|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
1-494 |
0e+00 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 1024.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 1 MNFHHLAYWQDKALSLAIENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGDWSLSSP 80
Cdd:PRK09847 1 MNFHHLAYWQDKALSLAIENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 81 AKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGV 160
Cdd:PRK09847 81 AKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 161 IAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAI 240
Cdd:PRK09847 161 IAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 241 AFTGSTRTGKQLLKDAGDSNMKRVWLEAGGKSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLA 320
Cdd:PRK09847 241 AFTGSTRTGKQLLKDAGDSNMKRVWLEAGGKSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 321 LLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFG 400
Cdd:PRK09847 321 LLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 401 PVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHAL 480
Cdd:PRK09847 401 PVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHAL 480
|
490
....*....|....
gi 16129261 481 EKFTELKTIWISLE 494
Cdd:PRK09847 481 EKFTELKTIWISLE 494
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
34-491 |
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: 835.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 34 NETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPI 113
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 114 RHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPS 193
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 194 EKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSNMKRVWLEAGGKSA 273
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 274 NIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSV 353
Cdd:cd07112 241 NIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 354 HSFIREGESKGQLLLDGRNAGLAAA----IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAV 429
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRVLTETggffVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129261 430 WTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
19-493 |
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: 639.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 19 ENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFerGDWSLSSPAKRKAVLNKLADLMEAHA 98
Cdd:COG1012 5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 99 EELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSS-HELAMIVREPVGVIAAIVPWNFPLLLTCWK 177
Cdd:COG1012 83 EELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDApGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 178 LGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAG 257
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 258 DsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDP 337
Cdd:COG1012 242 E-NLKRVTLELGGKNPAIVLDDA-DLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 338 ATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA--IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQA 414
Cdd:COG1012 320 GTDMGPLISEAQLERVLAYIEDAVAEGaELLTGGRRPDGEGGyfVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 415 LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYN-DGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
Cdd:COG1012 400 IALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTtGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
31-489 |
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: 624.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 31 AAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTG 110
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPA--WRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 111 KPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVIL 190
Cdd:pfam00171 81 KPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 191 KPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGdSNMKRVWLEAGG 270
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA-QNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 271 KSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHA 350
Cdd:pfam00171 239 KNPLIVLEDA-DLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 351 DSVHSFIREGESKGQLLLDGRNAGLA--AAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAA 428
Cdd:pfam00171 318 ERVLKYVEDAKEEGAKLLTGGEAGLDngYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129261 429 VWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM-TVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:pfam00171 398 VFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
22-489 |
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: 596.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEEL 101
Cdd:cd07091 6 LFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERDRDEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 102 ALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
Cdd:cd07091 86 AALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSNM 261
Cdd:cd07091 166 LAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSNL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 262 KRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
Cdd:cd07091 246 KKVTLELGGKSPNIVFDDA-DLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 342 GTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLAN 419
Cdd:cd07091 325 GPQVSKAQFDKILSYIESGKKEGATLLTGgeRHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERAN 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 420 DSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07091 405 DTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
60-491 |
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: 565.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 60 DRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRhSLRDDIPGAARAIRWYAEAIDKVY 139
Cdd:cd07078 1 DAAVAAARAAFK--AWAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 140 GEVATTSS-HELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLN 218
Cdd:cd07078 78 GEVIPSPDpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 219 VVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQ 298
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDA-DLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 299 GQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLA 376
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGgkRLEGGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 377 AA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYN 455
Cdd:cd07078 316 GYfVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 16129261 456 DG-DMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:cd07078 396 VGaEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
39-491 |
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: 560.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 39 TVDPVTQAPLAKIARGKSVDIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLR 118
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP--GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 119 DDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPL 198
Cdd:cd07093 79 RDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 199 SAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFA 278
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 279 DCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIR 358
Cdd:cd07093 238 DA-DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 359 EGESKG-QLLLDGRNAGLAAAIG-----PTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTR 432
Cdd:cd07093 317 LARAEGaTILTGGGRPELPDLEGgyfvePTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129261 433 DLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
39-491 |
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: 543.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 39 TVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlR 118
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRET-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 119 DDIPGAARAIRWYAEAIDKVYGEVATTSSHE-LAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSP 197
Cdd:cd07114 80 AQVRYLAEWYRYYAGLADKIEGAVIPVDKGDyLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 198 LSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVF 277
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 278 ADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFI 357
Cdd:cd07114 239 DDA-DLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 358 REGESKG-QLLLDGRNAGLAAA-----IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWT 431
Cdd:cd07114 318 ARAREEGaRVLTGGERPSGADLgagyfFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 432 RDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:cd07114 398 RDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
39-493 |
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: 539.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 39 TVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLR 118
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 119 DDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPL 198
Cdd:cd07115 79 LDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 199 SAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFA 278
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAG-NLKRVSLELGGKSANIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 279 DCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIR 358
Cdd:cd07115 238 DA-DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 359 EGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSR 436
Cdd:cd07115 317 VGREEGARLLTGgkRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129261 437 AHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
23-495 |
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: 539.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 103 LLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPAL 182
Cdd:cd07119 81 RLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 183 AAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMK 262
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 263 RVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMG 342
Cdd:cd07119 239 KVALELGGKNPNIVFADA-DFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 343 TLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIG----PTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGgkRPTGDELAKGyfvePTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129261 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISLEA 495
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLSP 476
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
22-493 |
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: 535.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFErGDWSLSSPAKRKAVLNKLADLMEAHAEEL 101
Cdd:cd07144 10 LFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE-SWWSKVTGEERGELLDKLADLVEKNRDLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 102 ALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
Cdd:cd07144 89 AAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGdSNM 261
Cdd:cd07144 169 LAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA-QNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 262 KRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQA-QNWQPGHPLDPATT 340
Cdd:cd07144 248 KAVTLECGGKSPALVFEDA-DLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 341 MGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA----IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQAL 415
Cdd:cd07144 327 VGPQVSKTQYDRVLSYIEKGKKEGaKLVYGGEKAPEGLGkgyfIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAI 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129261 416 QLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
Cdd:cd07144 407 KKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHINL 484
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
22-489 |
2.44e-178 |
|
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: 508.58 E-value: 2.44e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEEL 101
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA--WSATSVEERAALLERIAEAYEARADEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 102 ALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKvYGEVATTSShelAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
Cdd:cd07138 79 AQAITLEMGAPITLARAAQVGLGIGHLRAAADALKD-FEFEERRGN---SLVVREPIGVCGLITPWNWPLNQIVLKVAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSnM 261
Cdd:cd07138 155 LAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADT-V 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 262 KRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
Cdd:cd07138 234 KRVALELGGKSANIILDDA-DLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 342 GTLIDCAHADSVHSFIREGESKGQLLL---DGRNAGLAAA--IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
Cdd:cd07138 313 GPLASAAQFDRVQGYIQKGIEEGARLVaggPGRPEGLERGyfVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129261 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVnNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07138 393 IANDTPYGLAGYVWSADPERARAVARRLRAGQVHI-NGAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
40-489 |
1.51e-177 |
|
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: 506.00 E-value: 1.51e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 40 VDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGDWSLSsPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRD 119
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRLS-PAERGRLLLRIARLIREHADELARLESLDTGKPLTQA-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 120 DIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLS 199
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 200 AIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFAD 279
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 280 CpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL-DPatTMGTLIDCAHADSVHSFIR 358
Cdd:cd07109 239 A-DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLeDP--DLGPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 359 EGESKG-QLLLDGRNAGLAAAIG----PTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRD 433
Cdd:cd07109 316 RARARGaRIVAGGRIAEGAPAGGyfvaPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129261 434 LSRAHRMSRRLKAGSVFVNNYND-GDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07109 396 GDRALRVARRLRAGQVFVNNYGAgGGIELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
22-493 |
3.40e-176 |
|
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: 503.80 E-value: 3.40e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEEL 101
Cdd:cd07559 3 NFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 102 ALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNM 261
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE-NL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 262 KRVWLEAGGKSANIVFAD----CPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDP 337
Cdd:cd07559 239 IPVTLELGGKSPNIFFDDamdaDDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 338 ATTMGTLIDCAHADSVHSFIREGESKGQLLLDG--RN--AGLAAA--IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSE 411
Cdd:cd07559 319 ETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGgeRLtlGGLDKGyfYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 412 EQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:cd07559 399 EEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILV 478
|
..
gi 16129261 492 SL 493
Cdd:cd07559 479 SY 480
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
22-493 |
3.59e-174 |
|
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: 498.59 E-value: 3.59e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFErGDWSLS-SPAKRKAVLNKLADLMEAHAEE 100
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE-TDWGLKvSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 101 LALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGP 180
Cdd:cd07143 88 LASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 181 ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSN 260
Cdd:cd07143 168 ALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 261 MKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
Cdd:cd07143 248 LKKVTLELGGKSPNIVFDDA-DLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTF 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 341 MGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLA 418
Cdd:cd07143 327 QGPQVSQIQYERIMSYIESGKAEGATVETGgkRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRA 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129261 419 NDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
Cdd:cd07143 407 NDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
20-492 |
8.35e-170 |
|
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: 487.63 E-value: 8.35e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGD-WSLSSPAKRKAVLNKLADLMEAHA 98
Cdd:cd07141 7 TKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSpWRTMDASERGRLLNKLADLIERDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 99 EELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
Cdd:cd07141 87 AYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
Cdd:cd07141 167 APALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
Cdd:cd07141 247 SNLKRVTLELGGKSPNIVFADA-DLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 339 TTMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
Cdd:cd07141 326 TEQGPQIDEEQFKKILELIESGKKEGAKLECGgkRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIE 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129261 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWIS 492
Cdd:cd07141 406 RANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
20-489 |
2.23e-169 |
|
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: 486.23 E-value: 2.23e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAE 99
Cdd:cd07142 4 TKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 100 ELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLG 179
Cdd:cd07142 84 ELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 180 PALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS 259
Cdd:cd07142 164 PALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 260 NMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPAT 339
Cdd:cd07142 244 NLKPVTLELGGKSPFIVCEDA-DVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 340 TMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQL 417
Cdd:cd07142 323 EQGPQVDKEQFEKILSYIEHGKEEGATLITGgdRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKR 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129261 418 ANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07142 403 ANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
42-491 |
2.97e-168 |
|
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: 482.61 E-value: 2.97e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 42 PVTQAPLAKIARGKSVDIDRAMSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRDDI 121
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 122 PGAARAIRWYAEAIDKVYGEVATT-SSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSA 200
Cdd:cd07118 83 EGAADLWRYAASLARTLHGDSYNNlGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 201 IRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADC 280
Cdd:cd07118 163 LMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 281 pDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREG 360
Cdd:cd07118 242 -DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 361 ESKG-QLLLDGRNAGLAAA--IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRA 437
Cdd:cd07118 321 RAEGaTLLLGGERLASAAGlfYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 16129261 438 HRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
21-489 |
1.10e-166 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 480.47 E-value: 1.10e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEE 100
Cdd:PLN02766 22 KLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 101 LALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGP 180
Cdd:PLN02766 102 LAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 181 ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSN 260
Cdd:PLN02766 182 ALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 261 MKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
Cdd:PLN02766 262 LKQVSLELGGKSPLLIFDDA-DVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 341 MGTLIDCAHADSVHSFIREGESKGQLLLDGrnaGLAAA-----IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQAL 415
Cdd:PLN02766 341 QGPQVDKQQFEKILSYIEHGKREGATLLTG---GKPCGdkgyyIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAI 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129261 416 QLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:PLN02766 418 KKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
22-493 |
1.29e-165 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 476.99 E-value: 1.29e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEEL 101
Cdd:TIGR02299 3 HFIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKR--WAELKAAERKRYLHKIADLIEQHADEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 102 ALLETLDTGKPIRHsLRDDIPGAARAIRWYAE-AIDKVYGEVATTSSHeLAMIVREPVGVIAAIVPWNFPLLLTCWKLGP 180
Cdd:TIGR02299 81 AVLECLDCGQPLRQ-TRQQVIRAAENFRFFADkCEEAMDGRTYPVDTH-LNYTVRVPVGPVGLITPWNAPFMLSTWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 181 ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSn 260
Cdd:TIGR02299 159 ALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMRNGADT- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 261 MKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
Cdd:TIGR02299 238 LKRFSMELGGKSPVIVFDDA-DLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPETE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 341 MGTLIDCAHADSVHSFIREGESKGQLLLDG---RNAGLAAAIG------PTIFVDVDPNASLSREEIFGPVLVVTRFTSE 411
Cdd:TIGR02299 317 VGPLIHPEHLAKVLGYVEAAEKEGATILVGgerAPTFRGEDLGrgnyvlPTVFTGADNHMRIAQEEIFGPVLTVIPFKDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 412 EQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:TIGR02299 397 EEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNVAL 476
|
..
