 271
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 272 SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRT 351
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 352 EQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKR 431
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1304905828 432 ANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 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: 692.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 29 VKFTKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALGRGRLLNQLADLVE 108
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 109 RDRTVLATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLV 188
Cdd:cd07142 80 KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 189 WKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEA 268
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 269 ASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFD 348
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 349 VRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEV 428
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304905828 429 IKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 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: 675.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 32 TKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALGRGRLLNQLADLVERDR 111
Cdd:COG1012 6 YPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 112 TVLATLETMDTGKPFLHAFFiDLEGCVKTLRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWK 190
Cdd:COG1012 83 EELAALLTLETGKPLAEARG-EVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 191 LAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAAS 270
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 271 RsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVR 350
Cdd:COG1012 242 E-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 351 TEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMED-RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVI 429
Cdd:COG1012 321 TDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1304905828 430 KRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIY-AQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| 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: 667.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 32 TKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgSPWRR-LDALGRGRLLNQLADLVERD 110
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWGLkVSGSKRGRCLSKLADLMERN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 111 RTVLATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWK 190
Cdd:cd07143 85 LDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 191 LAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAAS 270
Cdd:cd07143 165 IAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 271 RSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVR 350
Cdd:cd07143 245 KSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 351 TEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIK 430
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1304905828 431 RANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
40-503 |
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: 663.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 40 WHESkSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALGRGRLLNQLADLVERDRTVLATLET 119
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 120 MDTGKPFLHAFFiDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGN 199
Cdd:pfam00171 77 LENGKPLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 200 TVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTL 279
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 280 ELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQ 359
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 360 KQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGL 439
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304905828 440 TAAVFTKNLDKALKLASALESGTVWINCYNAIYA-QAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
26-509 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 662.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 26 SLEVKFTKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALGRGRLLNQLAD 105
Cdd:PLN02466 52 PVQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTAYERSRILLRFAD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 106 LVERDRTVLATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLL 185
Cdd:PLN02466 131 LLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 186 MLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLV 265
Cdd:PLN02466 211 MFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 266 KEAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGD 345
Cdd:PLN02466 291 LELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 346 PFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNI 425
Cdd:PLN02466 371 PFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 426 EEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:PLN02466 451 DEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 530
|
....
gi 1304905828 506 KLDD 509
Cdd:PLN02466 531 PLKN 534
|
|
| 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: 655.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 32 TKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgSPWRRLDALGRGRLLNQLADLVERDR 111
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 112 TVLATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKL 191
Cdd:cd07144 86 DLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 192 APALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASr 271
Cdd:cd07144 166 APALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 272 SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKR-PVGDPFDVR 350
Cdd:cd07144 245 QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 351 TEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMED---RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEE 427
Cdd:cd07144 325 TVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 428 VIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 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: 618.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 72 DKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPfLHAFFIDLEGCVKTLRYFAGWADKI 151
Cdd:cd07078 1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 152 QGRTIPTDD-NVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVV 230
Cdd:cd07078 77 HGEVIPSPDpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 231 NIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQ 310
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 311 GQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAME-DR 389
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEgGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 390 GLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYN 469
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 1304905828 470 A-IYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07078 396 VgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
35-508 |
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: 604.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALGRGRLLNQLADLVERDRTVL 114
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSG-EWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 115 ATLETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPA 194
Cdd:cd07119 80 ARLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 195 LCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNL 274
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQG 354
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 355 PQIDQKQFDKILDLIESGKKEGAKLECGGSAMED----RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIK 430
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304905828 431 RANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLD 508
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLS 475
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
28-512 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 604.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 28 EVKFTKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALGRGRLLNQLADLV 107
Cdd:PLN02766 17 EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 108 ERDRTVLATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLML 187
Cdd:PLN02766 96 EEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 188 VWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKE 267
Cdd:PLN02766 176 FMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 268 AASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPF 347
Cdd:PLN02766 256 AAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 348 DVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEE 427
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 428 VIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPL 495
|
....*
gi 1304905828 508 DDkSP 512
Cdd:PLN02766 496 YN-SP 499
|
|
| 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: 588.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 46 GKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSpWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKP 125
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 126 FLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKP 205
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 206 AEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRSNLKRVTLELGGKN 285
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 286 PCIVCADA-DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDK 364
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 365 ILDLIESGKKEGAKLECGGSA--MEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAA 442
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1304905828 443 VFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 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: 578.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 51 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFqRGSPWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPfLHAF 130
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAF-EGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKL-IRET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 131 FIDLEGCVKTLRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQT 209
Cdd:cd07114 79 RAQVRYLAEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 210 PLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIV 289
Cdd:cd07114 159 PASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 290 CADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLI 369
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 370 ESGKKEGAKLECGGSAME----DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFT 445
Cdd:cd07114 318 ARAREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 446 KNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07114 398 RDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| 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: 569.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 51 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAF 130
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG---WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 131 FIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTP 210
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 211 LTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVC 290
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIE 370
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 371 SGKKEGAKLECGGSAME----DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTK 446
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1304905828 447 NLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| 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: 567.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 51 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAF 130
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 131 FIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTP 210
Cdd:cd07115 78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 211 LTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVC 290
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIE 370
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 371 SGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDK 450
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1304905828 451 ALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| 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: 558.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 28 EVKF-TKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALGRGRLLNQLADL 106
Cdd:cd07140 1 TLKMpHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENG-EWGKMNARDRGRLMYRLADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 107 VERDRTVLATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTD----DNVVCFTRHEPIGVCGAITPWNF 182
Cdd:cd07140 80 MEEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 183 PLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVG 262
Cdd:cd07140 160 PLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 263 KLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRP 342
Cdd:cd07140 240 KHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 343 VGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKF 422
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 423 KN--IEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEV 500
Cdd:cd07140 400 DDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKT 479
|
....*.
gi 1304905828 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: 532.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFf 131
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 132 IDLEGCVKTLRYFAGWADKIQGRTIPTDD-NVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTP 210
Cdd:cd07103 78 GEVDYAASFLEWFAEEARRIYGRTIPSPApGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 211 LTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVC 290
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIE 370
Cdd:cd07103 237 DDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 371 SGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDK 450
Cdd:cd07103 317 DAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1304905828 451 ALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 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: 529.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 33 KIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRT 112
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT---WGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 113 VLATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLA 192
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 193 PALCCGNTVVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRs 272
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 273 NLKRVTLELGGKNPCIVCADA-----DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPF 347
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 348 DVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGG----SAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFK 423
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGerltLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 424 NIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
....
gi 1304905828 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 |
2.25e-180 |
|
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: 514.36 E-value: 2.25e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 34 IFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAF---QRGSPWRRLDalgrgrLLNQLADLVERD 110
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFpawSATSVEERAA------LLERIAEAYEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 111 RTVLATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVcftrHEPIGVCGAITPWNFPLLMLVWK 190
Cdd:cd07138 75 ADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEERRGNSLVV----REPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 191 LAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAAS 270
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 271 RSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVR 350
Cdd:cd07138 231 DT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 351 TEQGPQIDQKQFDKILDLIESGKKEGAKLECGGS---AMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEE 427
Cdd:cd07138 310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1304905828 428 VIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINcYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
52-505 |
1.41e-179 |
|
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: 511.69 E-value: 1.41e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFF 131
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG---WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 132 iDLEGCVKTLRYFAGWAdkIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPL 211
Cdd:cd07106 79 -EVGGAVAWLRYTASLD--LPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 212 TALYLGSLIKEVgFPPGVVNIVPGfGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVCA 291
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 292 DADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIES 371
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 372 GKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKA 451
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1304905828 452 LKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
35-509 |
2.00e-179 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 512.89 E-value: 2.00e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLV-ERDRtV 113
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERND-E 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 114 LATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAP 193
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 194 ALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPtVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRSn 273
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 274 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQ 353
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 354 GPQIDQKQFDKILDLIESGKKEGAKLECGGSAME----DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVI 429
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTeggfANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 430 KRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLDD 509
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEMGP 483
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
51-503 |
1.05e-177 |
|
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: 507.23 E-value: 1.05e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 51 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAF 130
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 131 fIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTP 210
Cdd:cd07090 78 -VDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 211 LTALYLGSLIKEVGFPPGVVNIVPGFGPTvGAAMSSHPQISKLAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVC 290
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIE 370
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 371 SGKKEGAKLECGGS--AMED---RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFT 445
Cdd:cd07090 315 SAKQEGAKVLCGGErvVPEDgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1304905828 446 KNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
65-505 |
4.79e-177 |
|
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: 505.33 E-value: 4.79e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 65 EGDKPDVDKAVEAAQAAFQRGsPWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFFiDLEGCVKTLRYF 144
Cdd:cd07118 15 EGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EIEGAADLWRYA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 145 AGWADKIQGRTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEV 223
Cdd:cd07118 93 ASLARTLHGDSYNNlGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 224 GFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAH 303
Cdd:cd07118 173 GLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFADADLDAAADAVV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 304 QGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGG 383
Cdd:cd07118 252 FGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 384 SAMEDR-GLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGT 462
Cdd:cd07118 332 ERLASAaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGT 411
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1304905828 463 VWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07118 412 VWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
33-507 |
1.18e-176 |
|
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: 505.45 E-value: 1.18e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 33 KIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRT 112
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT---WRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 113 VLATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLA 192
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 193 PALCCGNTVVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRs 272
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 273 NLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTE 352
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 353 QGPQIDQKQFDKILDLIESGKKEGAKLECGG----SAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEV 428
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGhrltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1304905828 429 IKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
35-501 |
7.21e-175 |
|
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: 500.49 E-value: 7.21e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVL 114
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGE---WAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 115 ATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPA 194
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 195 LCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASrSNL 274
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQG 354
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 355 PQIDQKQFDKILDLIESGKKEGAKLECGGSAME----DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIK 430
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPEnvglQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1304905828 431 RANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVK 501
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
51-504 |
3.53e-174 |
|
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: 498.41 E-value: 3.53e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 51 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPfLHAF 130
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR---WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKP-LDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 131 FIDLEGCVKTLRYFAGWADKI---QGRTIPTDDN-VVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPA 206
Cdd:cd07110 77 AWDVDDVAGCFEYYADLAEQLdakAERAVPLPSEdFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 207 EQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNP 286
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKIL 366
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 367 DLIESGKKEGAKLECGGSAME--DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVF 444
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 445 TKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
76-505 |
2.69e-173 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 492.51 E-value: 2.69e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 76 EAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPfLHAFFIDLEGCVKTLRYFAGWADKIQGRT 155
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKP-IEEALGEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 156 IP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVP 234
Cdd:cd06534 77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 235 GFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCC 314
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 315 TAASRVFVEEQVYAEFVRRSVeyakkrpvgdpfdvrteqgpqidqkqfdkildliesgkkegaklecggsamedrglfik 394
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 395 pTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIY-A 473
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVgP 335
|
410 420 430
....*....|....*....|....*....|..
gi 1304905828 474 QAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
52-505 |
2.28e-170 |
|
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: 488.67 E-value: 2.28e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFf 131
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESG--WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 132 IDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPL 211
Cdd:cd07109 79 ADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 212 TALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCA 291
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 292 DADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDvRTEQGPQIDQKQFDKILDLIES 371
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 372 GKKEGAKLECGGSAMEDR---GLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNL 448
Cdd:cd07109 317 ARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 449 DKALKLASALESGTVWINCYNA---IyaQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNYGAgggI--ELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
35-503 |
2.47e-168 |
|
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: 484.06 E-value: 2.47e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESKSGKkfATYNPSTL-EKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTV 113
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSDTsDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 114 LATLETMDTGKPFLHAFFiDLEGCVKTLRYFAGWADKIQGRTIP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLA 192
Cdd:cd07097 79 LARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 193 PALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASrS 272
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 273 NLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTE 352
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 353 QGPQIDQKQFDKILDLIESGKKEGAKLECGGSA--MEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIK 430
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304905828 431 RANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYA-QAPFGGFKMSGNG-RELGEYALAEYTEVKTV 503
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDyHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
35-505 |
1.60e-167 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 481.76 E-value: 1.60e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALGRGRLLNQLADLVERDRTVL 114
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAA-QKA--WERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 115 ATLETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAP 193
Cdd:cd07088 78 AKLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDrPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 194 ALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsN 273
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-N 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 274 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQ 353
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 354 GPQIDQKQFDKILDLIESGKKEGAKLECGGSAME-DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRA 432
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1304905828 433 NSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
52-505 |
4.36e-167 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 479.90 E-value: 4.36e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFF 131
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPS---WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 132 IDLEGCVKTLRYFAGWADKIQGRT----IPtddNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAE 207
Cdd:cd07092 79 DELPGAVDNFRFFAGAARTLEGPAageyLP---GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 208 QTPLTALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPC 287
Cdd:cd07092 156 TTPLTTLLLAELAAEV-LPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILD 367
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 368 LIEsGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKN 447
Cdd:cd07092 314 FVE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1304905828 448 LDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
31-507 |
1.10e-163 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 472.47 E-value: 1.10e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 31 FTKIFINNEWhESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERD 110
Cdd:PRK13473 2 QTKLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE---WSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 111 RTVLATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTipTDDNVVCFT---RHEPIGVCGAITPWNFPLLML 187
Cdd:PRK13473 78 ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKA--AGEYLEGHTsmiRRDPVGVVASIAPWNYPLMMA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 188 VWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKE 267
Cdd:PRK13473 156 AWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 268 AASRSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPF 347
Cdd:PRK13473 235 AAADS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 348 DVRTEQGPQIDQKQFDKILDLIESGKKEG-AKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIE 426
Cdd:PRK13473 314 DEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 427 EVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
|
.
gi 1304905828 507 L 507
Cdd:PRK13473 474 H 474
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
51-507 |
1.56e-163 |
|
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: 471.09 E-value: 1.56e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 51 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPfLHAF 130
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE---WRATTPLERARMLRELATRLREHAEELALIDALDCGNP-VSAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 131 FIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTP 210
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 211 LTALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRSnLKRVTLELGGKNPCIVC 290
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 291 ADADLDLAVECAHQGVFFN-QGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLI 369
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 370 ESGKKEGAKLECGGSAMED----RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFT 445
Cdd:cd07107 315 DSAKREGARLVTGGGRPEGpaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304905828 446 KNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
35-505 |
1.88e-163 |
|
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: 471.83 E-value: 1.88e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESKSGKKFATYNPSTLEKIC-EVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALGRGRLLNQLADLVERDRTV 113
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVVgTFPLSTASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 114 LATLETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLA 192
Cdd:cd07131 79 LARLVTREMGKPLAEGR-GDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 193 PALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRS 272
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 273 NlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTE 352
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 353 QGPQIDQKQFDKILDLIESGKKEGAKLECGGSAME----DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEV 428
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTgggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 429 IKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAiYAQAPFGGFKMSGNG-RELGEYALAEYTEVKTVTI 505
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIGA-EVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
19-504 |
7.02e-162 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 468.83 E-value: 7.02e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 19 ALPRPVRSLevkftkiFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQR--GSPWRRLDALGR 96
Cdd:PLN02467 2 AIPVPRRQL-------FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkGKDWARTTGAVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 97 GRLLNQLADLVERDRTVLATLETMDTGKPFLHAFF--IDLEGCVKtlrYFAGWADKIQGR-----TIPtDDNVVCFTRHE 169
Cdd:PLN02467 75 AKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWdmDDVAGCFE---YYADLAEALDAKqkapvSLP-METFKGYVLKE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 170 PIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQ 249
Cdd:PLN02467 151 PLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 250 ISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAE 329
Cdd:PLN02467 231 VDKIAFTGSTATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 330 FVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMED--RGLFIKPTVFSEVTDTMRI 407
Cdd:PLN02467 310 FLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 408 AKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGR 487
Cdd:PLN02467 390 WREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGR 469
|
490
....*....|....*..
gi 1304905828 488 ELGEYALAEYTEVKTVT 504
Cdd:PLN02467 470 ELGEWGLENYLSVKQVT 486
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
52-503 |
3.84e-161 |
|
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: 465.18 E-value: 3.84e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRlDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFF 131
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTG-DWST-DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 132 IDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVC-----FTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPA 206
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEFDLPVPALRGgpgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 207 EQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNP 286
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKIL 366
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 367 DLIESGKKEGAKLECGGSAME--DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVF 444
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAglDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1304905828 445 TKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
70-505 |
4.77e-161 |
|
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: 463.93 E-value: 4.77e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 70 DVDKAVEAAQAAFQrgsPWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFFiDLEGCVKTLRYFAGWAD 149
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAF-EVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 150 KIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLT-ALYLGSLIKEVGFPP 227
Cdd:cd07104 77 RPEGEILPSDvPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 228 GVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVF 307
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 308 FNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAme 387
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 388 dRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINC 467
Cdd:cd07104 314 -EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 1304905828 468 YNAI-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07104 393 QTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
53-505 |
1.49e-159 |
|
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: 461.06 E-value: 1.49e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 53 NPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFFI 132
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 133 DLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLT 212
Cdd:cd07108 80 EAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 213 ALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLV-KEAASRsnLKRVTLELGGKNPCIVCA 291
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIyRAAADR--LIPVSLELGGKSPMIVFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 292 DADLDLAVECAHQGV-FFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIE 370
Cdd:cd07108 237 DADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 371 SGKKE-GAKLECGGSAMED----RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFT 445
Cdd:cd07108 317 LGLSTsGATVLRGGPLPGEgplaDGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1304905828 446 KNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELG-EYALAEYTEVKTVTI 505
Cdd:cd07108 397 RDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
34-505 |
2.14e-155 |
|
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: 450.87 E-value: 2.14e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 34 IFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALGRGRLLNQLADLVERDRTV 113
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 114 LATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADK---IQGRTIPTDDNVVcfTRHEPIGVCGAITPWNFPLLMLVWK 190
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDfpfEERRPGSGGGHVL--VRREPVGVVAAIVPWNAPLFLAALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 191 LAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGfGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAAS 270
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 271 RsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVR 350
Cdd:cd07139 237 E-RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 351 TEQGPQIDQKQFDKILDLIESGKKEGAKLECGGS--AMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEV 428
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1304905828 429 IKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYnAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
49-505 |
5.27e-155 |
|
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: 449.47 E-value: 5.27e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 49 FATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLH 128
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 129 AFFiDLEGCVKTLRYFAGWADKIQGRTIPTDDN-VVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAE 207
Cdd:cd07150 78 AWF-ETTFTPELLRAAAGECRRVRGETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 208 QTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPC 287
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILD 367
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 368 LIESGKKEGAKLECGGsamEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKN 447
Cdd:cd07150 316 QVEDAVAKGAKLLTGG---KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 448 LDKALKLASALESGTVWINCyNAIY--AQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07150 393 LQRAFKLAERLESGMVHIND-PTILdeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
35-497 |
3.23e-154 |
|
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: 448.38 E-value: 3.23e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVL 114
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES---WSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 115 ATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQgrtipTDdnvvcFTRHEPIGVCGAITPWNFPLLMLVWKLAPA 194
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLD-----TE-----LAGWKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 195 LCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGfGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRSNl 274
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTG- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQG 354
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 355 PQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANS 434
Cdd:cd07111 330 AIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANN 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1304905828 435 LEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEY 497
Cdd:cd07111 410 TPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
15-503 |
1.53e-152 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 444.90 E-value: 1.53e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 15 RKPPALPRPVRSLEVKFTKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDAL 94
Cdd:PLN02278 8 MDAQSALVKLRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLTAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 95 GRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGRTIPTDD-NVVCFTRHEPIGV 173
Cdd:PLN02278 85 ERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAI-GEVAYGASFLEYFAEEAKRVYGDIIPSPFpDRRLLVLKQPVGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 174 CGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKL 253
Cdd:PLN02278 164 VGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 254 AFTGSTEVGKLVKEAASRSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRR 333
Cdd:PLN02278 244 TFTGSTAVGKKLMAGAAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 334 SVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIF 413
Cdd:PLN02278 323 FSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 414 GPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYA 493
Cdd:PLN02278 403 GPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYG 482
|
490
....*....|
gi 1304905828 494 LAEYTEVKTV 503
Cdd:PLN02278 483 IDEYLEIKYV 492
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
32-508 |
5.14e-152 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 443.18 E-value: 5.14e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 32 TKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSpWRRLDALGRGRLLNQLADLVERDR 111
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLADLMEAHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 112 TVLATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKL 191
Cdd:PRK09847 99 EELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 192 APALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASR 271
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 272 SNLKRVTLELGGKNPCIVCADA-DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVR 350
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 351 TEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAmeDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIK 430
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNA--GLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304905828 431 RANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLD 508
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISLE 494
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
35-506 |
6.59e-149 |
|
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: 434.95 E-value: 6.59e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgSPWRRLDALGRGRLLNQLADLVERDRTVL 114
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 115 ATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTI------PTDDNVVCFTRHEPIGVCGAITPWNFPLLMLV 188
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLapsipsMQGERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 189 WKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGpTVGAAMSSHPQISKLAFTGSTEVGKLVKEA 268
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 269 ASrSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFD 348
Cdd:cd07113 240 AA-SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 349 VRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEV 428
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304905828 429 IKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
49-505 |
1.07e-147 |
|
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: 431.00 E-value: 1.07e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 49 FATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLH 128
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV---MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 129 AFfIDLEGCVKTLRYFAGWADKIQGRTIPTDD-----NVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVV 203
Cdd:cd07145 78 SR-VEVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 204 KPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLV-KEAASRsnLKRVTLELG 282
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIaSKAGGT--GKKVALELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 283 GKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQF 362
Cdd:cd07145 235 GSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 363 DKILDLIESGKKEGAKLECGGSAMEdrGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAA 442
Cdd:cd07145 315 ERMENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1304905828 443 VFTKNLDKALKLASALESGTVWINCYNAI-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07145 393 VFTNDINRALKVARELEAGGVVINDSTRFrWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
52-505 |
1.67e-147 |
|
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: 430.09 E-value: 1.67e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGspwRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPfLHAFF 131
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKP-IKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 132 IDLEGCVKTLRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPA 206
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKRLAGETIPFDaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 207 EQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASrsnLKRVTLELGGKNP 286
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGSNAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKIL 366
Cdd:cd07149 237 VIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 367 DLIESGKKEGAKLECGGSAmedRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTK 446
Cdd:cd07149 317 EWVEEAVEGGARLLTGGKR---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTN 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 447 NLDKALKLASALESGTVWIN-CYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07149 394 DLQKALKAARELEVGGVMINdSSTFRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
35-505 |
2.37e-147 |
|
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: 430.83 E-value: 2.37e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESkSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVL 114
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 115 ATLETMDTGKPFLHAF-----FIDLegCvktlRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLV 188
Cdd:cd07086 78 GRLVSLEMGKILPEGLgevqeMIDI--C----DYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 189 WKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEV----GFPPGVVNIVPGFGPtVGAAMSSHPQISKLAFTGSTEVGKL 264
Cdd:cd07086 152 WNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 265 VKEAASRSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVG 344
Cdd:cd07086 231 VGETVARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 345 DPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAME--DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKF 422
Cdd:cd07086 310 DPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDggEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 423 KNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALES--GTVWIN--CYNAiYAQAPFGGFKMSGNGRELGEYALAEYT 498
Cdd:cd07086 390 DSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVNipTSGA-EIGGAFGGEKETGGGRESGSDAWKQYM 468
|
....*..