gi 16129261 492 SL 493
Cdd:TIGR02299 477 AL 478
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
22-489 |
9.10e-165 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 474.37 E-value: 9.10e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEEL 101
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 102 ALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKV-YGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGP 180
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFpFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 181 ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsN 260
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE-R 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 261 MKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
Cdd:cd07139 239 LARVTLELGGKSAAIVLDDA-DLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 341 MGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAA--IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGggRPAGLDRGwfVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129261 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYnDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07139 398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
40-489 |
1.65e-163 |
|
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: 470.57 E-value: 1.65e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 40 VDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGDWSLSsPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRD 119
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWSTD-AEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 120 DIPGAARAIRWYAEAIDKVYGEVATTSSHELAM-----IVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSE 194
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPALRGGpgrrvVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 195 KSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSAN 274
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 275 IVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVH 354
Cdd:cd07089 240 IVLDDA-DLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 355 SFIREGESKGQLLLDG--RNAGLAAA--IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVW 430
Cdd:cd07089 319 GYIARGRDEGARLVTGggRPAGLDKGfyVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129261 431 TRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
65-491 |
1.27e-159 |
|
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: 457.08 E-value: 1.27e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 65 AARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRhSLRDDIPGAARAIRWYAEAIDKVYGEVAT 144
Cdd:cd06534 2 AARAAFK--AWAALPPAERAAILRKIADLLEERREELAALETLETGKPIE-EALGEVARAIDTFRYAAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 145 -TSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGF 223
Cdd:cd06534 79 sPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 224 GHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCI 303
Cdd:cd06534 159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDA-DLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 304 AGTRLLLEESIADEFLALLKqqaqnwqpghpldpattmgtlidcahadsvhsfiregeskgqllldgrnaglaaaigpTI 383
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV----------------------------------------------------------TV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 384 FVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM-TVP 462
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGpEAP 338
|
410 420
....*....|....*....|....*....
gi 16129261 463 FGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:cd06534 339 FGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
40-489 |
4.43e-159 |
|
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: 458.82 E-value: 4.43e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 40 VDPVTQAPLAKIARGKSVDIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRD 119
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFK--TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-RG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 120 DIPGAARAIRWYAEAIDKVYGEVATTSS-HELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPL 198
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIPSPApGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 199 SAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFA 278
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAAD-TVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 279 DCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIR 358
Cdd:cd07103 238 DA-DLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 359 EGESKG-QLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSR 436
Cdd:cd07103 317 DAVAKGaKVLTGGKRLGLGGYfYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 16129261 437 AHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07103 397 AWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
21-493 |
6.15e-159 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 460.12 E-value: 6.15e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEE 100
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK--IWAAMTAMERSRILRRAVDILRERNDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 101 LALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGP 180
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 181 ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGhEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSn 260
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 261 MKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDA-DLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 341 MGTLIDCAHADSVHSFIREGESKGQLLLDG----RNAGLA--AAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQA 414
Cdd:PRK13252 323 FGPLVSFAHRDKVLGYIEKGKAEGARLLCGgerlTEGGFAngAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEV 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129261 415 LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
Cdd:PRK13252 403 IARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEM 481
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
21-487 |
6.63e-159 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 459.38 E-value: 6.63e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 21 RLFINGEYtAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEE 100
Cdd:PRK13473 4 KLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 101 LALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVAT------TSshelaMIVREPVGVIAAIVPWNFPLLLT 174
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAAGeyleghTS-----MIRRDPVGVVASIAPWNYPLMMA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 175 CWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLK 254
Cdd:PRK13473 156 AWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 255 DAGDSnMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHP 334
Cdd:PRK13473 235 AAADS-VKRTHLELGGKAPVIVFDDA-DLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 335 LDPATTMGTLIDCAHADSVHSFIRE--GESKGQLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSE 411
Cdd:PRK13473 313 DDEDTELGPLISAAHRDRVAGFVERakALGHIRVVTGGEAPDGKGYyYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129261 412 EQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVnnyNDGDMTV---PFGGYKQSGNGRDKSLHALEKFTELK 487
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWV---NTHFMLVsemPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
22-493 |
2.12e-156 |
|
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: 453.06 E-value: 2.12e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEEL 101
Cdd:cd07117 3 LFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 102 ALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
Cdd:cd07117 81 AMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNM 261
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK-KL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 262 KRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
Cdd:cd07117 239 IPATLELGGKSANIIFDDA-NWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 342 GTLIDCAHADSVHSFIREGESKGQLLLDG----RNAGLAAA--IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQAL 415
Cdd:cd07117 318 GAQVNKDQLDKILSYVDIAKEEGAKILTGghrlTENGLDKGffIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129261 416 QLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
Cdd:cd07117 398 DMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
23-487 |
4.42e-155 |
|
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: 449.65 E-value: 4.42e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFerGDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 103 LLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPAL 182
Cdd:TIGR01804 79 KLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 183 AAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMK 262
Cdd:TIGR01804 159 AAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAG-HLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 263 RVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMG 342
Cdd:TIGR01804 238 HVTMELGGKSPLIVFDDA-DLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 343 TLIDCAHADSVHSFIREGESKGQLLLDG----RNAGL--AAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGggrpENVGLqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129261 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 487
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
40-487 |
3.56e-151 |
|
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: 438.68 E-value: 3.56e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 40 VDPVTQAPLAKIARGKSVDIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRD 119
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFP--SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 120 DIPGAARAIRWYAEAIDKVYGEVAT------TSshelaMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPS 193
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTLEGPAAGeylpghTS-----MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 194 EKSPLSAIRLAGLAKEaGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSA 273
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 274 NIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSV 353
Cdd:cd07092 233 VIVFDDA-DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 354 HSFIREGESKGQLLLDGRNA-GLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTR 432
Cdd:cd07092 312 AGFVERAPAHARVLTGGRRAeGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 16129261 433 DLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 487
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIK 446
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
39-491 |
7.98e-151 |
|
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: 438.28 E-value: 7.98e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 39 TVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIrHSLR 118
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE--WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPI-EEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 119 DDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPL 198
Cdd:cd07090 78 VDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 199 SAIRLAGLAKEAGLPDGVLNVVTGFGhEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFA 278
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAK-GIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 279 DCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIR 358
Cdd:cd07090 236 DA-DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 359 EGESKGQLLLDGRN-----AGLA--AAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWT 431
Cdd:cd07090 315 SAKQEGAKVLCGGErvvpeDGLEngFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 432 RDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
20-493 |
1.35e-150 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 440.78 E-value: 1.35e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAE 99
Cdd:PLN02466 58 TQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 100 ELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLG 179
Cdd:PLN02466 138 ELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 180 PALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS 259
Cdd:PLN02466 218 PALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKS 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 260 NMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPAT 339
Cdd:PLN02466 298 NLKPVTLELGGKSPFIVCEDA-DVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 340 TMGTLIDCAHADSVHSFIREG-ESKGQLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQL 417
Cdd:PLN02466 377 EQGPQIDSEQFEKILRYIKSGvESGATLECGGDRFGSKGYyIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRR 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129261 418 ANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
Cdd:PLN02466 457 ANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTPL 532
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
39-493 |
9.02e-148 |
|
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: 430.26 E-value: 9.02e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 39 TVDPVTQAPLAKIARGKSVDIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRhSLR 118
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP--EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 119 DDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPL 198
Cdd:cd07107 78 GDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 199 SAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSnMKRVWLEAGGKSANIVFA 278
Cdd:cd07107 158 SALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 279 DCpDLQQAASATAAGI-FYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFI 357
Cdd:cd07107 236 DA-DPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 358 REGESKGQLLLDG--RNAGLAAAIG----PTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWT 431
Cdd:cd07107 315 DSAKREGARLVTGggRPEGPALEGGfyvePTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129261 432 RDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
39-489 |
2.58e-147 |
|
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: 429.08 E-value: 2.58e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 39 TVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLR 118
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 119 DdIPGAARAIRWYA---EAIDKVYGEVATTSSHELAMIVR-EPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSE 194
Cdd:cd07110 79 D-VDDVAGCFEYYAdlaEQLDAKAERAVPLPSEDFKARVRrEPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 195 KSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGdSNMKRVWLEAGGKSAN 274
Cdd:cd07110 158 LTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA-QDIKPVSLELGGKSPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 275 IVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVH 354
Cdd:cd07110 237 IVFDDA-DLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 355 SFIREGESKG-QLLLDGRNAGLAAA---IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVW 430
Cdd:cd07110 316 SFIARGKEEGaRLLCGGRRPAHLEKgyfIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129261 431 TRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
15-491 |
5.14e-144 |
|
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: 421.90 E-value: 5.14e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 15 SLAIENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGDWSLSSPAKRKAVLNKLADLM 94
Cdd:cd07140 1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 95 EAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTS----SHELAMIVREPVGVIAAIVPWNFP 170
Cdd:cd07140 81 EEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 171 LLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGK 250
Cdd:cd07140 161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 251 QLLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQ 330
Cdd:cd07140 241 HIMKSCAVSNLKKVSLELGGKSPLIIFADC-DMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 331 PGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRF 408
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGaTLVYGGKQVDRPGFfFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 409 TSE--EQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTEL 486
Cdd:cd07140 400 DDGdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKT 479
|
....*
gi 16129261 487 KTIWI 491
Cdd:cd07140 480 KTVTI 484
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
21-483 |
4.06e-143 |
|
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: 419.49 E-value: 4.06e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEE 100
Cdd:cd07111 23 GHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 101 LALLETLDTGKPIRHSlRD-DIPGAARAIRWYAEAIDKVygevattsshELAMIVREPVGVIAAIVPWNFPLLLTCWKLG 179
Cdd:cd07111 101 FAVLESLDNGKPIRES-RDcDIPLVARHFYHHAGWAQLL----------DTELAGWKPVGVVGQIVPWNFPLLMLAWKIC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 180 PALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHeAGQALSRHNDIDAIAFTGSTRTGKQLLKD-AGD 258
Cdd:cd07111 170 PALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRAtAGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 259 SnmKRVWLEAGGKSANIVFaDCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
Cdd:cd07111 249 G--KKLSLELGGKSPFIVF-DDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 339 TTMGTLIDCAHADSVHSFIREGESKG----QLLLDGRNAGLAAAigPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQA 414
Cdd:cd07111 326 IDMGAIVDPAQLKRIRELVEEGRAEGadvfQPGADLPSKGPFYP--PTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEA 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129261 415 LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKF 483
Cdd:cd07111 404 VALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
39-491 |
2.17e-142 |
|
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: 416.76 E-value: 2.17e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 39 TVDPVTQAPLAKIARGKSVDIDRAMSAARGVFerGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLR 118
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 119 DDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPL 198
Cdd:cd07108 79 PEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 199 SAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFA 278
Cdd:cd07108 159 AVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 279 DCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIR 358
Cdd:cd07108 237 DADLDDAVDGAIAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 359 EG-ESKGQLLLDGRNAGLAAA------IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWT 431
Cdd:cd07108 317 LGlSTSGATVLRGGPLPGEGPladgffVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129261 432 RDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHA-LEKFTELKTIWI 491
Cdd:cd07108 397 RDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTVNI 457
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
40-491 |
1.08e-140 |
|
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: 411.92 E-value: 1.08e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 40 VDPVTQAPLAKIARGKSVDIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRD 119
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFP--GWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 120 DIPGAARAIRWYA--EAIDKVYGEVATTSshelAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSP 197
Cdd:cd07106 79 EVGGAVAWLRYTAslDLPDEVIEDDDTRR----VELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 198 LSAIRLAGLAKEAgLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVF 277
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAK-TLKRVTLELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 278 ADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFI 357
Cdd:cd07106 232 PDV-DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 358 REGESKGQLLLDGrnaGLAAA-----IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTR 432
Cdd:cd07106 311 EDAKAKGAKVLAG---GEPLDgpgyfIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSS 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129261 433 DLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:cd07106 388 DLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
22-491 |
1.43e-140 |
|
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: 412.99 E-value: 1.43e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFeRGDWSLSSPAKRKAVLNKLADLMEAHAEEL 101
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAF-VSAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 102 ALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTS------SHELAMIVREPVGVIAAIVPWNFPLLLTC 175
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSipsmqgERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 176 WKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGhEAGQALSRHNDIDAIAFTGSTRTGKQLLKD 255
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 256 AGdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL 335
Cdd:cd07113 240 AA-SDLTRVTLELGGKNAAAFLKDA-DIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 336 DPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNA--GLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQ 413
Cdd:cd07113 318 DESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEAlaGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129261 414 ALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:cd07113 398 LIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
23-487 |
9.83e-140 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 411.39 E-value: 9.83e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP--SWSKLTASERSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 103 LLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEV-ATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
Cdd:PLN02278 106 QLMTLEQGKPLKEA-IGEVAYGASFLEYFAEEAKRVYGDIiPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSnM 261
Cdd:PLN02278 185 LAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT-V 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 262 KRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
Cdd:PLN02278 264 KRVSLELGGNAPFIVFDDA-DLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 342 GTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAAI-GPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLAN 419
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGaKVLLGGKRHSLGGTFyEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAN 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129261 420 DSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 487
Cdd:PLN02278 423 DTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIK 490
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
17-494 |
1.82e-138 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 408.35 E-value: 1.82e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 17 AIENR-LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFER---GDWSLSSPAKRKAVLNKLAD 92
Cdd:PLN02467 4 PVPRRqLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgKDWARTTGAVRAKYLRAIAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 93 LMEAHAEELALLETLDTGKPIRHSLRDdIPGAARAIRWYA---EAIDKvygevATTSSHELAM------IVREPVGVIAA 163
Cdd:PLN02467 84 KITERKSELAKLETLDCGKPLDEAAWD-MDDVAGCFEYYAdlaEALDA-----KQKAPVSLPMetfkgyVLKEPLGVVGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 164 IVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFT 243
Cdd:PLN02467 158 ITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 244 GSTRTGKQLLKDAGdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLK 323
Cdd:PLN02467 238 GSTATGRKIMTAAA-QMVKPVSLELGGKSPIIVFDDV-DLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 324 QQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAA--IGPTIFVDVDPNASLSREEIF 399
Cdd:PLN02467 316 KWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGgkRPEHLKKGffIEPTIITDVTTSMQIWREEVF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 400 GPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHA 479
Cdd:PLN02467 396 GPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWG 475
|
490
....*....|....*..
gi 16129261 480 LEKFTELK--TIWISLE 494
Cdd:PLN02467 476 LENYLSVKqvTKYISDE 492
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
37-491 |
4.75e-138 |
|
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: 405.58 E-value: 4.75e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 37 FETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHS 116
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV--MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 117 lRDDIPGAARAIRWYAEAIDKVYGEVATTSSHE-----LAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILK 191
Cdd:cd07145 79 -RVEVERTIRLFKLAAEEAKVLRGETIPVDAYEynerrIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 192 PSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGdSNMKRVWLEAGGK 271
Cdd:cd07145 158 PSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 272 SANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHAD 351
Cdd:cd07145 237 DPMIVLKDA-DLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 352 SVHSFIREGESKGQLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWT 431
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGKRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129261 432 RDLSRAHRMSRRLKAGSVFVNN---YNDGDMtvPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:cd07145 396 NDINRALKVARELEAGGVVINDstrFRWDNL--PFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
23-492 |
1.65e-137 |
|
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: 405.30 E-value: 1.65e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELA 102
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 103 LLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPAL 182
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 183 AAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMK 262
Cdd:cd07116 162 AAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 263 RVWLEAGGKSANIVFADCPDLQQAASATAAGIF----YNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
Cdd:cd07116 240 PVTLELGGKSPNIFFADVMDADDAFFDKALEGFvmfaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 339 TTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAAIG-----PTIFVDVDpNASLSREEIFGPVLVVTRFTSEE 412
Cdd:cd07116 320 TMIGAQASLEQLEKILSYIDIGKEEGaEVLTGGERNELGGLLGggyyvPTTFKGGN-KMRIFQEEIFGPVLAVTTFKDEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 413 QALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWIS 492
Cdd:cd07116 399 EALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLVS 478
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
37-489 |
2.44e-136 |
|
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: 401.20 E-value: 2.44e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 37 FETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGDwslSSPA-KRKAVLNKLADLMEAHAEELALLETLDTGKPIRH 115
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMK---SLPAyERAEILERAAQLLEERREEFARTIALEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 116 SLRDdipgAARAIRWY---AEAIDKVYGEV-----ATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNS 187
Cdd:cd07149 78 ARKE----VDRAIETLrlsAEEAKRLAGETipfdaSPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 188 VILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGdsnMKRVWLE 267
Cdd:cd07149 154 VVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 268 AGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDC 347
Cdd:cd07149 231 LGSNAAVIVDADA-DLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 348 AHADSVHSFIREGESKG-QLLLDGRNAGlaAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLG 426
Cdd:cd07149 310 AEAERIEEWVEEAVEGGaRLLTGGKRDG--AILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129261 427 AAVWTRDLSRAHRMSRRLKAGSVFVN---NYNDGDMtvPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07149 388 AGVFTNDLQKALKAARELEVGGVMINdssTFRVDHM--PYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
23-491 |
4.27e-136 |
|
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: 400.87 E-value: 4.27e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK--AWERLPAIERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 103 LLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEV-ATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
Cdd:cd07088 79 KLIVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIiPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNM 261
Cdd:cd07088 158 LVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-NI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 262 KRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDA-DLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 342 GTLIDCAHADSVHSFIREG-ESKGQLLLDGRNAGLAAA--IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLA 418
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAvEAGATLLTGGKRPEGEKGyfYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129261 419 NDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
39-489 |
3.39e-135 |
|
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: 398.26 E-value: 3.39e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 39 TVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGDWSlSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlR 118
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEA-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 119 DDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPL 198
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 199 SAIRLAGLAKEA-GLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGdSNMKRVWLEAGGKSANIVF 277
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 278 ADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFI 357
Cdd:cd07120 238 DDA-DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 358 REGESKG-QLLLDGR--NAGLA--AAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTR 432
Cdd:cd07120 317 ERAIAAGaEVVLRGGpvTEGLAkgAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129261 433 DLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07120 397 DLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
23-491 |
7.50e-135 |
|
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: 398.16 E-value: 7.50e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 23 FINGEYTAAAEneTFETVDPV-TQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEEL 101
Cdd:cd07097 4 YIDGEWVAGGD--GEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 102 ALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGE-VATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGP 180
Cdd:cd07097 80 ARLLTREEGKTLPEA-RGEVTRAGQIFRYYAGEALRLSGEtLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 181 ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGdSN 260
Cdd:cd07097 159 ALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-AR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 261 MKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDA-DLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 341 MGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAAIG----PTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEGyylaPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129261 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDG-DMTVPFGGYKQSGNG-RDKSLHALEKFTELKTIWI 491
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGvDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTVYV 473
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
58-493 |
2.60e-131 |
|
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: 387.66 E-value: 2.60e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 58 DIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKpIRHSLRDDIPGAARAIRWYAEAIDK 137
Cdd:cd07104 1 DVDRAYAAAAAAQK--AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGS-TRPKAAFEVGAAIAILREAAGLPRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 138 VYGEV-ATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLS-AIRLAGLAKEAGLPDG 215
Cdd:cd07104 78 PEGEIlPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 216 VLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIF 295
Cdd:cd07104 158 VLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDA-DLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 296 YNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAG 374
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGaRLLTGGTYEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 375 LAAAigPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNny 454
Cdd:cd07104 316 LFYQ--PTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIN-- 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 16129261 455 ndgDMTV------PFGGYKQSGNGRDKSLHALEKFTELKtiWISL 493
Cdd:cd07104 392 ---DQTVndephvPFGGVKASGGGRFGGPASLEEFTEWQ--WITV 431
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
37-493 |
1.99e-130 |
|
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: 385.91 E-value: 1.99e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 37 FETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHS 116
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP--AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 117 LRDdIPGAARAIRWYAEAIDKVYGEV-----ATTSShelaMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILK 191
Cdd:cd07150 79 WFE-TTFTPELLRAAAGECRRVRGETlpsdsPGTVS----MSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 192 PSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGdSNMKRVWLEAGGK 271
Cdd:cd07150 154 PSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG-RHLKKITLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 272 SANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHAD 351
Cdd:cd07150 233 NPLIVLADA-DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 352 SVHSFIREGESKG-QLLLDGRNAGLAAAigPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVW 430
Cdd:cd07150 312 RIKRQVEDAVAKGaKLLTGGKYDGNFYQ--PTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAIL 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129261 431 TRDLSRAHRMSRRLKAGSVFVNNYN-DGDMTVPFGGYKQSGNGRDKSLHALEKFTELKtiWISL 493
Cdd:cd07150 390 TNDLQRAFKLAERLESGMVHINDPTiLDEAHVPFGGVKASGFGREGGEWSMEEFTELK--WITV 451
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
23-491 |
8.30e-129 |
|
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: 382.85 E-value: 8.30e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 23 FINGEYTAAAENETFETVDPV-TQAPLAKIARGKSVDIDRAMSAARGVFerGDWSLSSPAKRKAVLNKLADLMEAHAEEL 101
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAF--PEWRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 102 ALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEvaTTSShEL----AMIVREPVGVIAAIVPWNFPLLLTCWK 177
Cdd:cd07131 80 ARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGE--TVPS-ELpnkdAMTRRQPIGVVALITPWNFPVAIPSWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 178 LGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAG 257
Cdd:cd07131 156 IFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 258 DSNmKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDP 337
Cdd:cd07131 236 RPN-KRVALEMGGKNPIIVMDDA-DLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 338 ATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNA---GLAAA--IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSE 411
Cdd:cd07131 314 ETDMGPLINEAQLEKVLNYNEIGKEEGaTLLLGGERLtggGYEKGyfVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 412 EQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDG-DMTVPFGGYKQSGNG-RDKSLHALEKFTELKTI 489
Cdd:cd07131 394 EEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGaEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
..
gi 16129261 490 WI 491
Cdd:cd07131 474 YV 475
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
38-491 |
6.24e-120 |
|
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: 359.05 E-value: 6.24e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 38 ETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSL 117
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAEN--RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 118 RDdIPGAARAIRWYAEAIDKVYGEV-----ATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKP 192
Cdd:cd07094 80 VE-VDRAIDTLRLAAEEAERIRGEEipldaTQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 193 SEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGdsnMKRVWLEAGGKS 272
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 273 ANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADS 352
Cdd:cd07094 236 PVIVDRDA-DLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 353 VHSFIREGESKG-QLLLDGRNAGlaAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWT 431
Cdd:cd07094 315 VERWVEEAVEAGaRLLCGGERDG--ALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129261 432 RDLSRAHRMSRRLKAGSVFVNNYNDGDM-TVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:cd07094 393 RDLNVAFKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
59-491 |
3.18e-118 |
|
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: 354.07 E-value: 3.18e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 59 IDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKV 138
Cdd:cd07100 1 IEAALDRAHAAFL--AWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYAENAEAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 139 YGEVATTSSHELAMIVREPVGVIAAIVPWNFPLlltcWK----LGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPD 214
Cdd:cd07100 78 LADEPIETDAGKAYVRYEPLGVVLGIMPWNFPF----WQvfrfAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 215 GVL-NVVTGfgHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGdSNMKRVWLEAGGKSANIVFADcPDLQQAASATAAG 293
Cdd:cd07100 154 GVFqNLLID--SDQVEAIIADPRVRGVTLTGSERAGRAVAAEAG-KNLKKSVLELGGSDPFIVLDD-ADLDKAVKTAVKG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 294 IFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDG--R 371
Cdd:cd07100 230 RLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGgkR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 372 NAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFV 451
Cdd:cd07100 310 PDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFI 389
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 16129261 452 NNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:cd07100 390 NGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
4-489 |
1.88e-117 |
|
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: 354.99 E-value: 1.88e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 4 HHLAYwqDKALS-----LAIENRLFINGEYTAAaeNETFETVDPV-TQAPLAKIARGKSVDIDRAMSAARGVFErgDWSL 77
Cdd:cd07124 14 NRAAF--RAALArvreeLGREYPLVIGGKEVRT--EEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFP--TWRR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 78 SSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDdipgAARAI---RWYAEAIDKVYGEVATTSSHELAMIV 154
Cdd:cd07124 88 TPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADAD----VAEAIdflEYYAREMLRLRGFPVEMVPGEDNRYV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 155 REPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRH 234
Cdd:cd07124 164 YRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEH 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 235 NDIDAIAFTGSTRTGKQLLKDA-----GDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLL 309
Cdd:cd07124 244 PDVRFIAFTGSREVGLRIYERAakvqpGQKWLKRVIAEMGGKNAIIVDEDA-DLDEAAEGIVRSAFGFQGQKCSACSRVI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 310 LEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAA---IGPTIFVD 386
Cdd:cd07124 323 VHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAEgyfVQPTIFAD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 387 VDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMtV---PF 463
Cdd:cd07124 403 VPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGAL-VgrqPF 481
|
490 500
....*....|....*....|....*..
gi 16129261 464 GGYKQSG-NGRDKSLHALEKFTELKTI 489
Cdd:cd07124 482 GGFKMSGtGSKAGGPDYLLQFMQPKTV 508
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
40-489 |
1.48e-116 |
|
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: 350.37 E-value: 1.48e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 40 VDPVTQAPLAKIARGKSVDIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPiRHSLRD 119
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQR--AWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 120 DIPGAARAIRWYAEAIDKV--YGEVATTS--SHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEK 195
Cdd:cd07099 78 EVLLALEAIDWAARNAPRVlaPRKVPTGLlmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 196 SPLSAIRLAGLAKEAGLPDGVLNVVTGFGhEAGQALSRHNdIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANI 275
Cdd:cd07099 158 TPLVGELLAEAWAAAGPPQGVLQVVTGDG-ATGAALIDAG-VDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 276 VFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHS 355
Cdd:cd07099 235 VLADA-DLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 356 FIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRD 433
Cdd:cd07099 314 HVDDAVAKGAKALTGgaRSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129261 434 LSRAHRMSRRLKAGSVFVNN--YNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
58-489 |
1.72e-116 |
|
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: 349.57 E-value: 1.72e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 58 DIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPiRHSLRDDIPGAARAIRWYAEAIDK 137
Cdd:cd07105 1 DADQAVEAAAAAFP--AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT-AAWAGFNVDLAAGMLREAASLITQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 138 VYGEVATTSSHE-LAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGV 216
Cdd:cd07105 78 IIGGSIPSDKPGtLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 217 LNVVTGFGHEAGQ---ALSRHNDIDAIAFTGSTRTGKQLLKDAGdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAG 293
Cdd:cd07105 158 LNVVTHSPEDAPEvveALIAHPAVRKVNFTGSTRVGRIIAETAA-KHLKPVLLELGGKAPAIVLEDA-DLDAAANAALFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 294 IFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGhpldpATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNA 373
Cdd:cd07105 236 AFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 374 ---GLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVF 450
Cdd:cd07105 311 desPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 16129261 451 VNNYNDGD-MTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07105 391 INGMTVHDePTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
26-494 |
7.23e-115 |
|
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: 346.60 E-value: 7.23e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 26 GEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLE 105
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA--QKEWAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 106 TLDTGKPIrhsLRDDIP-GAARAI-RWYAEAIDKVYGEV--ATTSSHElAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
Cdd:cd07151 79 IRESGSTR---IKANIEwGAAMAItREAATFPLRMEGRIlpSDVPGKE-NRVYREPLGVVGVISPWNFPLHLSMRSVAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 182 LAAGNSVILKPSEKSPLSA-IRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsN 260
Cdd:cd07151 155 LALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR-H 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 261 MKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
Cdd:cd07151 234 LKKVALELGGNNPFVVLEDA-DIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 341 MGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAaaIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLAN 419
Cdd:cd07151 313 VGPLINESQVDGLLDKIEQAVEEGaTLLVGGEAEGNV--LEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 420 DSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNnyndgDMTV------PFGGYKQSGNGRDKSLHALEKFTELKtiWISL 493
Cdd:cd07151 391 DTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-----DQPVndephvPFGGEKNSGLGRFNGEWALEEFTTDK--WISV 463
|
.