gi 1304905828 499 EVKTVTI 505
Cdd:cd07086 469 RRSTCTI 475
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
34-504 |
4.01e-140 |
|
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: 413.54 E-value: 4.01e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 34 IFINNEwhESKSGKKFATYNPS-TLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRT 112
Cdd:cd07124 35 LVIGGK--EVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPT---WRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 113 VLATLETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLA 192
Cdd:cd07124 110 ELAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 193 PALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASR- 271
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 272 ----SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPF 347
Cdd:cd07124 269 qpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 348 DVRTEQGPQIDQKQFDKILDLIESGKKEGaKLECGGSAMED--RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNI 425
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 426 EEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAIYAQAPFGGFKMSG-NGRELGEYALAEYTEVKT 502
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGtGSKAGGPDYLLQFMQPKT 507
|
..
gi 1304905828 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 |
6.60e-140 |
|
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: 411.85 E-value: 6.60e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVL 114
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA---WGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 115 ATLETMDTGKPFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPA 194
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 195 LCCGNTVVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNL 274
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 275 KRVTLELGGKNPCIVCA------DADLDLAVECAhqGVF-FNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPF 347
Cdd:cd07116 239 IPVTLELGGKSPNIFFAdvmdadDAFFDKALEGF--VMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 348 DVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGL----FIKPTVFSEvTDTMRIAKEEIFGPVQPILKFK 423
Cdd:cd07116 317 DTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 424 NIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07116 396 DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNL 475
|
..
gi 1304905828 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 |
1.19e-136 |
|
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: 403.72 E-value: 1.19e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESksGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGsPWRRLDALGRGRLLNQLADLVERDRTVL 114
Cdd:TIGR03216 4 FINGAFVES--GKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAA-LKG-PWGKMTVAERADLLYAVADEIERRFDDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 115 ATLETMDTGKPFLHAFFIDLEGCVKTLRYFAgwaDKIqgRTIPTD---------DNVVCFTRHEPIGVCGAITPWNFPLL 185
Cdd:TIGR03216 80 LAAEVADTGKPRSLASHLDIPRGAANFRVFA---DVV--KNAPTEcfematpdgKGALNYAVRKPLGVVGVISPWNLPLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 186 MLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGP-TVGAAMSSHPQISKLAFTGSTEVGKL 264
Cdd:TIGR03216 155 LMTWKVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGETRTGSA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 265 VKEAASRSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVG 344
Cdd:TIGR03216 235 IMKAAADG-VKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 345 DPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGG-----SAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPI 419
Cdd:TIGR03216 314 VPDDPATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGgvpdfGDALAGGAWVQPTIWTGLPDSARVVTEEIFGPCCHI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 420 LKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTE 499
Cdd:TIGR03216 394 APFDSEEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTE 473
|
....*...
gi 1304905828 500 VKTVTIKL 507
Cdd:TIGR03216 474 LTNVCIKL 481
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
38-506 |
1.47e-136 |
|
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: 402.84 E-value: 1.47e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 38 NEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRgsPWRRLDALGRGRLLNQLADLVERDRTVLATL 117
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA-QK--EWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 118 ETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGRTIPTD----DNVVcftRHEPIGVCGAITPWNFPLLMLVWKLAP 193
Cdd:cd07151 78 LIRESGSTRIKAN-IEWGAAMAITREAATFPLRMEGRILPSDvpgkENRV---YREPLGVVGVISPWNFPLHLSMRSVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 194 ALCCGNTVVVKPAEQTPLTA-LYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRs 272
Cdd:cd07151 154 ALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 273 NLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTE 352
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 353 QGPQIDQKQFDKILDLIESGKKEGAKLECGGSAmedRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRA 432
Cdd:cd07151 313 VGPLINESQVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELA 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1304905828 433 NSLEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAiYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:cd07151 390 NDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINdqPVND-EPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
51-504 |
8.51e-134 |
|
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: 395.56 E-value: 8.51e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 51 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFqRGSPWRRlDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAF 130
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAF-DETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 131 FiDLEGCVKTLRYFAGWADKIQGRTI-PTDDNVVCFTRhEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQT 209
Cdd:cd07120 79 F-EISGAISELRYYAGLARTEAGRMIePEPGSFSLVLR-EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 210 PLTALYLGSLIKEV-GFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCI 288
Cdd:cd07120 157 AQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPCI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 289 VCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDL 368
Cdd:cd07120 236 VFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 369 IESGKKEGAK-LECGGSAMED--RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFT 445
Cdd:cd07120 316 VERAIAAGAEvVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1304905828 446 KNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07120 396 RDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
52-501 |
1.02e-131 |
|
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: 389.87 E-value: 1.02e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAff 131
Cdd:TIGR01780 2 YNPATGEIIGSVPDQGVDETEAAIRAAYEAFKT---WRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 132 idlEGCVKT----LRYFAGWADKIQGRTIPT--DDNVVCFTRhEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKP 205
Cdd:TIGR01780 77 ---KGEILYaasfLEWFAEEAKRVYGDTIPSpqSDKRLIVIK-QPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 206 AEQTPLTALYLGSLIKEVGFPPGVVNIVPG-FGPTVGAAMSSHPQISKLAFTGSTEVGK-LVKEAAsrSNLKRVTLELGG 283
Cdd:TIGR01780 153 AEQTPLSALALARLAEQAGIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNVGKiLMKQSA--STVKKVSMELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 284 KNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFD 363
Cdd:TIGR01780 231 NAPFIVFDDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 364 KILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAV 443
Cdd:TIGR01780 311 KVEKHIADAVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYF 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1304905828 444 FTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVK 501
Cdd:TIGR01780 391 FSRDLSRIWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
53-505 |
3.05e-131 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 388.71 E-value: 3.05e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 53 NPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFfI 132
Cdd:cd07094 5 NPYDGEVIGKVPADDRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR-V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 133 DLEGCVKTLRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAE 207
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 208 QTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASrsnLKRVTLELGGKNPC 287
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILD 367
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 368 LIESGKKEGAKLECGGsamEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKN 447
Cdd:cd07094 318 WVEEAVEAGARLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1304905828 448 LDKALKLASALESGTVWINCYNAIYAQA-PFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
70-505 |
2.94e-130 |
|
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: 385.39 E-value: 2.94e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 70 DVDKAVEAAQAAFQrgsPWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFFiDLEGCVKTLRYFAGWAD 149
Cdd:cd07105 1 DADQAVEAAAAAFP---AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGF-NVDLAAGMLREAASLIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 150 KIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPG 228
Cdd:cd07105 77 QIIGGSIPSDkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 229 VVNIV---PGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQG 305
Cdd:cd07105 157 VLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 306 VFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDpfdvrTEQGPQIDQKQFDKILDLIESGKKEGAKLECGG-S 384
Cdd:cd07105 236 AFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGlA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 385 AMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVW 464
Cdd:cd07105 311 DESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1304905828 465 INCYNaIY--AQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07105 391 INGMT-VHdePTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
52-505 |
4.05e-130 |
|
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: 385.81 E-value: 4.05e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPfLHAFF 131
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAA-QRA--WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 132 IDLEGCVKTLRYFAGWADKI-QGRTIPTDD---NVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAE 207
Cdd:cd07099 77 LEVLLALEAIDWAARNAPRVlAPRKVPTGLlmpNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 208 QTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTvGAAMSSHPqISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPC 287
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILD 367
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 368 LIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKN 447
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 448 LDKALKLASALESGTVWINC--YNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
33-506 |
2.07e-129 |
|
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: 384.62 E-value: 2.07e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 33 KIFINNEWHESkSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQ----RGSPWRRLDALGRgrllnqLADLVE 108
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRgwwpTMPLEERIDCLHK------FADLLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 109 RDRTVLATLETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFP 183
Cdd:cd07082 76 ENKEEVANLLMWEIGKTLKDAL-KEVDRTIDYIRDTIEELKRLDGDSLPGDwfpgtKGKIAQVRREPLGVVLAIGPFNYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 184 LLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGK 263
Cdd:cd07082 155 LNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 264 LVKEAASRsnlKRVTLELGGKNPCIVCADADLDLAV-ECAHQGVFFNqGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRP 342
Cdd:cd07082 235 RLKKQHPM---KRLVLELGGKDPAIVLPDADLELAAkEIVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 343 VGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEdrGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKF 422
Cdd:cd07082 311 VGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 423 KNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNA----IYaqaPFGGFKMSGNGRELGEYALAEYT 498
Cdd:cd07082 389 NDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrgpdHF---PFLGRKDSGIGTQGIGDALRSMT 465
|
....*...
gi 1304905828 499 EVKTVTIK 506
Cdd:cd07082 466 RRKGIVIN 473
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
71-505 |
3.95e-129 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 382.58 E-value: 3.95e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 71 VDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFF-IDLegCVKTLRYFAGWAD 149
Cdd:cd07100 1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAeVEK--CAWICRYYAENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 150 K-IQGRTIPTDDNVvCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPG 228
Cdd:cd07100 76 AfLADEPIETDAGK-AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 229 VVNIVPGFGPTVGAAMSsHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFF 308
Cdd:cd07100 155 VFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 309 NQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMED 388
Cdd:cd07100 233 NAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 389 RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCY 468
Cdd:cd07100 313 PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGM 392
|
410 420 430
....*....|....*....|....*....|....*..
gi 1304905828 469 NAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07100 393 VKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
58-505 |
1.47e-128 |
|
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: 381.64 E-value: 1.47e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 58 EKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFFiDLEGC 137
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAA-QRA--WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGF-EVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 138 VKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTA-LYL 216
Cdd:cd07152 78 IGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 217 GSLIKEVGFPPGVVNIVPGfGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLD 296
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 297 LAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEG 376
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 377 AKLECGGSAmedRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLAS 456
Cdd:cd07152 316 ARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1304905828 457 ALESGTVWINCYNAIY-AQAPFGGFKMSGNGRELGEYA-LAEYTEVKTVTI 505
Cdd:cd07152 393 RLRTGMLHINDQTVNDePHNPFGGMGASGNGSRFGGPAnWEEFTQWQWVTV 443
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
36-507 |
4.41e-123 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 370.03 E-value: 4.41e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 36 INNEWHESKsgKKFATYNPS-TLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVL 114
Cdd:PRK03137 41 IGGERITTE--DKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFET---WKKWSPEDRARILLRAAAIIRRRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 115 ATLETMDTGKPFLHAFfIDLEGCVKTLRYFA----GWADKIQGRTIPTDDNvvcFTRHEPIGVCGAITPWNFPLLMLVWK 190
Cdd:PRK03137 116 SAWLVKEAGKPWAEAD-ADTAEAIDFLEYYArqmlKLADGKPVESRPGEHN---RYFYIPLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 191 LAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAAS 270
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 271 RSN-----LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGD 345
Cdd:PRK03137 272 KVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 346 PFDvRTEQGPQIDQKQFDKILDLIESGKKEGaKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNI 425
Cdd:PRK03137 352 PED-NAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 426 EEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAIYAQAPFGGFKMSGNGRELG--EYaLAEYTEVK 501
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGFNMSGTDSKAGgpDY-LLLFLQAK 508
|
....*.