gi 16129261 494 E 494
Cdd:cd07151 464 Q 464
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
38-489 |
3.78e-114 |
|
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: 344.34 E-value: 3.78e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 38 ETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdwslSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSL 117
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEEALREALALAASYRST-----LTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 118 RDdIPGAARAIRWYAEAIDKVYGE-----VATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKP 192
Cdd:cd07146 77 YE-VGRAADVLRFAAAEALRDDGEsfscdLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 193 SEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGdsnMKRVWLEAGGKS 272
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 273 ANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADS 352
Cdd:cd07146 233 PLIVMDDA-DLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 353 VHSFIREGESKG-QLLLDGRNAGlaAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWT 431
Cdd:cd07146 312 IENRVEEAIAQGaRVLLGNQRQG--ALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129261 432 RDLSRAHRMSRRLKAGSVfvnNYNDG----DMTVPFGGYKQSGNG-RDKSLHALEKFTELKTI 489
Cdd:cd07146 390 NDLDTIKRLVERLDVGTV---NVNEVpgfrSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
21-489 |
4.03e-113 |
|
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: 342.57 E-value: 4.03e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEE 100
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP--AWSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 101 LALLETLDTGKPIRHSlRDDIpgaARAIrwyaEAIdkvygEVATTSSHEL-------------AMIVREPVGVIAAIVPW 167
Cdd:cd07085 80 LARLITLEHGKTLADA-RGDV---LRGL----EVV-----EFACSIPHLLkgeylenvargidTYSYRQPLGVVAGITPF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 168 NFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTR 247
Cdd:cd07085 147 NFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 248 TGKQLLKDAGdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQ 327
Cdd:cd07085 226 VGEYIYERAA-ANGKRVQALGGAKNHAVVMPDA-DLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 328 NWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-----IGPTIFVDVDPNASLSREEIFGP 401
Cdd:cd07085 304 KLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGaKLVLDGRGVKVPGYengnfVGPTILDNVTPDMKIYKEEIFGP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 402 VLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNnyndgdMTVP-------FGGYKQSGNGrd 474
Cdd:cd07085 384 VLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN------VPIPvplaffsFGGWKGSFFG-- 455
|
490 500
....*....|....*....|
gi 16129261 475 kSLHALEK-----FTELKTI 489
Cdd:cd07085 456 -DLHFYGKdgvrfYTQTKTV 474
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
23-489 |
1.70e-112 |
|
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: 340.70 E-value: 1.70e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 23 FINGEYTAAaENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFeRGDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
Cdd:cd07082 5 LINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAG-RGWWPTMPLEERIDCLHKFADLLKENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 103 LLETLDTGKPIRHSLRDDIPGAARaIRWYAEAIDKVYGEVATTSSHE-----LAMIVREPVGVIAAIVPWNFPLLLTCWK 177
Cdd:cd07082 83 NLLMWEIGKTLKDALKEVDRTIDY-IRDTIEELKRLDGDSLPGDWFPgtkgkIAQVRREPLGVVLAIGPFNYPLNLTVSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 178 LGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAG 257
Cdd:cd07082 162 LIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 258 dsnMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIF-YNqGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLD 336
Cdd:cd07082 242 ---MKRLVLELGGKDPAIVLPDA-DLELAAKEIVKGALsYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 337 PATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
Cdd:cd07082 317 NGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIE 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129261 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYND-GDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07082 397 LANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrGPDHFPFLGRKDSGIGTQGIGDALRSMTRRKGI 470
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
37-487 |
2.11e-108 |
|
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: 329.59 E-value: 2.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 37 FETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHS 116
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRP--MRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 117 lRDDIPGAARAIRWYAEAIDKVYGEVATTSSHE-----LAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILK 191
Cdd:cd07147 79 -RGEVARAIDTFRIAAEEATRIYGEVLPLDISArgegrQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 192 PSEKSPLSAIRLAGLAKEAGLPDGVLNVVTgFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsnmKRVWLEAGGK 271
Cdd:cd07147 158 PASRTPLSALILGEVLAETGLPKGAFSVLP-CSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 272 SANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHAD 351
Cdd:cd07147 234 AAVIVDSDA-DLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 352 SVHSFIREGESKG-QLLLDGRNAGlaAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVW 430
Cdd:cd07147 313 RVEGWVNEAVDAGaKLLTGGKRDG--ALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 431 TRDLSRAHRMSRRLKAGSVFVNN---YNDGDMtvPFGGYKQSGNGRDKSLHALEKFTELK 487
Cdd:cd07147 391 TRDLEKALRAWDELEVGGVVINDvptFRVDHM--PYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
30-489 |
3.29e-106 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 326.45 E-value: 3.29e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 30 AAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDT 109
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA--QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 110 GKPIRHSLrDDIPGAARAIRWYAEAIDKVYGE--------VATTSSHelamiVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
Cdd:PRK09407 105 GKARRHAF-EEVLDVALTARYYARRAPKLLAPrrragalpVLTKTTE-----LRQPKGVVGVISPWNYPLTLAVSDAIPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHndIDAIAFTGSTRTGKQLLKDAGdSNM 261
Cdd:PRK09407 179 LLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAG-RRL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 262 KRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
Cdd:PRK09407 256 IGFSLELGGKNPMIVLDDA-DLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 342 GTLIDCAHADSVHSFIREGESKGQLLLDGRNAglAAAIG-----PTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
Cdd:PRK09407 335 GSLISEAQLETVSAHVDDAVAKGATVLAGGKA--RPDLGplfyePTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129261 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVfvnNYNDG------DMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:PRK09407 413 RANDTPYGLNASVWTGDTARGRAIAARIRAGTV---NVNEGyaaawgSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
48-493 |
5.20e-106 |
|
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: 323.09 E-value: 5.20e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 48 LAKIARGKSVDIDRAmsAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKpIRHSLRDDIPGAARA 127
Cdd:cd07152 4 LGEVGVADAADVDRA--AARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGS-IRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 128 IRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSA-IRLAGL 206
Cdd:cd07152 81 LHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 207 AKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQA 286
Cdd:cd07152 161 FEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDA-DLDLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 287 ASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-Q 365
Cdd:cd07152 238 ASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGaR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 366 LLLDGRNAGLAAAigPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLK 445
Cdd:cd07152 318 LEAGGTYDGLFYR--PTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 16129261 446 AGSVFVNnyndgDMTV------PFGGYKQSGNGRDKSLHA-LEKFTELKtiWISL 493
Cdd:cd07152 396 TGMLHIN-----DQTVndephnPFGGMGASGNGSRFGGPAnWEEFTQWQ--WVTV 443
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
23-491 |
1.22e-102 |
|
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: 315.66 E-value: 1.22e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 23 FINGEYTAAAEnETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFerGDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
Cdd:cd07086 2 VIGGEWVGSGG-ETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF--KEWRKVPAPRRGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 103 LLETLDTGKPIRHSLRDdipgaarairwYAEAID----------KVYGEVATT--SSHELaMIVREPVGVIAAIVPWNFP 170
Cdd:cd07086 79 RLVSLEMGKILPEGLGE-----------VQEMIDicdyavglsrMLYGLTIPSerPGHRL-MEQWNPLGVVGVITAFNFP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 171 LLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEA----GLPDGVLNVVTGFGhEAGQALSRHNDIDAIAFTGST 246
Cdd:cd07086 147 VAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGST 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 247 RTGKQLLKDAGDSNmKRVWLEAGGKSANIVFaDCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQA 326
Cdd:cd07086 226 EVGRRVGETVARRF-GRVLLELGGNNAIIVM-DDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 327 QNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA---IGPTIFVDVDPNASLSREEIFGPV 402
Cdd:cd07086 304 KQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGgTVLTGGKRIDGGEPgnyVEPTIVTGVTDDARIVQEETFAPI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 403 LVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHR-MSRR-LKAGSVFVNNYNDG-DMTVPFGGYKQSGNGRDKSLHA 479
Cdd:cd07086 384 LYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRwLGPKgSDCGIVNVNIPTSGaEIGGAFGGEKETGGGRESGSDA 463
|
490
....*....|..
gi 16129261 480 LEKFTELKTIWI 491
Cdd:cd07086 464 WKQYMRRSTCTI 475
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
59-489 |
3.54e-101 |
|
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: 311.10 E-value: 3.54e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 59 IDRAMSAARGvfergdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKV 138
Cdd:cd07102 24 LERARAAQKG------WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-GGEIRGMLERARYMISIAEEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 139 YGEV-ATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVL 217
Cdd:cd07102 97 LADIrVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 218 NVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYN 297
Cdd:cd07102 177 QVLHL-SHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYVRPDA-DLDAAAESLVDGAFFN 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 298 QGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLA 376
Cdd:cd07102 254 SGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGaRALIDGALFPED 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 377 AA----IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVN 452
Cdd:cd07102 334 KAggayLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMN 413
|
410 420 430
....*....|....*....|....*....|....*..
gi 16129261 453 NYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07102 414 RCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
41-489 |
3.76e-100 |
|
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: 308.47 E-value: 3.76e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 41 DPVTQAPLAKIARGKSVDIDRAMSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLrDD 120
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAA--QRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAF-EE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 121 IPGAARAIRWYAEAIDKVYGE--------VATTSSHElamivREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKP 192
Cdd:cd07101 79 VLDVAIVARYYARRAERLLKPrrrrgaipVLTRTTVN-----RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 193 SEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHndIDAIAFTGSTRTGKQLLKDAGdSNMKRVWLEAGGKS 272
Cdd:cd07101 154 DSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAG-RRLIGCSLELGGKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 273 ANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADS 352
Cdd:cd07101 231 PMIVLEDA-DLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 353 VHSFIREGESKGQLLLDGRNAglAAAIGP-----TIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGA 427
Cdd:cd07101 310 VTAHVDDAVAKGATVLAGGRA--RPDLGPyfyepTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129261 428 AVWTRDLSRAHRMSRRLKAGSVfvnNYNDG------DMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07101 388 SVWTRDGARGRRIAARLRAGTV---NVNEGyaaawaSIDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
23-493 |
3.48e-98 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 304.52 E-value: 3.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELA 102
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPA--WRALTAKERANILRRWFNLMMEHQDDLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 103 LLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIV-REPVGVIAAIVPWNFPLLLTCWKLGPA 181
Cdd:PRK11241 92 RLMTLEQGKPLAEA-KGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIViKQPIGVTAAITPWNFPAAMITRKAGPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGdSNM 261
Cdd:PRK11241 171 LAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCA-KDI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 262 KRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
Cdd:PRK11241 250 KKVSLELGGNAPFIVFDDA-DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 342 GTLIDCAHADSVHSFIREGESKGQLLLDGrnaGLAAAIG-----PTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
Cdd:PRK11241 329 GPLIDEKAVAKVEEHIADALEKGARVVCG---GKAHELGgnffqPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129261 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
Cdd:PRK11241 406 QANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
40-473 |
1.52e-91 |
|
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: 286.50 E-value: 1.52e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 40 VDPVTQAPLAKIARGKSVDIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRD 119
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQR--EWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 120 DIPGAARAIRWYAEaidkvYGEVA---------TTSSHELAMIVREPVGVIAAIVPWNFPL--LLtcwklGPALAA---G 185
Cdd:cd07098 79 EILVTCEKIRWTLK-----HGEKAlrpesrpggLLMFYKRARVEYEPLGVVGAIVSWNYPFhnLL-----GPIIAAlfaG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 186 NSVILKPSEKSPLSAIRLAGLAKEA----GLPDGVLNVVTGFGhEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSnM 261
Cdd:cd07098 149 NAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAES-L 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 262 KRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
Cdd:cd07098 227 TPVVLELGGKDPAIVLDDA-DLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 342 GTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIG----PTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQAL 415
Cdd:cd07098 306 GAMISPARFDRLEELVADAVEKGARLLAGgkRYPHPEYPQGhyfpPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAV 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 416 QLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTV--PFGGYKQSGNGR 473
Cdd:cd07098 386 EIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQqlPFGGVKGSGFGR 445
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
22-489 |
1.38e-89 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 282.98 E-value: 1.38e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 22 LFINGE--YTAaaenETFETVDPV-TQAPLAKIARGKSVDIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHA 98
Cdd:PRK03137 39 LIIGGEriTTE----DKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE--TWKKWSPEDRARILLRAAAIIRRRK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 99 EELALLETLDTGKPIRHSLRDdipgAARAI---RWYA-EAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLT 174
Cdd:PRK03137 113 HEFSAWLVKEAGKPWAEADAD----TAEAIdflEYYArQMLKLADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 175 CWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLK 254
Cdd:PRK03137 189 AGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 255 DA-----GDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNW 329
Cdd:PRK03137 269 RAakvqpGQIWLKRVIAEMGGKDAIVVDEDA-DLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKEL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 330 QPGHPLDPAtTMGTLIDCAHADSVHSFIREGESKGQLLLDG-RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRF 408
Cdd:PRK03137 348 TVGNPEDNA-YMGPVINQASFDKIMSYIEIGKEEGRLVLGGeGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 409 TSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSG-NGRDKSLHALEKFTE 485
Cdd:PRK03137 427 KDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIvgYHPFGGFNMSGtDSKAGGPDYLLLFLQ 506
|
....
gi 16129261 486 LKTI 489
Cdd:PRK03137 507 AKTV 510
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
39-490 |
1.86e-85 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 270.96 E-value: 1.86e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 39 TVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlR 118
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA-R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 119 DDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPL 198
Cdd:PRK13968 88 AEVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 199 SAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALsrhND--IDAIAFTGSTRTGKQLLKDAGdSNMKRVWLEAGGKSANIV 276
Cdd:PRK13968 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMI---NDsrIAAVTVTGSVRAGAAIGAQAG-AALKKCVLELGGSDPFIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 277 FADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSF 356
Cdd:PRK13968 244 LNDA-DLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 357 IREGESKG-QLLLDGRN-AGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDL 434
Cdd:PRK13968 323 VEATLAEGaRLLLGGEKiAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDE 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 16129261 435 SRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIW 490
Cdd:PRK13968 403 TQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
87-491 |
6.89e-82 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 259.67 E-value: 6.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 87 LNKLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGE-VATTSSHELAMIVREPVGVIAAIV 165
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEiIQSDRPGENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 166 PWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGS 245
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 246 TRTGKQLLkDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQ 325
Cdd:PRK10090 160 VSAGEKIM-AAAAKNITKVCLELGGKAPAIVMDDA-DLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 326 AQNWQPGHPLD-PATTMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPV 402
Cdd:PRK10090 238 MQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGgkAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 403 LVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEK 482
Cdd:PRK10090 318 LPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHE 397
|
....*....
gi 16129261 483 FTELKTIWI 491
Cdd:PRK10090 398 YLQTQVVYL 406
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
32-491 |
2.18e-80 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 257.36 E-value: 2.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 32 AENETFETVDPVTQAplakiargksvDIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGK 111
Cdd:PRK09406 9 ATGETVKTFTALTDD-----------EVDAAIARAHARFR--DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 112 PIRhSLRDDIPGAARAIRWYAEAIDKVYGEV---ATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSV 188
Cdd:PRK09406 76 TLA-SAKAEALKCAKGFRYYAEHAEALLADEpadAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 189 ILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTgFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSnMKRVWLEA 268
Cdd:PRK09406 155 LLKHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 269 GGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCA 348
Cdd:PRK09406 233 GGSDPFIVMPSA-DLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 349 HADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLG 426
Cdd:PRK09406 312 GRDEVEKQVDDAVAAGATILCGgkRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129261 427 AAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
Cdd:PRK09406 392 SNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
7-472 |
2.66e-80 |
|
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: 259.05 E-value: 2.66e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 7 AYWQDKALSLAIENRL----FINGEytAAAENETFETVDPV-TQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPA 81
Cdd:cd07125 16 LEALADALKAFDEKEWeaipIINGE--ETETGEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAG--WSATPVE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 82 KRKAVLNKLADLMEAHAEELALLETLDTGKpirhSLRDDIPGAARAI---RWYAEAIDKVYGEVATTSSH-ELAMIVREP 157
Cdd:cd07125 92 ERAEILEKAADLLEANRGELIALAAAEAGK----TLADADAEVREAIdfcRYYAAQARELFSDPELPGPTgELNGLELHG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 158 VGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDI 237
Cdd:cd07125 168 RGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 238 DAIAFTGSTRTGKQLLKdagdsnmkrvWL------------EAGGKSANIVFADCpDLQQAA-----SAtaagiFYNQGQ 300
Cdd:cd07125 248 DGVIFTGSTETAKLINR----------ALaerdgpilpliaETGGKNAMIVDSTA-LPEQAVkdvvqSA-----FGSAGQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 301 VCIAgTRLL-LEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLL----LDGRNAGL 375
Cdd:cd07125 312 RCSA-LRLLyLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIapapLDDGNGYF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 376 AAaigPTIFVDVdpNASLSREEIFGPVLVVTRFTSE--EQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNN 453
Cdd:cd07125 391 VA---PGIIEIV--GIFDLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINR 465
|
490 500
....*....|....*....|....*
gi 16129261 454 yndgDMT---V---PFGGYKQSGNG 472
Cdd:cd07125 466 ----NITgaiVgrqPFGGWGLSGTG 486
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
21-489 |
6.31e-79 |
|
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: 254.42 E-value: 6.31e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEE 100
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFL--TWGQTSLAQRTSVLLRYQALLKEHRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 101 LALLETLDTGKPIRHSLRDdipgAARAIRWYAEAID---KVYGEVATTSSHELAMI-VREPVGVIAAIVPWNFPLLLTCW 176
Cdd:TIGR01722 80 IAELITAEHGKTHSDALGD----VARGLEVVEHACGvnsLLKGETSTQVATRVDVYsIRQPLGVCAGITPFNFPAMIPLW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 177 KLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGkQLLKDA 256
Cdd:TIGR01722 156 MFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIG-RYIHTT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 257 GDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESiADEFLALLKQQAQNWQPGHPLD 336
Cdd:TIGR01722 234 GSAHGKRVQALGGAKNHMVVMPDA-DKDAAADALVGAAYGAAGQRCMAISAAVLVGA-ADEWVPEIRERAEKIRIGPGDD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 337 PATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-----IGPTIFVDVDPNASLSREEIFGPVLVVTRFTS 410
Cdd:TIGR01722 312 PGAEMGPLITPQAKDRVASLIAGGAAEGaEVLLDGRGYKVDGYeegnwVGPTLLERVPPTMKAYQEEIFGPVLCVLEADT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 411 EEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgDMTVP-----FGGYKQSGNGrdkSLHALEK--- 482
Cdd:TIGR01722 392 LEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNV----PIPVPlpyfsFTGWKDSFFG---DHHIYGKqgt 464
|
....*....
gi 16129261 483 --FTELKTI 489
Cdd:TIGR01722 465 hfYTRGKTV 473
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
38-472 |
8.15e-77 |
|
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: 248.10 E-value: 8.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 38 ETVDPVTQAPLAKIARGKSVDIDRAMSAARGVF-ERGDWSlsSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPirhs 116
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNNWL--PAHERIAILERLADLMEERADELALLIAREGGKP---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 117 LRDDIPGAARAI---RWYAEAIDKVYGE-----VATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSV 188
Cdd:cd07148 76 LVDAKVEVTRAIdgvELAADELGQLGGReipmgLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 189 ILKPSEKSPLSAIRLAGLAKEAGLPDG-VLNVVTgfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSNmkRVWLE 267
Cdd:cd07148 156 IVKPALATPLSCLAFVDLLHEAGLPEGwCQAVPC--ENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT--RCALE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 268 AGGkSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDC 347
Cdd:cd07148 232 HGG-AAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 348 AHADSVHSFIREGESKG-QLLLDGRNAGlAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLG 426
Cdd:cd07148 311 REVDRVEEWVNEAVAAGaRLLCGGKRLS-DTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQ 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 16129261 427 AAVWTRDLSRAHRMSRRLKAGSVFVNnyndgDMT------VPFGGYKQSGNG 472
Cdd:cd07148 390 AAVFTKDLDVALKAVRRLDATAVMVN-----DHTafrvdwMPFAGRRQSGYG 436
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
58-473 |
1.01e-76 |
|
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: 247.18 E-value: 1.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 58 DIDRAMSAARGVFerGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAAR---AIRWYAEA 134
Cdd:cd07095 1 QVDAAVAAARAAF--PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKidiSIKAYHER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 135 IdkvyGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPD 214
Cdd:cd07095 79 T----GERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 215 GVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSNMKRVWLEAGGKSANIVFADcPDLQQAASATAAGI 294
Cdd:cd07095 155 GVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDV-ADIDAAAYLIVQSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 295 FYNQGQVCIAGTRLLLEES-IADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGR- 371
Cdd:cd07095 233 FLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGgEPLLAMEr 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 372 -NAGlAAAIGPTIfVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVF 450
Cdd:cd07095 313 lVAG-TAFLSPGI-IDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVN 390
|
410 420
....*....|....*....|....
gi 16129261 451 VNNYNDG-DMTVPFGGYKQSGNGR 473
Cdd:cd07095 391 WNRPTTGaSSTAPFGGVGLSGNHR 414
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
22-489 |
1.54e-75 |
|
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: 245.95 E-value: 1.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 22 LFINGEYTAAAENETfeTVDPV-TQAPLAKIARGKSVDIDRAMSAARGVFerGDWSLSSPAKRKAVLNKLADLMEAHAEE 100
Cdd:cd07083 21 LVIGGEWVDTKERMV--SVSPFaPSEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAADLLRRRRRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 101 LALLETLDTGKPIRHSLrDDIPGAARAIRWYAEAIDKVYG--EVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
Cdd:cd07083 97 LIATLTYEVGKNWVEAI-DDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
Cdd:cd07083 176 VAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAAR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 259 -----SNMKRVWLEAGGKSANIVfADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGH 333
Cdd:cd07083 256 lapgqTWFKRLYVETGGKNAIIV-DETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 334 PLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDG-RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEE 412
Cdd:cd07083 335 PEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGkRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 413 --QALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPFGGYKQSG-NGRDKSLHALEKFTELK 487
Cdd:cd07083 415 faEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVgvQPFGGFKLSGtNAKTGGPHYLRRFLEMK 494
|
..
gi 16129261 488 TI 489
Cdd:cd07083 495 AV 496
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
22-473 |
1.61e-72 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 237.93 E-value: 1.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 22 LFINGEYtAAAENETFETVDPVTQAPlakIARGKSV---DIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHA 98
Cdd:PRK09457 3 LWINGDW-IAGQGEAFESRNPVSGEV---LWQGNDAtaaQVDAAVRAARAAFP--AWARLSFEERQAIVERFAALLEENK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 99 EELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
Cdd:PRK09457 77 EELAEVIARETGKPLWEA-ATEVTAMINKIAISIQAYHERTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
Cdd:PRK09457 156 VPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 259 SNMKRVWLEAGGKSAnIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESI-ADEFLALLKQQAQNWQPGHPL-D 336
Cdd:PRK09457 235 QPEKILALEMGGNNP-LVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRWDaE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 337 PATTMGTLIDCAHADS-VHSFIREGESKGQLLLDGRNAGLAAA-IGPTIfVDVDPNASLSREEIFGPVLVVTRFTSEEQA 414
Cdd:PRK09457 314 PQPFMGAVISEQAAQGlVAAQAQLLALGGKSLLEMTQLQAGTGlLTPGI-IDVTGVAELPDEEYFGPLLQVVRYDDFDEA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129261 415 LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVfvnNYND----GDMTVPFGGYKQSGNGR 473
Cdd:PRK09457 393 IRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIV---NWNKpltgASSAAPFGGVGASGNHR 452
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
21-495 |
4.58e-63 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 213.08 E-value: 4.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEE 100
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA--WAKTPLWKRAELLHKAAAILKEHKAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 101 LALLETLDTGKPirhsLRDDIPGAARA---IRWYAEAIDKVYGE--------VATTSSHELAMIVREPVGVIAAIVPWNF 169
Cdd:PLN00412 95 IAECLVKEIAKP----AKDAVTEVVRSgdlISYTAEEGVRILGEgkflvsdsFPGNERNKYCLTSKIPLGVVLAIPPFNY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 170 PLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTrTG 249
Cdd:PLN00412 171 PVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD-TG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 250 KQLLKDAGdsnMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNW 329
Cdd:PLN00412 250 IAISKKAG---MVPLQMELGGKDACIVLEDA-DLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 330 QPGHPLDPAtTMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLaaaIGPTIFVDVDPNASLSREEIFGPVLVVTR 407
Cdd:PLN00412 326 TVGPPEDDC-DITPVVSESSANFIEGLVMDAKEKGATFCQEwkREGNL---IWPLLLDNVRPDMRIAWEEPFGPVLPVIR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 408 FTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNY-NDGDMTVPFGGYKQSGNGRDKSLHALEKFTEL 486
Cdd:PLN00412 402 INSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIGSQGITNSINMMTKV 481
|
....*....
gi 16129261 487 KTIWISLEA 495
Cdd:PLN00412 482 KSTVINLPK 490
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
83-489 |
1.45e-62 |
|
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: 209.69 E-value: 1.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 83 RKAVLNKLADLMEAHAEEL--ALLEtlDTGKP--------IrHSLRDDIPGAARAIRWYAEAiDKVYGEVATTSSHelAM 152
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIaaALYA--DLGKPpaeaylteI-AVVLGEIDHALKHLKKWMKP-RRVSVPLLLQPAK--AY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 153 IVREPVGVIAAIVPWNFPLLLTcwkLGP---ALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAgQ 229
Cdd:cd07087 96 VIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVA-T 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 230 ALSRHNdIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLL 309
Cdd:cd07087 171 ALLAEP-FDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDA-NLEVAARRIAWGKFLNAGQTCIAPDYVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 310 LEESIADEFLALLKQQAQNWQPGHPLDpATTMGTLIDCAHADSVHSFIREGE--SKGQLLLDGRnaglaaAIGPTIFVDV 387
Cdd:cd07087 248 VHESIKDELIEELKKAIKEFYGEDPKE-SPDYGRIINERHFDRLASLLDDGKvvIGGQVDKEER------YIAPTILDDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 388 DPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVnnyNDGDM-----TVP 462
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCV---NDVLLhaaipNLP 397
|
410 420
....*....|....*....|....*..