gi 1304905828 502 TVTIKL 507
Cdd:PRK03137 509 TVSEMF 514
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
42-504 |
2.44e-120 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 363.43 E-value: 2.44e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 42 ESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALGRGRLLNQLADLVERDRTVLATLETMD 121
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QRA--WAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 122 TGKPFLHAF--FIDLegcVKTLRYFAGWADKI------QGrTIPTDDNVVcfTRHEPIGVCGAITPWNFPLLMLVWKLAP 193
Cdd:PRK09407 104 TGKARRHAFeeVLDV---ALTARYYARRAPKLlaprrrAG-ALPVLTKTT--ELRQPKGVVGVISPWNYPLTLAVSDAIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 194 ALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHpqISKLAFTGSTEVGKLVKEAASRsN 273
Cdd:PRK09407 178 ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGR-R 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 274 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQ 353
Cdd:PRK09407 255 LIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 354 GPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRG-LFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRA 432
Cdd:PRK09407 335 GSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304905828 433 NSLEYGLTAAVFTKNLDKALKLASALESGTVWIN-CYNAIYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:PRK09407 415 NDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNeGYAAAWGsvDAPMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
53-505 |
4.19e-120 |
|
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: 360.14 E-value: 4.19e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 53 NPSTLEKICEVEEGDKPDVDKAVEAAqaafqrGSPWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFFi 132
Cdd:cd07146 5 NPYTGEVVGTVPAGTEEALREALALA------ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 133 DLEGCVKTLRYFAGWADKIQGRTIPTDDNV-----VCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAE 207
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFSCDLTAngkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 208 QTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASrsnLKRVTLELGGKNPC 287
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILD 367
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 368 LIESGKKEGAKLECGGsamEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKN 447
Cdd:cd07146 315 RVEEAIAQGARVLLGN---QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304905828 448 LDKALKLASALESGTVWIN---CYNAiyAQAPFGGFKMSGNG-RELGEYALAEYTEVKTVTI 505
Cdd:cd07146 392 LDTIKRLVERLDVGTVNVNevpGFRS--ELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
54-504 |
3.24e-116 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 350.46 E-value: 3.24e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 54 PSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFfID 133
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA-QRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAF-EE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 134 LEGCVKTLRYFAGWADKI-----QGRTIPT-DDNVVCftrHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAE 207
Cdd:cd07101 79 VLDVAIVARYYARRAERLlkprrRRGAIPVlTRTTVN---RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 208 QTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQIskLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPC 287
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAGR-RLIGCSLELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILD 367
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 368 LIESGKKEGAKLECGGSAMEDRG-LFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTK 446
Cdd:cd07101 313 HVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1304905828 447 NLDKALKLASALESGTVWIN-CYNAIYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNeGYAAAWAsiDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
32-504 |
1.77e-114 |
|
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: 346.81 E-value: 1.77e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 32 TKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDR 111
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 112 TVLATLETMDTGKPFLHAffidlEGCVktLR-----YFA-GWADKIQGRTIP-TDDNVVCFTRHEPIGVCGAITPWNFPL 184
Cdd:cd07085 78 DELARLITLEHGKTLADA-----RGDV--LRglevvEFAcSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 185 LMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGaAMSSHPQISKLAFTGSTEVGKL 264
Cdd:cd07085 151 MIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVN-ALLDHPDIKAVSFVGSTPVGEY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 265 VKEAASRSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVG 344
Cdd:cd07085 230 IYERAAANG-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 345 DPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGG----SAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPIL 420
Cdd:cd07085 309 AGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGrgvkVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 421 KFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINcynaIYAQAP-----FGGFKMS--GNGRELGEYA 493
Cdd:cd07085 389 RVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VPIPVPlaffsFGGWKGSffGDLHFYGKDG 464
|
490
....*....|.
gi 1304905828 494 LAEYTEVKTVT 504
Cdd:cd07085 465 VRFYTQTKTVT 475
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
52-505 |
6.76e-114 |
|
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: 344.23 E-value: 6.76e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFF 131
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 132 iDLEGCVKTLRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPA 206
Cdd:cd07147 81 -EVARAIDTFRIAAEEATRIYGEVLPLDisargEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 207 EQTPLTALYLGSLIKEVGFPPGVVNIVPGfgPTVGAAM-SSHPQISKLAFTGSTEVGKLVKEAASRsnlKRVTLELGGKN 285
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 286 PCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKI 365
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 366 LDLIESGKKEGAKLECGGsamEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFT 445
Cdd:cd07147 315 EGWVNEAVDAGAKLLTGG---KRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1304905828 446 KNLDKALKLASALESGTVWINCYNAIYA-QAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07147 392 RDLEKALRAWDELEVGGVVINDVPTFRVdHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
35-507 |
1.52e-112 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 341.89 E-value: 1.52e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALGRGRLLNQLADLVERDRTVL 114
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRWFNLMMEHQDDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 115 ATLETMDTGKPFLHAFFiDLEGCVKTLRYFAGWADKIQGRTIP---TDDNVVCFTrhEPIGVCGAITPWNFPLLMLVWKL 191
Cdd:PRK11241 91 ARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTIPghqADKRLIVIK--QPIGVTAAITPWNFPAAMITRKA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 192 APALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASR 271
Cdd:PRK11241 168 GPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 272 sNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRT 351
Cdd:PRK11241 248 -DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 352 EQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKR 431
Cdd:PRK11241 327 TIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQ 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1304905828 432 ANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:PRK11241 407 ANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
34-504 |
1.92e-112 |
|
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: 342.62 E-value: 1.92e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 34 IFINNEWHESKSgkKFATYNPS-TLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRT 112
Cdd:TIGR01237 35 LVINGERVETEN--KIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEA---WKKTDPEERAAILFKAAAIVRRRRH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 113 VLATLETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGR----TIPTDDNVVCFTrhePIGVCGAITPWNFPLLMLV 188
Cdd:TIGR01237 110 EFSALLVKEVGKPWNEAD-AEVAEAIDFMEYYARQMIELAKGkpvnSREGETNQYVYT---PTGVTVVISPWNFPFAIMV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 189 WKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEA 268
Cdd:TIGR01237 186 GMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFER 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 269 ASR-----SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPV 343
Cdd:TIGR01237 266 AAKvqpgqKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 344 GDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGaKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFK 423
Cdd:TIGR01237 346 GPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRAS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 424 NIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAIYAQAPFGGFKMSGNGRELG--EYaLAEYTE 499
Cdd:TIGR01237 425 DFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrnITGAIVGYQPFGGFKMSGTDSKAGgpDY-LALFMQ 503
|
....*
gi 1304905828 500 VKTVT 504
Cdd:TIGR01237 504 AKTVT 508
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
141-508 |
1.00e-111 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 337.09 E-value: 1.00e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 141 LRYFAGWADKIQGRTIPTD---DNVVCFTRhePIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLG 217
Cdd:PRK10090 41 IDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 218 SLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDL 297
Cdd:PRK10090 119 KIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 298 AVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRT-EQGPQIDQKQFDKILDLIESGKKEG 376
Cdd:PRK10090 198 AVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 377 AKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLAS 456
Cdd:PRK10090 278 ARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIK 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1304905828 457 ALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLD 508
Cdd:PRK10090 358 GLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVVYLQSD 409
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
45-503 |
1.40e-107 |
|
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: 329.03 E-value: 1.40e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 45 SGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgSPWRRLDALgRGRLLNQLADLVERDRTVLATLETMDTGK 124
Cdd:TIGR04284 13 SAGTFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDE-TDWSRDTAL-RVRCLRQLRDALRAHVEELRELTIAEVGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 125 PFLHAFFIDLEGCVKTLRYFAGWADKIQGRT---------IPTDDNVvcftRHEPIGVCGAITPWNFPLLMLVWKLAPAL 195
Cdd:TIGR04284 91 PRMLTAGAQLEGPVDDLGFAADLAESYAWTTdlgvaspmgIPTRRTL----RREAVGVVGAITPWNFPHQINLAKLGPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 196 CCGNTVVVKPAEQTPLTALYLGSLIKE-VGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRSnL 274
Cdd:TIGR04284 167 AAGNTVVLKPAPDTPWCAAVLGELIAEhTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRAVMADAAAT-L 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQG 354
Cdd:TIGR04284 246 KKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADPGTVCG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 355 PQIDQKQFDKILDLIESGKKEGAKLECGGS--AMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRA 432
Cdd:TIGR04284 326 PVISARQRDRVQSYLDLAVAEGGRFACGGGrpADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRIA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1304905828 433 NSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:TIGR04284 406 NDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETKLI 476
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
52-503 |
1.52e-104 |
|
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: 320.35 E-value: 1.52e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFF 131
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAA-QKG--WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 132 iDLEGCVKTLRYFAGWADK-IQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTP 210
Cdd:cd07102 78 -EIRGMLERARYMISIAEEaLADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 211 LTALYLGSLIKEVGFPPGVVNIVPGFGPTvGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVC 290
Cdd:cd07102 157 LCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYVR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIE 370
Cdd:cd07102 235 PDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 371 SGKKEGAKLECGG---SAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKN 447
Cdd:cd07102 315 DAIAKGARALIDGalfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1304905828 448 LDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07102 395 IARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
52-504 |
3.63e-104 |
|
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: 319.63 E-value: 3.63e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 52 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFF 131
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQRE---WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 132 ID-LEGCVK---TLRYFAGWAdkiqgRTIPTDDNVVCFTR-----HEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVV 202
Cdd:cd07098 78 GEiLVTCEKirwTLKHGEKAL-----RPESRPGGLLMFYKrarveYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 203 VKPAEQTPLTALYLGSLIKEV----GFPPGVVNIVPGFGPTvGAAMSSHPQISKLAFTGSTEVGKLVKEAASRSnLKRVT 278
Cdd:cd07098 153 VKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 279 LELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQID 358
Cdd:cd07098 231 LELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 359 QKQFDKILDLIESGKKEGAKLECGGS----AMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANS 434
Cdd:cd07098 311 PARFDRLEELVADAVEKGARLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANS 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304905828 435 LEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIY--AQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07098 391 TEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYyvQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
37-505 |
7.36e-96 |
|
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: 298.74 E-value: 7.36e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 37 NNEWheSKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLAT 116
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 117 LETMDTGKPFLHAF-----FIDLegCvktlRYFAGWADKIQGRTIPTD--DNVVCFTRHePIGVCGAITPWNFPLLMLVW 189
Cdd:cd07130 79 LVSLEMGKILPEGLgevqeMIDI--C----DFAVGLSRQLYGLTIPSErpGHRMMEQWN-PLGVVGVITAFNFPVAVWGW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 190 KLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEV----GFPPGVVNIVPGfGPTVGAAMSSHPQISKLAFTGSTEVGKLV 265
Cdd:cd07130 152 NAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 266 KEAASRsNLKRVTLELGGKNPCIVCADADLDLAVecahQGVFF----NQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKR 341
Cdd:cd07130 231 GQAVAA-RFGRSLLELGGNNAIIVMEDADLDLAV----RAVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 342 PVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFsEVTDTMRIAKEEIFGPVQPILK 421
Cdd:cd07130 306 RIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 422 FKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCyNAIYAQA----PFGGFKMSGNGRELGEYALAEY 497
Cdd:cd07130 385 FDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNV-NIGTSGAeiggAFGGEKETGGGRESGSDAWKQY 463
|
....*...
gi 1304905828 498 TEVKTVTI 505
Cdd:cd07130 464 MRRSTCTI 471
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
50-505 |
3.27e-93 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 291.26 E-value: 3.27e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 50 ATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPfLHA 129
Cdd:PRK09406 4 ATINPATGETVKTFTALTDDEVDAAIARAHARFRD---YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 130 FFIDLEGCVKTLRYFAGWADKIQGRTiPTDDNVV----CFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKP 205
Cdd:PRK09406 80 AKAEALKCAKGFRYYAEHAEALLADE-PADAAAVgasrAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 206 AEQTPLTALYLGSLIKEVGFPPGVVNIVpgfgpTVGA----AMSSHPQISKLAFTGSTEVGKLVKEAASRSnLKRVTLEL 281
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGFPDGCFQTL-----LVGSgaveAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 282 GGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQ 361
Cdd:PRK09406 233 GGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 362 FDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTA 441
Cdd:PRK09406 313 RDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1304905828 442 AVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:PRK09406 393 NAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
22-504 |
6.61e-92 |
|
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: 289.09 E-value: 6.61e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 22 RPVRSLEVKFTKIFINNEWHESKSGKkfATYNPS-TLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLL 100
Cdd:cd07083 9 RRVKEEFGRAYPLVIGGEWVDTKERM--VSVSPFaPSEVVGTTAKADKAEAEAALEAAWAAFKT---WKDWPQEDRARLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 101 NQLADLVERDRTVLATLETMDTGKPFLHAFfIDLEGCVKTLRYFAGWADKIQGR-----TIPTDDNVvcfTRHEPIGVCG 175
Cdd:cd07083 84 LKAADLLRRRRRELIATLTYEVGKNWVEAI-DDVAEAIDFIRYYARAALRLRYPavevvPYPGEDNE---SFYVGLGAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 176 AITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAF 255
Cdd:cd07083 160 VISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 256 TGSTEVGKLVKEAASR-----SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEF 330
Cdd:cd07083 240 TGSLETGKKIYEAAARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 331 VRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGaKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKE 410
Cdd:cd07083 320 LERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 411 EIFGPVQPILKFKNIE--EVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAIYAQAPFGGFKMSG-N 485
Cdd:cd07083 399 EIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkITGALVGVQPFGGFKLSGtN 478
|
490
....*....|....*....
gi 1304905828 486 GRELGEYALAEYTEVKTVT 504
Cdd:cd07083 479 AKTGGPHYLRRFLEMKAVA 497
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
53-505 |
6.54e-86 |
|
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: 272.37 E-value: 6.54e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 53 NPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSPWrrLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFF- 131
Cdd:cd07148 5 NPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 132 ----ID-LEGCVKTLRYFAGwadkiqgRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTV 201
Cdd:cd07148 83 vtraIDgVELAADELGQLGG-------REIPMGltpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 202 VVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGfGPTVGAAMSSHPQISKLAFTGSTEVGKLVkeaasRSNLK---RVT 278
Cdd:cd07148 156 IVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPC-ENAVAEKLVTDPRVAFFSFIGSARVGWML-----RSKLApgtRCA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 279 LELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQID 358
Cdd:cd07148 230 LEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 359 QKQFDKILDLIESGKKEGAKLECGGSAMEDRGLfiKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYG 438
Cdd:cd07148 310 PREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304905828 439 LTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQ-APFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07148 388 FQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
35-505 |
4.40e-83 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 266.75 E-value: 4.40e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESKSGKkfATYNPSTLEK-ICEVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALGRGRLLNQLADLVERDRTV 113
Cdd:cd07125 36 IINGEETETGEGA--PVIDPADHERtIGEVSLADAEDVDAALAIAAAAF---AGWSATPVEERAEILEKAADLLEANRGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 114 LATLETMDTGKPFLHAF-----FIDLegcvktLRYFAGWADKIQGRTI---PTD--DNVVCftrhEPIGVCGAITPWNFP 183
Cdd:cd07125 111 LIALAAAEAGKTLADADaevreAIDF------CRYYAAQARELFSDPElpgPTGelNGLEL----HGRGVFVCISPWNFP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 184 LLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGK 263
Cdd:cd07125 181 LAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 264 LVKEAASRSNLKRVTL--ELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKR 341
Cdd:cd07125 261 LINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 342 PVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEgAKLECGGSAMEDRGLFIKPTVFSEV-TDTMRiakEEIFGPVQPIL 420
Cdd:cd07125 341 KVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVgIFDLT---TEVFGPILHVI 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 421 KFK--NIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINcYN---AIYAQAPFGGFKMSGNGRELG--EYa 493
Cdd:cd07125 417 RFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN-RNitgAIVGRQPFGGWGLSGTGPKAGgpNY- 494
|
490
....*....|..
gi 1304905828 494 LAEYTEVKTVTI 505
Cdd:cd07125 495 LLRFGNEKTVSL 506
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
70-498 |
8.36e-80 |
|
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: 255.66 E-value: 8.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 70 DVDKAVEAAQAAFqrgSPWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAffidlEGCVKTLryfagwAD 149
Cdd:cd07095 1 QVDAAVAAARAAF---PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA-----QTEVAAM------AG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 150 KI-------QGRTIPTD---DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSL 219
Cdd:cd07095 67 KIdisikayHERTGERAtpmAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 220 IKEVGFPPGVVNIVPGfGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAV 299
Cdd:cd07095 147 WEEAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 300 ECAHQGVFFNQGQCCTAASRVFVEE-QVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAK 378
Cdd:cd07095 226 YLIVQSAFLTAGQRCTCARRLIVPDgAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 379 LECGGSAMEDRGLFIKPTVFsEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASAL 458
Cdd:cd07095 306 PLLAMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARI 384
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1304905828 459 ESGTV-WINCYNAIYAQAPFGGFKMSGNGRELGEYAlAEYT 498
Cdd:cd07095 385 RAGIVnWNRPTTGASSTAPFGGVGLSGNHRPSAYYA-ADYC 424
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
53-503 |
1.79e-78 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 253.25 E-value: 1.79e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 53 NPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVeRDRT-VLATLETMDTGKPFLHAff 131
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRD---WRETNIDYRAQKLRDIGKAL-RARSeEMAQMITREMGKPINQA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 132 idlEGCVKTLRYFAGWADKiQG----RTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPA 206
Cdd:PRK13968 87 ---RAEVAKSANLCDWYAE-HGpamlKAEPTlVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 207 EQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVgAAMSSHPQISKLAFTGSTEVGKLVKEAASRSnLKRVTLELGGKNP 286
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKIL 366
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 367 DLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTK 446
Cdd:PRK13968 321 HQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1304905828 447 NLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:PRK13968 401 DETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
164-503 |
8.71e-78 |
|
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: 250.61 E-value: 8.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 164 CFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGfGPTVGAA 243
Cdd:cd07134 94 SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-DAEVAQA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 244 MSSHPqISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVE 323
Cdd:cd07134 172 LLELP-FDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 324 EQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQI-DQKQFDKILDLIESGKKEGAKLECGGsAMEDRGLFIKPTVFSEVT 402
Cdd:cd07134 250 ESVKDAFVEHLKAEIEKFYGKDAARKASPDLARIvNDRHFDRLKGLLDDAVAKGAKVEFGG-QFDAAQRYIAPTVLTNVT 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 403 DTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVwinCYNAIYAQA-----PF 477
Cdd:cd07134 329 PDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGV---VVNDVVLHFlnpnlPF 405
|
330 340
....*....|....*....|....*.
gi 1304905828 478 GGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07134 406 GGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
33-511 |
3.92e-77 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 250.83 E-value: 3.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 33 KIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALGRGRLLNQLADLVERDRT 112
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA-QKA--WAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 113 VLATLETMDTGKPFLHAF--------FIDL---EGCvktlRYFAgwadkiQGRTIPTDD------NVVCFTRHEPIGVCG 175
Cdd:PLN00412 94 PIAECLVKEIAKPAKDAVtevvrsgdLISYtaeEGV----RILG------EGKFLVSDSfpgnerNKYCLTSKIPLGVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 176 AITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAF 255
Cdd:PLN00412 164 AIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 256 TGStEVGKLVKEAASRSNLKrvtLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSV 335
Cdd:PLN00412 244 TGG-DTGIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 336 EYAKKRPVGDPFDvRTEQGPQIDQKQFDKILDLIESGKKEGAKLeCGGSAMEdrGLFIKPTVFSEVTDTMRIAKEEIFGP 415
Cdd:PLN00412 320 AKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATF-CQEWKRE--GNLIWPLLLDNVRPDMRIAWEEPFGP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 416 VQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYA-QAPFGGFKMSGNGRELGEYAL 494
Cdd:PLN00412 396 VLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQGITNSI 475
|
490
....*....|....*..
gi 1304905828 495 AEYTEVKTVTIKLDDKS 511
Cdd:PLN00412 476 NMMTKVKSTVINLPKPS 492
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
74-505 |
2.11e-76 |
|
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: 246.67 E-value: 2.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 74 AVEAAQAAFQRGS----PWRR--LDALGRGrllnqladLVERDRTVLATLETmDTGKPFLHAFFIDLEGCVK----TLRY 143
Cdd:cd07087 3 LVARLRETFLTGKtrslEWRKaqLKALKRM--------LTENEEEIAAALYA-DLGKPPAEAYLTEIAVVLGeidhALKH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 144 FAGWADKiqgRTIPTDDNVV---CFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLI 220
Cdd:cd07087 74 LKKWMKP---RRVSVPLLLQpakAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 221 KEVgFPPGVVNIVPGfGPTVGAAMSSHPqISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVE 300
Cdd:cd07087 151 PKY-FDPEAVAVVEG-GVEVATALLAEP-FDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 301 CAHQGVFFNQGQCCTAASRVFVEEQVYAEFVrrsvEYAKKRpvgdpfdVRTEQGPQ----------IDQKQFDKILDLIE 370
Cdd:cd07087 227 RIAWGKFLNAGQTCIAPDYVLVHESIKDELI----EELKKA-------IKEFYGEDpkespdygriINERHFDRLASLLD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 371 SGKkegakLECGGSAMEDRgLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDK 450
Cdd:cd07087 296 DGK-----VVIGGQVDKEE-RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAV 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 451 ALKLASALESGTVwinCYNAIYAQA-----PFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07087 370 QERVLAETSSGGV---CVNDVLLHAaipnlPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
169-492 |
4.53e-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: 235.86 E-value: 4.53e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 169 EPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGfGPTVGAAMSSHP 248
Cdd:cd07136 99 EPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQELLDQK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 249 qISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYA 328
Cdd:cd07136 177 -FDYIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 329 EFVRRSVEYAKKRPVGDPfdVRTEQGPQI-DQKQFDKILDLIESGKkegakLECGGSAmEDRGLFIKPTVFSEVTDTMRI 407
Cdd:cd07136 255 KFIKELKEEIKKFYGEDP--LESPDYGRIiNEKHFDRLAGLLDNGK-----IVFGGNT-DRETLYIEPTILDNVTWDDPV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 408 AKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINcyNAIYAQA----PFGGFKMS 483
Cdd:cd07136 327 MQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN--DTIMHLAnpylPFGGVGNS 404
|
....*....
gi 1304905828 484 GNGRELGEY 492
Cdd:cd07136 405 GMGSYHGKY 413
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
33-504 |
2.02e-70 |
|
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: 232.46 E-value: 2.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 33 KIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALGRGRLLNQLADLVERDRT 112
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 113 VLATLETMDTGKPFlhaffIDLEGCV----KTLRYFAGWADKIQGRTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLML 187
Cdd:TIGR01722 79 EIAELITAEHGKTH-----SDALGDVarglEVVEHACGVNSLLKGETSTQvATRVDVYSIRQPLGVCAGITPFNFPAMIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 188 VWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGaAMSSHPQISKLAFTGSTEVGKLVKE 267
Cdd:TIGR01722 154 LWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPIGRYIHT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 268 AASRSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVyAEFVRRSVEYAKKRPVGDPF 347
Cdd:TIGR01722 233 TGSAHG-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 348 DVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAME----DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFK 423
Cdd:TIGR01722 311 DPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKvdgyEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEAD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 424 NIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCynAIYAQAP---FGGFKMS--GNGRELGEYALAEYT 498
Cdd:TIGR01722 391 TLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNV--PIPVPLPyfsFTGWKDSffGDHHIYGKQGTHFYT 468
|
....*.
gi 1304905828 499 EVKTVT 504
Cdd:TIGR01722 469 RGKTVT 474
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
167-503 |
8.13e-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: 226.98 E-value: 8.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 167 RHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGfGPTVGAAMSS 246
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTG-GADVAAAFSS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 247 HPqISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQV 326
Cdd:cd07133 176 LP-FDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 327 YAEFVRRSVEYAKKR-PvgdpfdvRTEQGPQ----IDQKQFDKILDLIESGKKEGAKL-ECGGSAMEDRGL-FIKPTVFS 399
Cdd:cd07133 254 LEEFVAAAKAAVAKMyP-------TLADNPDytsiINERHYARLQGLLEDARAKGARViELNPAGEDFAATrKLPPTLVL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 400 EVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINcyNAIY--AQ--A 475
Cdd:cd07133 327 NVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN--DTLLhvAQddL 404
|
330 340
....*....|....*....|....*...