gi 16129261 463 FGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07087 398 FGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
58-489 |
2.12e-60 |
|
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: 204.38 E-value: 2.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 58 DIDRAMSAARGVFERGdwSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDK 137
Cdd:cd07135 6 EIDSIHSRLRATFRSG--KTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 138 -VYGEVATTSSHELAM----IVREPVGVIAAIVPWNFPLLLTcwkLGP---ALAAGNSVILKPSEKSPLSAIRLAGLAKE 209
Cdd:cd07135 84 wAKDEKVKDGPLAFMFgkprIRKEPLGVVLIIGPWNYPVLLA---LSPlvgAIAAGCTVVLKPSELTPHTAALLAELVPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 210 AgLPDGVLNVVTGFGHEAGQALSRHndIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASA 289
Cdd:cd07135 161 Y-LDPDAFQVVQGGVPETTALLEQK--FDKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNA-DLELAAKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 290 TAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPaTTMGTLIDCAHADSVHSFIRegESKGQLLLD 369
Cdd:cd07135 236 ILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANAS-PDYTRIVNPRHFNRLKSLLD--TTKGKVVIG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 370 GRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSV 449
Cdd:cd07135 313 GEMDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGV 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 16129261 450 FVnnyNDGDM-----TVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07135 393 VI---NDTLIhvgvdNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
25-473 |
2.06e-59 |
|
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: 202.82 E-value: 2.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 25 NGEYTAAAEneTFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALL 104
Cdd:cd07130 4 DGEWGGGGG--VVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE--WRDVPAPKRGEIVRQIGDALRKKKEALGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 105 ETLDTGKPIRHSLRD-----DI----PGAARAIrwyaeaidkvYGEVATT--SSHELaMIVREPVGVIAAIVPWNFPLLL 173
Cdd:cd07130 80 VSLEMGKILPEGLGEvqemiDIcdfaVGLSRQL----------YGLTIPSerPGHRM-MEQWNPLGVVGVITAFNFPVAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 174 TCWKLGPALAAGNSVILKPSEKSPLSAIR----LAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTG 249
Cdd:cd07130 149 WGWNAAIALVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 250 KQLLKDAGDsNMKRVWLEAGGKSANIVFaDCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNW 329
Cdd:cd07130 228 RQVGQAVAA-RFGRSLLELGGNNAIIVM-EDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 330 QPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNA--GLAAAIGPTIfVDVDPNASLSREEIFGPVLVVTR 407
Cdd:cd07130 306 RIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVidGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 408 FTSEEQALQLANDSQYGLGAAVWTRDLSRAHR-MSrrlKAGS----VFVNnyndgdmtVP---------FGGYKQSGNGR 473
Cdd:cd07130 385 FDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRwLG---PKGSdcgiVNVN--------IGtsgaeiggaFGGEKETGGGR 453
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
67-473 |
1.47e-58 |
|
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: 199.37 E-value: 1.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 67 RGVFE---RGDWSL--SSPAKRKAVLNKLADLMEAHAEEL--ALLEtlDTGKPIR-------HSLRDDIPGAARAI-RWY 131
Cdd:cd07134 1 RRVFAaqqAHALALraSTAAERIAKLKRLKKAILARREEIiaALAA--DFRKPAAevdlteiLPVLSEINHAIKHLkKWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 132 AEaiDKVYGEVATTSSHelAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAG 211
Cdd:cd07134 79 KP--KRVRTPLLLFGTK--SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 212 LPDGVlNVVTGfGHEAGQALSRHnDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATA 291
Cdd:cd07134 155 DEDEV-AVFEG-DAEVAQALLEL-PFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETA-DLKKAAKKIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 292 AGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQ-AQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDG 370
Cdd:cd07134 230 WGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEiEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 371 rnaGLAAA----IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKA 446
Cdd:cd07134 310 ---GQFDAaqryIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSS 386
|
410 420 430
....*....|....*....|....*....|.
gi 16129261 447 GSVFVNN----YNDGDMtvPFGGYKQSGNGR 473
Cdd:cd07134 387 GGVVVNDvvlhFLNPNL--PFGGVNNSGIGS 415
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
79-473 |
5.50e-56 |
|
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: 192.70 E-value: 5.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 79 SPAKRKAVLNKLADLMEAHAEELA----------------LLETLDTGKPIRHSLRddipgaaRAIRWYAEAidKVYGEV 142
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAeaisadfghrsrhetlLAEILPSIAGIKHARK-------HLKKWMKPS--RRHVGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 143 ATTSSHelAMIVREPVGVIAAIVPWNFPLLLTcwkLGP---ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDgVLNV 219
Cdd:cd07133 89 LFLPAK--AEVEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 220 VTGfGHEAGQALSRHnDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQG 299
Cdd:cd07133 163 VTG-GADVAAAFSSL-PFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDA-DLAKAAERIAFGKLLNAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 300 QVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTmgTLIDCAHADSVHSFIREGESKG----QLLLDGRNAGL 375
Cdd:cd07133 239 QTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNPDYT--SIINERHYARLQGLLEDARAKGarviELNPAGEDFAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 376 AAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVnnyN 455
Cdd:cd07133 317 TRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTI---N 393
|
410 420
....*....|....*....|...
gi 16129261 456 DGDMTV-----PFGGYKQSGNGR 473
Cdd:cd07133 394 DTLLHVaqddlPFGGVGASGMGA 416
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
23-489 |
9.36e-56 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 196.12 E-value: 9.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELA 102
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL--WRNTPITTRQRVMLKFQELIRKNMDKLA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 103 LLETLDTGKPIRHSLRDDIPG-------AARAIRWYAEAIDKVYGEVATTSshelamiVREPVGVIAAIVPWNFPLLLTC 175
Cdd:PLN02419 195 MNITTEQGKTLKDSHGDIFRGlevvehaCGMATLQMGEYLPNVSNGVDTYS-------IREPLGVCAGICPFNFPAMIPL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 176 WKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKD 255
Cdd:PLN02419 268 WMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHG-TNDTVNAICDDEDIRAVSFVGSNTAGMHIYAR 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 256 AGdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESiADEFLALLKQQAQNWQPGHPL 335
Cdd:PLN02419 347 AA-AKGKRIQSNMGAKNHGLVLPDA-NIDATLNALLAAGFGAAGQRCMALSTVVFVGD-AKSWEDKLVERAKALKVTCGS 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 336 DPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-----IGPTIFVDVDPNASLSREEIFGPVLVVTRFT 409
Cdd:PLN02419 424 EPDADLGPVISKQAKERICRLIQSGVDDGaKLLLDGRDIVVPGYekgnfIGPTILSGVTPDMECYKEEIFGPVLVCMQAN 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 410 SEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgDMTVPFGGYKQSGN----GRDKSLH---ALEK 482
Cdd:PLN02419 504 SFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV----PIPVPLPFFSFTGNkasfAGDLNFYgkaGVDF 579
|
....*..
gi 16129261 483 FTELKTI 489
Cdd:PLN02419 580 FTQIKLV 586
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
58-472 |
1.55e-54 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 197.34 E-value: 1.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 58 DIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLrDDIPGAARAIRWYA-EAID 136
Cdd:PRK11904 586 QVEQALAAARAAFPA--WSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAI-AEVREAVDFCRYYAaQARR 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 137 KVYGEVA----TTSSHELAMivrEPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGL 212
Cdd:PRK11904 663 LFGAPEKlpgpTGESNELRL---HGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGI 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 213 PDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGK---QLL--KDAgdsnmKRVWL--EAGGKSANIVfaDCPDL-Q 284
Cdd:PRK11904 740 PKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARiinRTLaaRDG-----PIVPLiaETGGQNAMIV--DSTALpE 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 285 QAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG 364
Cdd:PRK11904 813 QVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREA 892
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 365 QLLLDGRNAGLAAA---IGPTIFvDVDpNASLSREEIFGPVLVVTRFTSEE--QALQLANDSQYGLGAAVWTRDLSRAHR 439
Cdd:PRK11904 893 RLLAQLPLPAGTENghfVAPTAF-EID-SISQLEREVFGPILHVIRYKASDldKVIDAINATGYGLTLGIHSRIEETADR 970
|
410 420 430
....*....|....*....|....*....|....*....
gi 16129261 440 MSRRLKAGSVFVNNyndgDMT---V---PFGGYKQSGNG 472
Cdd:PRK11904 971 IADRVRVGNVYVNR----NQIgavVgvqPFGGQGLSGTG 1005
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
59-487 |
2.91e-54 |
|
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: 189.74 E-value: 2.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 59 IDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLrDDIPGAARAIRWYAEAIDKV 138
Cdd:TIGR01238 76 VQAAIDSAQQAFP--TWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAI-AEVREAVDFCRYYAKQVRDV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 139 YGEVATtsshelamivrEPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLN 218
Cdd:TIGR01238 153 LGEFSV-----------ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 219 VVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSNMKRVWL--EAGGKSANIVfaDCPDL-QQAASATAAGIF 295
Cdd:TIGR01238 222 LLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIV--DSTALpEQVVRDVLRSAF 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 296 YNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG----QLLLDGR 371
Cdd:TIGR01238 300 DSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkkiaQLTLDDS 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 372 NAGLAAAIGPTIFVDVDPNASLSReEIFGPVLVVTRFTSEE--QALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSV 449
Cdd:TIGR01238 380 RACQHGTFVAPTLFELDDIAELSE-EVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNC 458
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 16129261 450 FVNNYNDGDM--TVPFGGYKQSGNG-RDKSLHALEKFTELK 487
Cdd:TIGR01238 459 YVNRNQVGAVvgVQPFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
153-487 |
4.76e-52 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 183.69 E-value: 4.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 153 IVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGfGHEAGQALS 232
Cdd:PTZ00381 105 IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 233 RHNdIDAIAFTGSTRTGKqLLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEE 312
Cdd:PTZ00381 183 KEP-FDHIFFTGSPRVGK-LVMQAAAENLTPCTLELGGKSPVIVDKSC-NLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 313 SIADEFLALLKQQAQNWQPGHPLDpATTMGTLIDCAHADSVHSFIRegESKGQLLLDGrNAGLAAA-IGPTIFVDVDPNA 391
Cdd:PTZ00381 260 SIKDKFIEALKEAIKEFFGEDPKK-SEDYSRIVNEFHTKRLAELIK--DHGGKVVYGG-EVDIENKyVAPTIIVNPDLDS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 392 SLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNN--YNDGDMTVPFGGYKQS 469
Cdd:PTZ00381 336 PLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDcvFHLLNPNLPFGGVGNS 415
|
330
....*....|....*...
gi 16129261 470 GNGRDKSLHALEKFTELK 487
Cdd:PTZ00381 416 GMGAYHGKYGFDTFSHPK 433
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
58-472 |
5.66e-51 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 187.07 E-value: 5.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 58 DIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKpirhSLRDDIpgaarA-IRwyaEAID 136
Cdd:COG4230 594 DVEAALAAAQAAFPA--WSATPVEERAAILERAADLLEAHRAELMALLVREAGK----TLPDAI-----AeVR---EAVD 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 137 --KVYGEVATTssHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPD 214
Cdd:COG4230 660 fcRYYAAQARR--LFAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPA 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 215 GVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGK----QLLKDAGDSnmkrVWL--EAGGKSANIVfadcpD----LQ 284
Cdd:COG4230 738 DVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARlinrTLAARDGPI----VPLiaETGGQNAMIV-----DssalPE 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 285 QA-----ASAtaagiFYNQGQVCIAgTRLL-LEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLID-------CAHad 351
Cdd:COG4230 809 QVvddvlASA-----FDSAGQRCSA-LRVLcVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDaearanlEAH-- 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 352 svhsfIREGESKGQLLLDGRNAGLAAA---IGPTIF-VDvdpnaSLSR--EEIFGPVLVVTRFTSEE--QALQLANDSQY 423
Cdd:COG4230 881 -----IERMRAEGRLVHQLPLPEECANgtfVAPTLIeID-----SISDleREVFGPVLHVVRYKADEldKVIDAINATGY 950
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 16129261 424 GLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgDMT---V---PFGGYKQSGNG 472
Cdd:COG4230 951 GLTLGVHSRIDETIDRVAARARVGNVYVNR----NIIgavVgvqPFGGEGLSGTG 1001
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
58-472 |
8.04e-49 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 180.83 E-value: 8.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 58 DIDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKpirhSLRDDIPGAARAI---RWYAEA 134
Cdd:PRK11905 591 DVERALAAAQAAFP--EWSATPAAERAAILERAADLMEAHMPELFALAVREAGK----TLANAIAEVREAVdflRYYAAQ 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 135 IDkvygevattssHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPD 214
Cdd:PRK11905 665 AR-----------RLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPK 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 215 GVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTG----KQLLKDAGDSnmkrVWL--EAGGKSANIVfaDCPDL-QQAA 287
Cdd:PRK11905 734 DALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVArliqRTLAKRSGPP----VPLiaETGGQNAMIV--DSSALpEQVV 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 288 SATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLL 367
Cdd:PRK11905 808 ADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV 887
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 368 ldgRNAGLAAA------IGPTIFvDVDPNASLSReEIFGPVLVVTRFTSEE--QALQLANDSQYGLGAAVWTRDLSRAHR 439
Cdd:PRK11905 888 ---HQLPLPAEtekgtfVAPTLI-EIDSISDLER-EVFGPVLHVVRFKADEldRVIDDINATGYGLTFGLHSRIDETIAH 962
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 16129261 440 MSRRLKAGSVFVN-NyndgdmTV-------PFGGYKQSGNG 472
Cdd:PRK11905 963 VTSRIRAGNIYVNrN------IIgavvgvqPFGGEGLSGTG 997
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
83-489 |
2.01e-48 |
|
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: 172.69 E-value: 2.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 83 RKAVLNKLADLMEAHAEELalLETL--DTGKPIRHSlrddipgaarairwYAEAIDKVYGE----------------VAT 144
Cdd:cd07136 22 RIEQLKKLKQAIKKYENEI--LEALkkDLGKSEFEA--------------YMTEIGFVLSEinyaikhlkkwmkpkrVKT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 145 TSSHELA--MIVREPVGVIAAIVPWNFPLLLTcwkLGP---ALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNV 219
Cdd:cd07136 86 PLLNFPSksYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 220 VTGfGHEAGQALSrHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQG 299
Cdd:cd07136 162 VEG-GVEENQELL-DQKFDYIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDA-NLKLAAKRIVWGKFLNAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 300 QVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDpATTMGTLIDCAHADSVHSFIREGEskgqLLLDGRNAGLAAAI 379
Cdd:cd07136 238 QTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLE-SPDYGRIINEKHFDRLAGLLDNGK----IVFGGNTDRETLYI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 380 GPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgdm 459
Cdd:cd07136 313 EPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIND------ 386
|
410 420 430
....*....|....*....|....*....|....*...