gi 1304905828 476 PFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07133 405 PFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
62-505 |
1.09e-67 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 235.48 E-value: 1.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 62 EVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAffID-LEGCVKT 140
Cdd:PRK11904 578 EVAFADAEQVEQALAAARAAFPA---WSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDA--IAeVREAVDF 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 141 LRYFAGWADKIQGRTI----PT-DDNVVcftRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALY 215
Cdd:PRK11904 653 CRYYAAQARRLFGAPEklpgPTgESNEL---RLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAE 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 216 LGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEA-ASRSNlKRVTL--ELGGKNPCIVCAD 292
Cdd:PRK11904 730 AVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTlAARDG-PIVPLiaETGGQNAMIVDST 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 293 ADLDLAVECAHQGVFFNQGQCCTAAsRV-FVEEQVY-----------AEFVrrsveyakkrpVGDPFDVRTEQGPQIDQK 360
Cdd:PRK11904 809 ALPEQVVDDVVTSAFRSAGQRCSAL-RVlFVQEDIAdrviemlkgamAELK-----------VGDPRLLSTDVGPVIDAE 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 361 QFDKILDLIESGKKEG---AKLECGGSAmeDRGLFIKPTVFsEVtDTMRIAKEEIFGPVQPILKFK--NIEEVIKRANSL 435
Cdd:PRK11904 877 AKANLDAHIERMKREArllAQLPLPAGT--ENGHFVAPTAF-EI-DSISQLEREVFGPILHVIRYKasDLDKVIDAINAT 952
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304905828 436 EYGLTAAVFTKNLDKALKLASALESGTVWINcYNAIYA----QaPFGGFKMSGNG-RELGEYALAEYTEVKTVTI 505
Cdd:PRK11904 953 GYGLTLGIHSRIEETADRIADRVRVGNVYVN-RNQIGAvvgvQ-PFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1025
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
42-486 |
2.45e-67 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 235.22 E-value: 2.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 42 ESKSGKKFATYNPSTLEKIC-EVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETM 120
Cdd:COG4230 565 EAASGEARPVRNPADHSDVVgTVVEATAADVEAALAAAQAAFPA---WSATPVEERAAILERAADLLEAHRAELMALLVR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 121 DTGKPFLHA---------FfidlegcvktLRYFAGwadkiQGRTIPTDDnvvcfTRHEPIGVCGAITPWNFPLLMLVWKL 191
Cdd:COG4230 642 EAGKTLPDAiaevreavdF----------CRYYAA-----QARRLFAAP-----TVLRGRGVFVCISPWNFPLAIFTGQV 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 192 APALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVkeaaSR 271
Cdd:COG4230 702 AAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLI----NR 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 272 SNLKR----VTL--ELGGKNPCIV---------CADadldlAVECAhqgvFFNQGQCCTAAsRV-FVEEQVY-------- 327
Cdd:COG4230 778 TLAARdgpiVPLiaETGGQNAMIVdssalpeqvVDD-----VLASA----FDSAGQRCSAL-RVlCVQEDIAdrvlemlk 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 328 ---AEFVrrsveyakkrpVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKL-ECGGSAMEDRGLFIKPTVFsEVtD 403
Cdd:COG4230 848 gamAELR-----------VGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLI-EI-D 914
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 404 TMRIAKEEIFGPVQPILKFK--NIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINcYNAIYA----QaPF 477
Cdd:COG4230 915 SISDLEREVFGPVLHVVRYKadELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN-RNIIGAvvgvQ-PF 992
|
....*....
gi 1304905828 478 GGFKMSGNG 486
Cdd:COG4230 993 GGEGLSGTG 1001
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
70-503 |
2.52e-67 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 223.25 E-value: 2.52e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 70 DVDKAVEAAQAAFQRGS----PWRRLDalgrgrlLNQLADLVERDRTVLATLETMDTGKPFLHAFFIDLEGC-------V 138
Cdd:cd07135 6 EIDSIHSRLRATFRSGKtkdlEYRLWQ-------LKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVkndilhmL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 139 KTLRYFAgwADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGS 218
Cdd:cd07135 79 KNLKKWA--KDEKVKDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 219 LIKEvGFPPGVVNIVPGFGPTVGAAMSSHpqISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLA 298
Cdd:cd07135 157 LVPK-YLDPDAFQVVQGGVPETTALLEQK--FDKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 299 VECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDvRTEQGPQIDQKQFDKILDLIESGKkegAK 378
Cdd:cd07135 233 AKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANA-SPDYTRIVNPRHFNRLKSLLDTTK---GK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 379 LECGGSaMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKnlDKALK---LA 455
Cdd:cd07135 309 VVIGGE-MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTD--DKSEIdhiLT 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1304905828 456 SALESGTVWINCY-NAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07135 386 RTRSGGVVINDTLiHVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
60-490 |
3.75e-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: 224.79 E-value: 3.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 60 ICEVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFlHAFFIDLEGCVK 139
Cdd:TIGR01238 65 VGQVFHANLAHVQAAIDSAQQAF---PTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTI-HNAIAEVREAVD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 140 TLRYFAGWADKiqgrTIPTDDnvvcftrHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSL 219
Cdd:TIGR01238 141 FCRYYAKQVRD----VLGEFS-------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVEL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 220 IKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRSNLKRVTL--ELGGKNPCIVCADADLDL 297
Cdd:TIGR01238 210 MQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVDSTALPEQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 298 AVECAHQGVFFNQGQCCTAASRVFVEEQVyAEFVRRSVEYAKKR-PVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEG 376
Cdd:TIGR01238 290 VVRDVLRSAFDSAGQRCSALRVLCVQEDV-ADRVLTMIQGAMQElKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQ 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 377 ---AKLECGGSAMEDRGLFIKPTVFSevTDTMRIAKEEIFGPVQPILKFK--NIEEVIKRANSLEYGLTAAVFTKNLDKA 451
Cdd:TIGR01238 369 kkiAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVHSRIETTY 446
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1304905828 452 LKLASALESGTVWIN--CYNAIYAQAPFGGFKMSGNGRELG 490
Cdd:TIGR01238 447 RWIEKHARVGNCYVNrnQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
35-486 |
4.22e-67 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 234.76 E-value: 4.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWH-------ESKSGKKFATYNPS-TLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADL 106
Cdd:PRK11905 548 FAAKTWHaapllagGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPE---WSATPAAERAAILERAADL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 107 VERDRTVLATLETMDTGKPFLHAffID-LEGCVKTLRYFAGwadkiQGRTIPTDDnvvcftRHEPIGVCGAITPWNFPLL 185
Cdd:PRK11905 625 MEAHMPELFALAVREAGKTLANA--IAeVREAVDFLRYYAA-----QARRLLNGP------GHKPLGPVVCISPWNFPLA 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 186 MLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLV 265
Cdd:PRK11905 692 IFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLI 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 266 -KEAASRSNlKRVTL--ELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAAsRV-FVEEQVyAEFVRRSVEYA-KK 340
Cdd:PRK11905 772 qRTLAKRSG-PPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSAL-RVlCLQEDV-ADRVLTMLKGAmDE 848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 341 RPVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKL-ECGGSAMEDRGLFIKPTVFsEVTDtMRIAKEEIFGPVQPI 419
Cdd:PRK11905 849 LRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLI-EIDS-ISDLEREVFGPVLHV 926
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1304905828 420 LKFK--NIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINcYNAIYA----QaPFGGFKMSGNG 486
Cdd:PRK11905 927 VRFKadELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN-RNIIGAvvgvQ-PFGGEGLSGTG 997
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
35-497 |
4.86e-67 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 224.07 E-value: 4.86e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESkSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALGRGRLLNQLADLVERDRTVL 114
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 115 ATLETMDTGKPFLHAffidlegcvKTlrYFAGWADKI-------QGRT----IPTDDNVVCFtRHEPIGVCGAITPWNFP 183
Cdd:PRK09457 80 AEVIARETGKPLWEA---------AT--EVTAMINKIaisiqayHERTgekrSEMADGAAVL-RHRPHGVVAVFGPYNFP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 184 LLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGfGPTVGAAMSSHPQISKLAFTGSTEVGK 263
Cdd:PRK09457 148 GHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 264 LV-KEAASRSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAE-FVRRSVEYAKKR 341
Cdd:PRK09457 227 LLhRQFAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 342 PVGDPFDvrTEQ---GPQIDQKQFDKILD----LIESGKK---EGAKLECGGSamedrglFIKPTVFsEVTDTMRIAKEE 411
Cdd:PRK09457 306 TVGRWDA--EPQpfmGAVISEQAAQGLVAaqaqLLALGGKsllEMTQLQAGTG-------LLTPGII-DVTGVAELPDEE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 412 IFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTV-WINCYNAIYAQAPFGGFKMSGNGRELG 490
Cdd:PRK09457 376 YFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHRPSA 455
|
....*..
gi 1304905828 491 EYAlAEY 497
Cdd:PRK09457 456 YYA-ADY 461
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
35-512 |
1.84e-64 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 217.78 E-value: 1.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWheSKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfqrGSPWRRLDALGRGRLLNQLADLVERDRTVL 114
Cdd:PLN02315 24 YVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEA---AKIWMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 115 ATLETMDTGKpFLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAP 193
Cdd:PLN02315 99 GRLVSLEMGK-ILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 194 ALCCGNTVVVKPAEQTPLTALYLGSLIKEV----GFPPGVVNIVPGfGPTVGAAMSSHPQISKLAFTGSTEVGKLVKEAA 269
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 270 SrSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDV 349
Cdd:PLN02315 257 N-ARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 350 RTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFsEVTDTMRIAKEEIFGPVQPILKFKNIEEVI 429
Cdd:PLN02315 336 GTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 430 KRANSLEYGLTAAVFTKNLDKALKLASALES--GTVWINC-YNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:PLN02315 415 EINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTIN 494
|
....*.
gi 1304905828 507 LDDKSP 512
Cdd:PLN02315 495 YGNELP 500
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
11-484 |
3.66e-64 |
|
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: 217.07 E-value: 3.66e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 11 GQPDRKppALPRPVRSLEVKFTKI--FINNEwhESKSGKKFATYNPST-LEKICEVEEGDKPDVDKAVEAAQAAfqRGSp 87
Cdd:cd07123 12 GSPERA--KLQEALAELKSLTVEIplVIGGK--EVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEA--RKE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 88 WRRLDALGRGRLLNQLADLVE---RDRTVLATLetMDTGKPFLHAFfIDlEGC--VKTLRYFAGWADKI-QGRTIPTDDN 161
Cdd:cd07123 85 WARMPFEDRAAIFLKAADLLSgkyRYELNAATM--LGQGKNVWQAE-ID-AACelIDFLRFNVKYAEELyAQQPLSSPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 162 VVCFTRHEPI-GVCGAITPWNFPLLMLVWKLAPALCcGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTV 240
Cdd:cd07123 161 VWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 241 GAAMSSHPQISKLAFTGSTEVGK-LVKEAASR----SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCT 315
Cdd:cd07123 240 GDTVLASPHLAGLHFTGSTPTFKsLWKQIGENldryRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 316 AASRVFVEEQVYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKE-GAKLECGGSAMEDRGLFIK 394
Cdd:cd07123 320 AASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 395 PTVFsEVTDTM-RIAKEEIFGPVQPILKF--KNIEEVIKRANSL-EYGLTAAVFTKNlDKALKLAS-ALE--SGTVWIN- 466
Cdd:cd07123 400 PTVI-ETTDPKhKLMTEEIFGPVLTVYVYpdSDFEETLELVDTTsPYALTGAIFAQD-RKAIREATdALRnaAGNFYINd 477
|
490
....*....|....*....
gi 1304905828 467 -CYNAIYAQAPFGGFKMSG 484
Cdd:cd07123 478 kPTGAVVGQQPFGGARASG 496
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
164-506 |
4.07e-60 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 205.65 E-value: 4.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 164 CFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGfGPTVGAA 243
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 244 MSSHPqISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVE 323
Cdd:PTZ00381 181 LLKEP-FDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 324 EQVYAEFVrRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIESgkkEGAKLECGGSA-MEDRglFIKPTVFSEVT 402
Cdd:PTZ00381 259 RSIKDKFI-EALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGEVdIENK--YVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 403 DTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAIYAQAPFGGF 480
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGGV 412
|
330 340
....*....|....*....|....*.
gi 1304905828 481 KMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
9-509 |
3.06e-59 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 206.14 E-value: 3.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 9 ENGQPdRKPPALPRpvrslevkftkiFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspW 88
Cdd:PLN02419 104 QSTQP-QMPPRVPN------------LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL---W 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 89 RRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPfLHAFFIDLEGCVKTLRYFAGWADKIQGRTIPTDDNVV-CFTR 167
Cdd:PLN02419 168 RNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKT-LKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVdTYSI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 168 HEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGaAMSSH 247
Cdd:PLN02419 247 REPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 248 PQISKLAFTGSTEVG-KLVKEAASRSnlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASR-VFVEEQ 325
Cdd:PLN02419 326 EDIRAVSFVGSNTAGmHIYARAAAKG--KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 326 VYAEfvRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAM----EDRGLFIKPTVFSEV 401
Cdd:PLN02419 404 KSWE--DKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 402 TDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCynAIYAQAPFggFK 481
Cdd:PLN02419 482 TPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPF--FS 557
|
490 500 510
....*....|....*....|....*....|....*
gi 1304905828 482 MSGNGREL-------GEYALAEYTEVKTVTIKLDD 509
Cdd:PLN02419 558 FTGNKASFagdlnfyGKAGVDFFTQIKLVTQKQKD 592
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
73-506 |
1.01e-55 |
|
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: 192.82 E-value: 1.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 73 KAVEAAQAAFQRGspwRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFFIDLEGCVKTLRY----FAGWA 148
Cdd:cd07132 2 EAVRRAREAFSSG---KTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYaisnLPEWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 149 -DKIQGRTIPT--DDnvvCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLI----- 220
Cdd:cd07132 79 kPEPVKKNLATllDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyld 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 221 KEVgFPpgVVNivpgfgptvGAAmsshPQISKLA--------FTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCAD 292
Cdd:cd07132 156 KEC-YP--VVL---------GGV----EETTELLkqrfdyifYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 293 ADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVrrsvEYAK---KRPVGDpfDVRTEQ--GPQIDQKQFDKILD 367
Cdd:cd07132 219 CDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFV----EALKktlKEFYGE--DPKESPdyGRIINDRHFQRLKK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 368 LIESGKkegakLECGGSaMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKN 447
Cdd:cd07132 293 LLSGGK-----VAIGGQ-TDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1304905828 448 LDKALKLASALESGTVwinCYN-----AIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:cd07132 367 KKVINKILSNTSSGGV---CVNdtimhYTLDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
69-503 |
3.82e-50 |
|
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: 177.60 E-value: 3.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 69 PDVDKAVEAAQAAFQRGSPWRRLDalgrgrlLNQLADLV-ERDRTVLATLETmDTGKPFLHAFFIDL----EGCVKTLRY 143
Cdd:cd07137 3 RLVRELRETFRSGRTRSAEWRKSQ-------LKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRDEVsvlvSSCKLAIKE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 144 FAGWAD----KIQGRTIPTDDNVVCftrhEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSL 219
Cdd:cd07137 75 LKKWMApekvKTPLTTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 220 IKEVgFPPGVVNIVPGfGPTVGAAMSSHpQISKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAV 299
Cdd:cd07137 151 IPEY-LDTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 300 ECAHQGVF-FNQGQCCTAASRVFVEEQVYAEFVRRSVEYAKKRPVGDPfdVRTEQGPQIDQKQFDKILDLIESGKKEGAK 378
Cdd:cd07137 227 RRIAGGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENP--KESKDLSRIVNSHHFQRLSRLLDDPSVADK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 379 LECGGSAMEDRgLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASAL 458
Cdd:cd07137 305 IVHGGERDEKN-LYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAET 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1304905828 459 ESGTVWINCYNAIYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07137 384 SSGGVTFNDTVVQYAidTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
53-486 |
2.44e-49 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 182.87 E-value: 2.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 53 NPSTLEKIC-EVEEGDKPDVDKAVEAAQAAfqrGSPWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFf 131
Cdd:PRK11809 665 NPADPRDIVgYVREATPAEVEQALESAVNA---APIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAI- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 132 IDLEGCVKTLRYFAGwadkiQGRTIPTDDNvvcftrHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPL 211
Cdd:PRK11809 741 AEVREAVDFLRYYAG-----QVRDDFDNDT------HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPL 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 212 TALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGKLV-KEAASR-SNLKRVT---LELGGKNP 286
Cdd:PRK11809 810 IAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLqRNLAGRlDPQGRPIpliAETGGQNA 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVyAEFVRRSV-----EYAkkrpVGDPFDVRTEQGPQIDQKQ 361
Cdd:PRK11809 890 MIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDV-ADRTLKMLrgamaECR----MGNPDRLSTDIGPVIDAEA 964
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 362 FDKILDLIESGKKEGAK---LECGGSAMEDRGLFIKPTVFsEVTDTMRIaKEEIFGPVQPILKFK--NIEEVIKRANSLE 436
Cdd:PRK11809 965 KANIERHIQAMRAKGRPvfqAARENSEDWQSGTFVPPTLI-ELDSFDEL-KREVFGPVLHVVRYNrnQLDELIEQINASG 1042
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1304905828 437 YGLTAAVFTKNLDKALKLASALESGTVWINcYNAIYA----QaPFGGFKMSGNG 486
Cdd:PRK11809 1043 YGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAvvgvQ-PFGGEGLSGTG 1094
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
169-504 |
1.62e-38 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 146.80 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 169 EPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGfGPTVGAAMSSHP 248
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEG-GPAVGEQLLQHK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 249 QiSKLAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIV-CADA--DLDLAVE---------CAhqgvffnqGQCCTA 316
Cdd:PLN02203 185 W-DKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdSLSSsrDTKVAVNrivggkwgsCA--------GQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 317 ASRVFVEEQvYAEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIESgKKEGAKLECGGSAMEDRgLFIKPT 396
Cdd:PLN02203 255 IDYVLVEER-FAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKD-PRVAASIVHGGSIDEKK-LFIEPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 397 VFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYA--Q 474
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAcdS 411
|
330 340 350
....*....|....*....|....*....|
gi 1304905828 475 APFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:PLN02203 412 LPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
77-466 |
3.15e-38 |
|
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: 145.07 E-value: 3.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 77 AAQAAFQRGSPWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFFIDleGCVKTLRYFA--GWADKIQGR 154
Cdd:cd07084 4 ALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENIC--GDQVQLRARAfvIYSYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 155 TIPTDDNVVCFTRHE---PIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVG-FPPGVV 230
Cdd:cd07084 82 PGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 231 NIVPGFGPTvGAAMSSHPQISKLAFTGSTEVGklvkeAASRSNLK--RVTLELGGKNPCIVCADADL--DLAVECAhQGV 306
Cdd:cd07084 162 TLINGDGKT-MQALLLHPNPKMVLFTGSSRVA-----EKLALDAKqaRIYLELAGFNWKVLGPDAQAvdYVAWQCV-QDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 307 FFNQGQCCTAASRVFVEEQVYAE-FVRRSVEYAKKRPVGDpfdvrTEQGPQIdqkQFDKILDLIESGKKEGAKLECGGSA 385
Cdd:cd07084 235 TACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLED-----LLLGPVQ---TFTTLAMIAHMENLLGSVLLFSGKE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 386 M------EDRGLFIKPTVF---SEVTDTMRIAKEEIFGPVQPILKFKNIEE--VIKRANSLEYGLTAAVFTKNLDKALKL 454
Cdd:cd07084 307 LknhsipSIYGACVASALFvpiDEILKTYELVTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPIFLQEL 386
|
410
....*....|...
gi 1304905828 455 ASALES-GTVWIN 466
Cdd:cd07084 387 IGNLWVaGRTYAI 399
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
121-503 |
3.67e-33 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 131.71 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 121 DTGKPFLHAFFID---LEGCVK-TLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALC 196
Cdd:PLN02174 59 DLGKPELESSVYEvslLRNSIKlALKQLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAIS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 197 CGNTVVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAMSShpQISKLAFTGSTEVGKLVKEAASRsNLKR 276
Cdd:PLN02174 139 AGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLEQ--KWDKIFYTGSSKIGRVIMAAAAK-HLTP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 277 VTLELGGKNPCIVCADADLDLAVECAHQGVF-FNQGQCCTAASRVFVEEQvYAEFVRRSVEYAKKRPVG-DPFDVRtEQG 354
Cdd:PLN02174 215 VVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKE-YAPKVIDAMKKELETFYGkNPMESK-DMS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 355 PQIDQKQFDKILDLIESgKKEGAKLECGGSamEDR-GLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRAN 433
Cdd:PLN02174 293 RIVNSTHFDRLSKLLDE-KEVSDKIVYGGE--KDReNLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIR 369
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304905828 434 SLEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:PLN02174 370 SRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiAVHLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
35-459 |
7.35e-30 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 122.51 E-value: 7.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESkSGKKFATYNPSTLEKICEVeegDKPDVDKAVEAAQAAFQRGSPWRRLDALGRGRLLNQLADLVERDRTVL 114
Cdd:PRK11903 8 YVAGRWQAG-SGAGTPLFDPVTGEELVRV---SATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 115 ATLETMDTGKPFLHAFFiDLEGCVKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPI----------GVCGAITPWNFPL 184
Cdd:PRK11903 84 YDIATANSGTTRNDSAV-DIDGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKDPAFqgqhvlvptrGVALFINAFNFPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 185 LMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVG-FPPGVVNIVPGfgptVGAAMSSHPQ-ISKLAFTGSTEVG 262
Cdd:PRK11903 163 WGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG----SSAGLLDHLQpFDVVSFTGSAETA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 263 KLVKE--AASRSNLkRVTLELGGKNPCIVCADAD-----LDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSV 335
Cdd:PRK11903 239 AVLRShpAVVQRSV-RVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 336 EYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIEsGKKEGAKLECGGSAME------DRGLFIKPTVF--SEVTDTMRI 407
Cdd:PRK11903 318 ARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLgaSDPDAATAV 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1304905828 408 AKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKnlDKALKLASALE 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 |
4.85e-25 |
|
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: 108.13 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 35 FINNEWHESkSGKKFATYNPSTLEKICEVEeGDKPDVDKAVEAAQaafQRGSP-WRRLDALGRGRLLNQLADLVERDRTV 113
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYAR---EKGGPaLRALTFHERAAMLKALAKYLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 114 LATLETmDTGKPFLHAFfIDLEGCVKTLRYFAGwadkiQGRTIPTDDNV-------------------VCFTRHepiGVC 174
Cdd:cd07128 79 LYALSA-ATGATRRDSW-IDIDGGIGTLFAYAS-----LGRRELPNAHFlvegdveplskdgtfvgqhILTPRR---GVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 175 GAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVG-FPPGVVNIVPGfgpTVGAAMSSHPQISKL 253
Cdd:cd07128 149 VHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG---SVGDLLDHLGEQDVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 254 AFTGSTEVG-KLVKEAASRSNLKRVTLELGGKNPCIVCADA-----DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVY 327
Cdd:cd07128 226 AFTGSAATAaKLRAHPNIVARSIRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 328 AEFVRRSVEYAKKRPVGDPFDVRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAME------DRGLFIKPTVF--- 398
Cdd:cd07128 306 DAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEvvgadaEKGAFFPPTLLlcd 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304905828 399 -----SEVTDTmriakeEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASAL 458
Cdd:cd07128 386 dpdaaTAVHDV------EAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGA 444
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
71-459 |
2.37e-23 |
|
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: 102.62 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 71 VDKAVEAAQAAFQrgsPWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHaffidLEG----CVKTLRYFA- 145
Cdd:cd07129 1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEAR-----LQGelgrTTGQLRLFAd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 146 -----GWADKI------QGRTIPTDDNVVCFTRHEPIGVCGAItpwNFPLLMLVW--KLAPALCCGNTVVVKPAEQTPLT 212
Cdd:cd07129 73 lvregSWLDARidpadpDRQPLPRPDLRRMLVPLGPVAVFGAS---NFPLAFSVAggDTASALAAGCPVVVKAHPAHPGT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 213 ALYLGSLIKEV----GFPPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGSTEVGK-LVKEAASRSNLKRVTLELGGKNPC 287
Cdd:cd07129 150 SELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRaLFDAAAARPEPIPFYAELGSVNPV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 288 IVCADADLDLAVECAhQG----VFFNQGQCCTAASRVFV-EEQVYAEFVRRSVEYAKKRPVGdpfdvrTEQGPQIdQKQF 362
Cdd:cd07129 230 FILPGALAERGEAIA-QGfvgsLTLGAGQFCTNPGLVLVpAGPAGDAFIAALAEALAAAPAQ------TMLTPGI-AEAY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 363 DKILDLIESGKkeGAKLECGGSAMEDRGLFiKPTVFSEVTDTMR---IAKEEIFGPVQPILKFKNIEEVIKRANSLEYGL 439
Cdd:cd07129 302 RQGVEALAAAP--GVRVLAGGAAAEGGNQA-APTLFKVDAAAFLadpALQEEVFGPASLVVRYDDAAELLAVAEALEGQL 378
|
410 420
....*....|....*....|..