gi 16129261 460 TV--------PFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07136 387 TImhlanpylPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
15-489 |
1.76e-45 |
|
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: 166.61 E-value: 1.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 15 SLAIENRLFINGEytaaaENETFETVDPVT----QAPLAKIARGKSVDIDRAMSAARGVfeRGDWSLSSPAKRKAVLNKL 90
Cdd:cd07123 28 SLTVEIPLVIGGK-----EVRTGNTGKQVMphdhAHVLATYHYADAALVEKAIEAALEA--RKEWARMPFEDRAAIFLKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 91 ADLMEAHAEELALLET-LDTGKPIRHSlrdDIPGAARAI---RWYAEAIDKVYGE--VATTSSHELAMIVREPVGVIAAI 164
Cdd:cd07123 101 ADLLSGKYRYELNAATmLGQGKNVWQA---EIDAACELIdflRFNVKYAEELYAQqpLSSPAGVWNRLEYRPLEGFVYAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 165 VPWNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTG 244
Cdd:cd07123 178 SPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 245 STRTGKQLLKDAGDS-----NMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFL 319
Cdd:cd07123 257 STPTFKSLWKQIGENldryrTYPRIVGETGGKNFHLVHPSA-DVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 320 ALLKQQAQNWQPGHPLDPATTMGTLID------------CAHADSVHSFIREGE---SKGQLlldgrnaglaaaIGPTIF 384
Cdd:cd07123 336 ERLLEELKEIKMGDPDDFSNFMGAVIDekafdrikgyidHAKSDPEAEIIAGGKcddSVGYF------------VEPTVI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 385 VDVDPNASLSREEIFGPVLVVTRFTSE--EQALQLAND-SQYGLGAAVWTRD------LSRAHRMSrrlkAGSVFVNNYN 455
Cdd:cd07123 404 ETTDPKHKLMTEEIFGPVLTVYVYPDSdfEETLELVDTtSPYALTGAIFAQDrkaireATDALRNA----AGNFYINDKP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 16129261 456 DGdmTV----PFGGYKQSG-NgrDK--SLHALEKFTELKTI 489
Cdd:cd07123 480 TG--AVvgqqPFGGARASGtN--DKagSPLNLLRWVSPRTI 516
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
62-487 |
5.76e-43 |
|
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: 157.77 E-value: 5.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 62 AMSAARGVFERGDwslSSPAK-RKAVLNKLADLMEAHAEELalLETL--DTGKPIRHSLRDDIPGAARAIRwyaEAIDKV 138
Cdd:cd07132 3 AVRRAREAFSSGK---TRPLEfRIQQLEALLRMLEENEDEI--VEALakDLRKPKFEAVLSEILLVKNEIK---YAISNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 139 YG-----EVATTSSHEL--AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLakeag 211
Cdd:cd07132 75 PEwmkpePVKKNLATLLddVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 212 LPDGVLN----VVTGFGHEAGQALSrhNDIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSANIVFADCpDLQQAA 287
Cdd:cd07132 150 IPKYLDKecypVVLGGVEETTELLK--QRFDYIFYTGSTSVGKIVMQ-AAAKHLTPVTLELGGKSPCYVDKSC-DIDVAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 288 SATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPAtTMGTLIDCAHADSVHSFIregeSKGQLL 367
Cdd:cd07132 226 RRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESP-DYGRIINDRHFQRLKKLL----SGGKVA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 368 LDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAG 447
Cdd:cd07132 301 IGGQTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSG 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 16129261 448 SVFVnnyNDGDM-----TVPFGGYKQSGNGRDKSLHALEKFTELK 487
Cdd:cd07132 381 GVCV---NDTIMhytldSLPFGGVGNSGMGAYHGKYSFDTFSHKR 422
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
83-489 |
3.91e-42 |
|
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: 155.26 E-value: 3.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 83 RKAVLNKLADLMEAHaeELALLETL--DTGKPIRHSLRDDIPGAARAI--------RWYAEaiDKVYGEVATTSSHelAM 152
Cdd:cd07137 23 RKSQLKGLLRLVDEN--EDDIFAALrqDLGKPSAESFRDEVSVLVSSCklaikelkKWMAP--EKVKTPLTTFPAK--AE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 153 IVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGfGHEAGQALS 232
Cdd:cd07137 97 IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 233 RHNdIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIF-YNQGQVCIAGTRLLLE 311
Cdd:cd07137 175 EQK-WDKIFFTGSPRVGRIIMA-AAAKHLTPVTLELGGKCPVIVDSTV-DLKVAVRRIAGGKWgCNNGQACIAPDYVLVE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 312 ESIADEFLALLKQQAQNWQPGHPLDPAtTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAAIGPTIFVDVDPNA 391
Cdd:cd07137 252 ESFAPTLIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLYIEPTILLDPPLDS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 392 SLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNN-----YNDgdmTVPFGGY 466
Cdd:cd07137 331 SIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDtvvqyAID---TLPFGGV 407
|
410 420
....*....|....*....|...
gi 16129261 467 KQSGNGRDKSLHALEKFTELKTI 489
Cdd:cd07137 408 GESGFGAYHGKFSFDAFSHKKAV 430
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
58-472 |
6.79e-40 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 154.36 E-value: 6.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 58 DIDRAMSAArgVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKpirhslrdDIPGAARAIRwyaEAIDK 137
Cdd:PRK11809 683 EVEQALESA--VNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGK--------TFSNAIAEVR---EAVDF 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 138 VY---GEVATTSSHElamiVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPD 214
Cdd:PRK11809 750 LRyyaGQVRDDFDND----THRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPA 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 215 GVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKD-AG--DSNMKRVWL--EAGGKSANIVfaDCPDL-QQAAS 288
Cdd:PRK11809 826 GVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNlAGrlDPQGRPIPLiaETGGQNAMIV--DSSALtEQVVA 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 289 ATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLL 368
Cdd:PRK11809 904 DVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVF 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 369 D-GRNAGLAAAIG----PTIfVDVDPNASLSReEIFGPVLVVTRFTSEE--QALQLANDSQYGLGAAVWTR-DLSRAHrM 440
Cdd:PRK11809 984 QaARENSEDWQSGtfvpPTL-IELDSFDELKR-EVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTRiDETIAQ-V 1060
|
410 420 430
....*....|....*....|....*....|....
gi 16129261 441 SRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNG 472
Cdd:PRK11809 1061 TGSAHVGNLYVNRNMVGAVvgVQPFGGEGLSGTG 1094
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
23-474 |
4.15e-39 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 148.44 E-value: 4.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 23 FINGEYTAAAENETfeTVDPVTQAPLAKIARGKSVDIDRAMSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
Cdd:PLN02315 24 YVGGEWRANGPLVS--SVNPANNQPIAEVVEASLEDYEEGLRACEEA--AKIWMQVPAPKRGEIVRQIGDALRAKLDYLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 103 LLETLDTGKPIrhslrddipgaARAIRWYAEAID----------KVYGEVATTSSHELAMI-VREPVGVIAAIVPWNFPL 171
Cdd:PLN02315 100 RLVSLEMGKIL-----------AEGIGEVQEIIDmcdfavglsrQLNGSIIPSERPNHMMMeVWNPLGIVGVITAFNFPC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 172 LLTCWKLGPALAAGNSVILKPSEKSPLSAIRL----AGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTR 247
Cdd:PLN02315 169 AVLGWNACIALVCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 248 TGkQLLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQ 327
Cdd:PLN02315 248 VG-LMVQQTVNARFGKCLLELSGNNAIIVMDDA-DIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 328 NWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNA--GLAAAIGPTIfVDVDPNASLSREEIFGPVLVV 405
Cdd:PLN02315 326 QVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAieSEGNFVQPTI-VEISPDADVVKEELFGPVLYV 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129261 406 TRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKA--GSVFVN-NYNDGDMTVPFGGYKQSGNGRD 474
Cdd:PLN02315 405 MKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVNiPTNGAEIGGAFGGEKATGGGRE 476
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
61-472 |
1.21e-35 |
|
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: 137.75 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 61 RAMSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRhsLRDDIPGAARAIRWYAEAID--KV 138
Cdd:cd07084 3 RALLAADIS--TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWM--FAENICGDQVQLRARAFVIYsyRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 139 YGEVATTSSHELAM---IVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAG-LPD 214
Cdd:cd07084 79 PHEPGNHLGQGLKQqshGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 215 GVLNVVTGFGHeAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSnmkRVWLEAGGKSANIVFADCPDLQQAASATAAGI 294
Cdd:cd07084 159 EDVTLINGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA---RIYLELAGFNWKVLGPDAQAVDYVAWQCVQDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 295 FYNQGQVCIAGTRLLLEESIADE-FLALLKQQAQNWQPGHP-LDPATTMGTLIDCAHADSvHSFIREGESKGQLLLDGRN 372
Cdd:cd07084 235 TACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLEDLlLGPVQTFTTLAMIAHMEN-LLGSVLLFSGKELKNHSIP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 373 AGLAAAIGPTIFVDVDPNAS---LSREEIFGPVLVVT--RFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRL-KA 446
Cdd:cd07084 314 SIYGACVASALFVPIDEILKtyeLVTEEIFGPFAIVVeyKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLwVA 393
|
410 420
....*....|....*....|....*....
gi 16129261 447 GSVFVNNYNDGD---MTVPFGGYKQSGNG 472
Cdd:cd07084 394 GRTYAILRGRTGvapNQNHGGGPAADPRG 422
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
67-489 |
7.29e-35 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 136.39 E-value: 7.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 67 RGVFERGdwSLSSPAKRKAVLNKLADLMEAHAEEL--ALLEtlDTGKPIRHSLRDDIPGAARAIRWYAEAIDK----VYG 140
Cdd:PLN02203 16 RETYESG--RTRSLEWRKSQLKGLLRLLKDNEEAIfkALHQ--DLGKHRVEAYRDEVGVLTKSANLALSNLKKwmapKKA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 141 EVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAirlAGLAKEAG--LPDGVLN 218
Cdd:PLN02203 92 KLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS---AFLAANIPkyLDSKAVK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 219 VVTGfGHEAGQALSRHNdIDAIAFTGSTRTGKqLLKDAGDSNMKRVWLEAGGKSANIV--FADCPDLQQAASATAAGIFY 296
Cdd:PLN02203 169 VIEG-GPAVGEQLLQHK-WDKIFFTGSPRVGR-IIMTAAAKHLTPVALELGGKCPCIVdsLSSSRDTKVAVNRIVGGKWG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 297 N-QGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPAtTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGL 375
Cdd:PLN02203 246 ScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 376 AAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVfvnNYN 455
Cdd:PLN02203 325 KLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV---TFN 401
|
410 420 430
....*....|....*....|....*....|....*....
gi 16129261 456 D-----GDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:PLN02203 402 DaiiqyACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
68-489 |
8.24e-35 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 136.33 E-value: 8.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 68 GVFERGDWSLSSpakrkavLNKLADLMEAHAEELALLETLDTGKPIRHS-------LRDDIPGAARAIR-WYAEAIDKVy 139
Cdd:PLN02174 26 GVTRGYEWRVTQ-------LKKLMIICDNHEPEIVAALRDDLGKPELESsvyevslLRNSIKLALKQLKnWMAPEKAKT- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 140 gevATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAkEAGLPDGVLNV 219
Cdd:PLN02174 98 ---SLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 220 VTGFGHEAGQALSRhnDIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIF-YNQ 298
Cdd:PLN02174 174 VEGAVTETTALLEQ--KWDKIFYTGSSKIGRVIMA-AAAKHLTPVVLELGGKSPVVVDSDT-DLKVTVRRIIAGKWgCNN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 299 GQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDpATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAA 378
Cdd:PLN02174 250 GQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 379 IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNN--YND 456
Cdd:PLN02174 329 IAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDiaVHL 408
|
410 420 430
....*....|....*....|....*....|...
gi 16129261 457 GDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
Cdd:PLN02174 409 ALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
59-452 |
1.39e-32 |
|
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: 129.20 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 59 IDRAMSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRH----------SLRddipGAARAI 128
Cdd:cd07129 1 VDAAAAAAAAAFE--SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARlqgelgrttgQLR----LFADLV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 129 R---WYAEAIDKVYGEVATTSSHELAMiVREPVGVIAAIVPWNFPLLLTCwkLG----PALAAGNSVILKPSEKSPLSAI 201
Cdd:cd07129 75 RegsWLDARIDPADPDRQPLPRPDLRR-MLVPLGPVAVFGASNFPLAFSV--AGgdtaSALAAGCPVVVKAHPAHPGTSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 202 RLAGLA----KEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKqLLKDAGDsnmKR-----VWLEAGgkS 272
Cdd:cd07129 152 LVARAIraalRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGR-ALFDAAA---ARpepipFYAELG--S 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 273 ANIVFADCPDLQQAASATAAG----IFYNQGQVCIA-GTRLLLEESIADEFLALLKQQAQNWQPGHPLDPAttmgtlIDC 347
Cdd:cd07129 226 VNPVFILPGALAERGEAIAQGfvgsLTLGAGQFCTNpGLVLVPAGPAGDAFIAALAEALAAAPAQTMLTPG------IAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 348 AHADSVHSfiREGESKGQLLLDGRNAGLAAAIGPTIFVdVDPNASLS----REEIFGPVLVVTRFTSEEQALQLANDSQY 423
Cdd:cd07129 300 AYRQGVEA--LAAAPGVRVLAGGAAAEGGNQAAPTLFK-VDAAAFLAdpalQEEVFGPASLVVRYDDAAELLAVAEALEG 376
|
410 420 430
....*....|....*....|....*....|...