gi 1304905828 440 TAAVF--TKNLDKALKLASALE 459
Cdd:cd07129 379 TATIHgeEDDLALARELLPVLE 400
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
96-479 |
9.51e-18 |
|
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: 85.35 E-value: 9.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 96 RGRLLNQLADLVERDRTVLATLETMDTGKPF--LHAFFIDLEGCVK--------TLRYFAGWADKIQGRTIPtdDNVVCF 165
Cdd:cd07077 18 RDLIINAIANALYDTRQRLASEAVSERGAYIrsLIANWIAMMGCSEsklyknidTERGITASVGHIQDVLLP--DNGETY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 166 TRHEPIGVCGAITPWNFPLLMlVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEV---GFPPGVVNIVPGFGPTVGA 242
Cdd:cd07077 96 VRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPSDELAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 243 AMSSHPQISKLAFTGSTEVgklVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCctaasrvFV 322
Cdd:cd07077 175 ELLSHPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQNAC-------AS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 323 EEQVYAefvrrsveyakkrpVGDPFDVRTEQgpqidqkqfdkildLIESGKKEGAKLECGgsamedrglfIKPtVFSEVT 402
Cdd:cd07077 245 EQNLYV--------------VDDVLDPLYEE--------------FKLKLVVEGLKVPQE----------TKP-LSKETT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 403 DTMRIAKEEIFGPVQPILKFKNIEEVIKRANSL--EYG--LTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFG 478
Cdd:cd07077 286 PSFDDEALESMTPLECQFRVLDVISAVENAWMIieSGGgpHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAG 365
|
.
gi 1304905828 479 G 479
Cdd:cd07077 366 K 366
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
69-459 |
9.93e-18 |
|
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: 85.37 E-value: 9.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 69 PDVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFFIDLEGCvktlryfagwA 148
Cdd:cd07121 4 ATVDDAVAAAKAAQKQ---YRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLA----------A 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 149 DKIQG-----RTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSL---- 219
Cdd:cd07121 71 EKTPGtedltTTAWSGDNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELinka 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 220 IKEVGFPPGVVNIVPGfgPTVGAA--MSSHPQISKLAFTGSTEVGKlvkeaASRSNLKRVTLELGGKNPCIVCADADLDL 297
Cdd:cd07121 151 IAEAGGPDNLVVTVEE--PTIETTneLMAHPDINLLVVTGGPAVVK-----AALSSGKKAIGAGAGNPPVVVDETADIEK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 298 AVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRSVEyakkrpvgdpfdvrtEQGPQIDQKQFDKILDLIESGKKEGA 377
Cdd:cd07121 224 AARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQR---------------NGAYVLNDEQAEQLLEVVLLTNKGAT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 378 ---KLEcGGSA---MEDRGLFIKPT---VFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGL--TAAVFTK 446
Cdd:cd07121 289 pnkKWV-GKDAskiLKAAGIEVPADirlIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSK 367
|
410
....*....|...
gi 1304905828 447 NLDKALKLASALE 459
Cdd:cd07121 368 NVENLTKMARAMQ 380
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
70-459 |
3.79e-17 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 83.80 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 70 DVDKAVEAAQAAFQRgspWRRLDALGRGRLLNQLADLVERDRTVLATLETMDTGKpflhaffidleGCVktlryfagwAD 149
Cdd:PRK15398 37 SVDDAVAAAKVAQQR---YQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGM-----------GRV---------ED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 150 KI-----QGRTIP----------TDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTAL 214
Cdd:PRK15398 94 KIaknvaAAEKTPgvedlttealTGDNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 215 YLGSL----IKEVGFPPGVVNIVPGfgPTVGAA--MSSHPQISKLAFTGstevGKLVKEAASRSNlKRVTLELGGKNPCI 288
Cdd:PRK15398 174 RAIELlneaIVAAGGPENLVVTVAE--PTIETAqrLMKHPGIALLVVTG----GPAVVKAAMKSG-KKAIGAGAGNPPVV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 289 VCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYAEFVRRsveyakkrpvgdpfdVRTEQGPQIDQKQFDKILDL 368
Cdd:PRK15398 247 VDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRL---------------MEKNGAVLLTAEQAEKLQKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 369 IESGKKEGAKLECGGSA---MEDRGLFIKPTV---FSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGL--T 440
Cdd:PRK15398 312 VLKNGGTVNKKWVGKDAakiLEAAGINVPKDTrllIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhT 391
|
410
....*....|....*....
gi 1304905828 441 AAVFTKNLDKALKLASALE 459
Cdd:PRK15398 392 AIMHSRNVDNLNKMARAIQ 410
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
170-443 |
3.05e-14 |
|
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: 74.84 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 170 PIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAMS-SHP 248
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 249 QIskLAFTGSTEVGklvkEAASRSNLKRVTLELGGKNPCIVCAD-ADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQ-V 326
Cdd:cd07126 222 RM--TLFTGSSKVA----ERLALELHGKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 327 YAEFVRRSVEYAKKRPVGDpfdvrTEQGP------QIDQKQFDKILDLiesgkkEGAKLECGGS------------AMED 388
Cdd:cd07126 296 QAGILDKLKALAEQRKLED-----LTIGPvltwttERILDHVDKLLAI------PGAKVLFGGKpltnhsipsiygAYEP 364
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1304905828 389 RGLFIkPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEE--VIKRANSLEYGLTAAV 443
Cdd:cd07126 365 TAVFV-PLEEIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAV 420
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
71-482 |
4.13e-10 |
|
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: 61.90 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 71 VDKAVEAAQAAfQRGSPWRRLDAlgRGRLLNQLADLVERDRTVLATLETMDTGKPFLHAFFIDlegCVKTLRYFAG-WAD 149
Cdd:cd07081 1 LDDAVAAAKVA-QQGLSCKSQEM--VDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIK---NHFAAEYIYNvYKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 150 KIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKP----AEQTPLTALYLGSLIKEVGF 225
Cdd:cd07081 75 EKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 226 PPGVVNIVPGFGPTVGAAMSSHPQISKLAFTGstevGKLVKEAAsRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQG 305
Cdd:cd07081 155 PENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAA-YSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 306 VFFNQGQCCTAASRVFVEEQVYAEFVRRsveyakkrpvgdpfdVRTEQGPQIDQKQFDKILDLIES---------GKKEG 376
Cdd:cd07081 230 KTFDNGVICASEQSVIVVDSVYDEVMRL---------------FEGQGAYKLTAEELQQVQPVILKngdvnrdivGQDAY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 377 AKLECGGSAM--EDRGLFIKPTVFSEvtdtMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEY----GLTAAVFTKNL-- 448
Cdd:cd07081 295 KIAAAAGLKVpqETRILIGEVTSLAE----HEPFAHEKLSPVLAMYRAANFADADAKALALKLeggcGHTSAMYSDNIka 370
|
410 420 430
....*....|....*....|....*....|....*
gi 1304905828 449 -DKALKLASALESGTVWINCYNAIYAQAPFGGFKM 482
Cdd:cd07081 371 iENMNQFANAMKTSRFVKNGPCSQGGLGDLYNFRG 405
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
67-322 |
7.30e-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: 51.71 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 67 DKPDVDKAVEAAQAAFQRgspWRRLDALGR-GRLLNQLADLVERDRTvLATLETMDTGKPFLHAFFID----LEGCVKTL 141
Cdd:cd07127 82 PQCDPDALLAAARAAMPG---WRDAGARARaGVCLEILQRLNARSFE-MAHAVMHTTGQAFMMAFQAGgphaQDRGLEAV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 142 RYfagwADKIQGRTIPTDDNVVCFTRHEPI-----------GV-----CGAITPWN-FPLLMlvwklaPALCCGNTVVVK 204
Cdd:cd07127 158 AY----AWREMSRIPPTAEWEKPQGKHDPLamektftvvprGValvigCSTFPTWNgYPGLF------ASLATGNPVIVK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 205 PAeqtPLTALYLGSLIK-------EVGFPPGVVNIV---PGFGptVGAAMSSHPQISKLAFTGSTEVGKLVKEAASRsnl 274
Cdd:cd07127 228 PH---PAAILPLAITVQvarevlaEAGFDPNLVTLAadtPEEP--IAQTLATRPEVRIIDFTGSNAFGDWLEANARQ--- 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1304905828 275 KRVTLELGGKNPCIVcaDADLDLAVECAHQGVFFN--QGQCCTAASRVFV 322
Cdd:cd07127 300 AQVYTEKAGVNTVVV--DSTDDLKAMLRNLAFSLSlySGQMCTTPQNIYV 347
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
169-467 |
1.44e-06 |
|
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: 50.57 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 169 EPIGVCGAITPWNFPLLMLVWKLAPALCCGNTVVVKP----AEQTPLTALYLGSLIKEVGFPPGVVNIVPgfGPTVGA-- 242
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhpraKKCSIEAAKIMREAAVAAGAPEGLIQWIE--EPSIELtq 171
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 243 AMSSHPQISKLAFTGStevGKLVKEAASRSnlkrvTLELG---GKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASR 319
Cdd:cd07122 172 ELMKHPDVDLILATGG---PGMVKAAYSSG-----KPAIGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQS 243
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 320 VFVEEQVYAEFVRRSVeyakkrpvgdpfdvrtEQGPQI----DQKQFDKILdLIESGK-------KEGAKL--ECGGSAM 386
Cdd:cd07122 244 VIVDDEIYDEVRAELK----------------RRGAYFlneeEKEKLEKAL-FDDGGTlnpdivgKSAQKIaeLAGIEVP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304905828 387 EDRGLFIKPtvFSEVTDTMRIAKEEIFgPVQPILKFKNIEEVIKRANS-LEY---GLTAAVFTKNLDKALKLASALESGT 462
Cdd:cd07122 307 EDTKVLVAE--ETGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKARElLEYggaGHTAVIHSNDEEVIEEFALRMPVSR 383
|
....*
gi 1304905828 463 VWINC 467
Cdd:cd07122 384 ILVNT 388
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