gi 16129261 424 GLGAAVW--TRDLSRAHRMSRRL--KAGSVFVN 452
Cdd:cd07129 377 QLTATIHgeEDDLALARELLPVLerKAGRLLFN 409
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
40-433 |
1.56e-27 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 115.57 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 40 VDPVTQAPLAKIArGKSVDIDRAMSAARgvfERGDWSLS--SPAKRKAVLNKLADLMEAHAEELALLETLDTGKpIRHSL 117
Cdd:PRK11903 24 FDPVTGEELVRVS-ATGLDLAAAFAFAR---EQGGAALRalTYAQRAALLAAIVKVLQANRDAYYDIATANSGT-TRNDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 118 RDDIPGAARAIRWYAEAIDKVyGEVATTSSHELAMIVREPV-----------GVIAAIVPWNFPLLLTCWKLGPALAAGN 186
Cdd:PRK11903 99 AVDIDGGIFTLGYYAKLGAAL-GDARLLRDGEAVQLGKDPAfqgqhvlvptrGVALFINAFNFPAWGLWEKAAPALLAGV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 187 SVILKPSEKSPLSAIRLAGLAKEAG-LPDGVLNVVTGfghEAGQALSRHNDIDAIAFTGSTRTGKQL-LKDAGDSNMKRV 264
Cdd:PRK11903 178 PVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG---SSAGLLDHLQPFDVVSFTGSAETAAVLrSHPAVVQRSVRV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 265 WLEAGGKSANIVfadCPDlqQAASATAAGIFYNQ---------GQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL 335
Cdd:PRK11903 255 NVEADSLNSALL---GPD--AAPGSEAFDLFVKEvvremtvksGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 336 DPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRN-------AGLAAAIGPTIFVDVDPNAS--LSREEIFGPVLVVT 406
Cdd:PRK11903 330 NDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGfalvdadPAVAACVGPTLLGASDPDAAtaVHDVEVFGPVATLL 409
|
410 420
....*....|....*....|....*..
gi 16129261 407 RFTSEEQALQLANDSQYGLGAAVWTRD 433
Cdd:PRK11903 410 PYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
58-453 |
3.27e-19 |
|
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: 89.60 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 58 DIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTG------KPIRHSLrddipgaarairwy 131
Cdd:cd07121 5 TVDDAVAAAKAAQKQ--YRKCTLADREKIIEAIREALLSNAEELAEMAVEETGmgrvedKIAKNHL-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 132 aeAIDKVYGE-----VATTSSHELAMIVREPVGVIAAIVPWNFPL-LLTCWKLGpALAAGNSVILKP---SEKSPLSAIR 202
Cdd:cd07121 69 --AAEKTPGTedlttTAWSGDNGLTLVEYAPFGVIGAITPSTNPTeTIINNSIS-MLAAGNAVVFNPhpgAKKVSAYAVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 203 LAGLA-KEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKdAGdsnmKRVwLEAGGKSANIVFADCP 281
Cdd:cd07121 146 LINKAiAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALS-SG----KKA-IGAGAGNPPVVVDETA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 282 DLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAqnwqpGHPLDPATTMGTLIDCAHADSVHSFIREge 361
Cdd:cd07121 220 DIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQRNG-----AYVLNDEQAEQLLEVVLLTNKGATPNKK-- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 362 skgqllLDGRNAG-LAAAIGPT-------IFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGL--GAAVWT 431
Cdd:cd07121 293 ------WVGKDASkILKAAGIEvpadirlIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHS 366
|
410 420
....*....|....*....|..
gi 16129261 432 RDLSRAHRMSRRLKAgSVFVNN 453
Cdd:cd07121 367 KNVENLTKMARAMQT-TIFVKN 387
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
58-453 |
1.59e-18 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 88.04 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 58 DIDRAMSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTG------KPIRHSLrddipgaarairwy 131
Cdd:PRK15398 37 SVDDAVAAAKVAQQR--YQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmgrvedKIAKNVA-------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 132 aeAIDKVYG-----EVATTSSHELAMIVREPVGVIAAIVPWNFPL-LLTCWKLGpALAAGNSVILKP---SEKSPLSAIR 202
Cdd:PRK15398 101 --AAEKTPGvedltTEALTGDNGLTLIEYAPFGVIGAVTPSTNPTeTIINNAIS-MLAAGNSVVFSPhpgAKKVSLRAIE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 203 -LAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKdagdSNmKRVwLEAGGKSANIVFADCP 281
Cdd:PRK15398 178 lLNEAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMK----SG-KKA-IGAGAGNPPVVVDETA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 282 DLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAqnwqpGHPLDPAtTMGTLIDCAHADSVH---SFIr 358
Cdd:PRK15398 252 DIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEKNG-----AVLLTAE-QAEKLQKVVLKNGGTvnkKWV- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 359 eGESKGQLLldgRNAGLAAAIGPT-IFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGL--GAAVWTRDLS 435
Cdd:PRK15398 325 -GKDAAKIL---EAAGINVPKDTRlLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRNVD 400
|
410
....*....|....*...
gi 16129261 436 RAHRMSRRLKAgSVFVNN 453
Cdd:PRK15398 401 NLNKMARAIQT-SIFVKN 417
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
23-433 |
1.35e-16 |
|
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: 82.32 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 23 FINGEYTAAAEnETFETVDPVTQAPLAKIaRGKSVDIDRAMSAARgvfERGDWSLS--SPAKRKAVLNKLADLMEAHAEE 100
Cdd:cd07128 4 YVAGQWHAGTG-DGRTLHDAVTGEVVARV-SSEGLDFAAAVAYAR---EKGGPALRalTFHERAAMLKALAKYLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 101 LALLETLDTGkpirhSLRD---DIPGAARAIRWYA-----EAIDK---VYGEVATTS-------SHelamIVREPVGVIA 162
Cdd:cd07128 79 LYALSAATGA-----TRRDswiDIDGGIGTLFAYAslgrrELPNAhflVEGDVEPLSkdgtfvgQH----ILTPRRGVAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 163 AIVPWNFPllltCW----KLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAG-LPDGVLNVVTGfghEAGQALSRHNDI 237
Cdd:cd07128 150 HINAFNFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG---SVGDLLDHLGEQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 238 DAIAFTGSTRTGKQL-LKDAGDSNMKRVWLEAGGKSANIVfadCPDLQQAASATAAgiFYNQ---------GQVCIAGTR 307
Cdd:cd07128 223 DVVAFTGSAATAAKLrAHPNIVARSIRFNAEADSLNAAIL---GPDATPGTPEFDL--FVKEvaremtvkaGQKCTAIRR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 308 LLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIrEGESKGQLLLDGRNAGLAAAIG------- 380
Cdd:cd07128 298 AFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPDRFEVVGAdaekgaf 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129261 381 --PTIFV--DVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRD 433
Cdd:cd07128 377 fpPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
79-325 |
1.97e-15 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 78.03 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 79 SPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRhslRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELA------- 151
Cdd:cd07077 14 HDEQRDLIINAIANALYDTRQRLASEAVSERGAYIR---SLIANWIAMMGCSESKLYKNIDTERGITASVGHIqdvllpd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 152 ----MIVREPVGVIAAIVPWNFPLLLTcWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGH-- 225
Cdd:cd07077 91 ngetYVRAFPIGVTMHILPSTNPLSGI-TSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILVLYVPHps 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 226 -EAGQALSRHNDIDAIAFTGstrtGKQLLKDA-GDSNMKRVWLEAGGKSANIVfaDCPDLQQAASATAAGIFYNQGQVCI 303
Cdd:cd07077 170 dELAEELLSHPKIDLIVATG----GRDAVDAAvKHSPHIPVIGFGAGNSPVVV--DETADEERASGSVHDSKFFDQNACA 243
|
250 260
....*....|....*....|..
gi 16129261 304 AGTRLLLEESIADEFLALLKQQ 325
Cdd:cd07077 244 SEQNLYVVDDVLDPLYEEFKLK 265
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
59-452 |
7.12e-15 |
|
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: 76.54 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 59 IDRAMSAARgVFERGdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIrwYAEAIDKV 138
Cdd:cd07081 1 LDDAVAAAK-VAQQG-LSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYI--YNVYKDEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 139 YGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGL----AKEAGLPD 214
Cdd:cd07081 77 TCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLllqaAVAAGAPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 215 GVLNVVTGFGHEAGQALSRHNDIDAIAFTGstrtGKQLLKdAGDSNMKRVwLEAGGKSANIVFADCPDLQQAASATAAGI 294
Cdd:cd07081 157 NLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVK-AAYSSGKPA-IGVGAGNTPVVIDETADIKRAVQSIVKSK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 295 FYNQGQVCIAGTRLLLEESIADEFLALLKQQAqnwqpghpldpattmGTLIDCAHADSVHSFI-REGESKGQLLldGRNA 373
Cdd:cd07081 231 TFDNGVICASEQSVIVVDSVYDEVMRLFEGQG---------------AYKLTAEELQQVQPVIlKNGDVNRDIV--GQDA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 374 G-LAAAIGPTI-------FVDVdpnASLSREEIFG-----PVLVVTRF----TSEEQALQLANDSQYGLGAAVWTRDLS- 435
Cdd:cd07081 294 YkIAAAAGLKVpqetrilIGEV---TSLAEHEPFAheklsPVLAMYRAanfaDADAKALALKLEGGCGHTSAMYSDNIKa 370
|
410
....*....|....*....
gi 16129261 436 --RAHRMSRRLKAGSVFVN 452
Cdd:cd07081 371 ieNMNQFANAMKTSRFVKN 389
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
156-452 |
8.57e-15 |
|
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: 76.38 E-value: 8.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 156 EPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGL----AKEAGLPDGVLNVVTGFGHEAGQAL 231
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKImreaAVAAGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 232 SRHNDIDAIAFTGstrtGKQLLKDAGDSnmkrvwleagGKSA------N---IVFADCpDLQQAASATAAGIFYNQGQVC 302
Cdd:cd07122 174 MKHPDVDLILATG----GPGMVKAAYSS----------GKPAigvgpgNvpaYIDETA-DIKRAVKDIILSKTFDNGTIC 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 303 IAGTRLLLEESIADEFLALLKQQ--------------AQNWQPGHPLDPATTmgtlidcahadsvhsfireGESKGQLll 368
Cdd:cd07122 239 ASEQSVIVDDEIYDEVRAELKRRgayflneeekekleKALFDDGGTLNPDIV-------------------GKSAQKI-- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 369 dGRNAGLAAAIGPTIFV----DVDPNASLSREEIFgPVLVVTRFTSEEQALQLANDSQ--YGLG--AAVWTRDLSRAHRM 440
Cdd:cd07122 298 -AELAGIEVPEDTKVLVaeetGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKARELLeyGGAGhtAVIHSNDEEVIEEF 375
|
330
....*....|..
gi 16129261 441 SRRLKAGSVFVN 452
Cdd:cd07122 376 ALRMPVSRILVN 387
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
23-417 |
1.72e-11 |
|
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: 66.37 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 23 FINGEYTAAAENETFetVDPVTQAPLAKIARGKSVDIDRAMSAARGVFERGdwsLSSPAKRKAVLNKLADLMEAHAEELA 102
Cdd:cd07126 2 LVAGKWKGASNYTTL--LDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSG---LHNPLKNPERYLLYGDVSHRVAHELR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 103 LLETLDT-GKPI-RHSLRDDIPGAARA--------------IRWYAEAIDkVYGEVATTSSHELamivREPVGVIAAIVP 166
Cdd:cd07126 77 KPEVEDFfARLIqRVAPKSDAQALGEVvvtrkflenfagdqVRFLARSFN-VPGDHQGQQSSGY----RWPYGPVAIITP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 167 WNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNdIDAIAFTGST 246
Cdd:cd07126 152 FNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEAN-PRMTLFTGSS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 247 RTGKQLLKDagdsnMK-RVWLEAGGKSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADE-FLALLKQ 324
Cdd:cd07126 231 KVAERLALE-----LHgKVKLEDAGFDWKILGPDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQAgILDKLKA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 325 QAQNWQPGH-PLDPATTMGTLIDCAHADSVHSFirEG---ESKGQLLLDGRNAGLAAAIGPT-IFV-----DVDPNASLS 394
Cdd:cd07126 306 LAEQRKLEDlTIGPVLTWTTERILDHVDKLLAI--PGakvLFGGKPLTNHSIPSIYGAYEPTaVFVpleeiAIEENFELV 383
|
410 420
....*....|....*....|...
gi 16129261 395 REEIFGPVLVVTRFTSEEQALQL 417
Cdd:cd07126 384 TTEVFGPFQVVTEYKDEQLPLVL 406
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
164-452 |
3.69e-10 |
|
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: 62.11 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 164 IVPWNFPLLLTC-----WKLGPA----LAAGNSVILKPSEKSPLSAIRLAGLAK----EAGL-PDGVLNVVTGFGHEAGQ 229
Cdd:cd07127 191 VVPRGVALVIGCstfptWNGYPGlfasLATGNPVIVKPHPAAILPLAITVQVARevlaEAGFdPNLVTLAADTPEEPIAQ 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 230 ALSRHNDIDAIAFTGSTRTGKQLLKDAGDsnmKRVWLEAGGKSaNIVFADCPDLQQAASATAAGIFYNQGQVCIA----- 304
Cdd:cd07127 271 TLATRPEVRIIDFTGSNAFGDWLEANARQ---AQVYTEKAGVN-TVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTpqniy 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 305 ----GTRLLLEESIADEFLALLKQQAQnwqpGHPLDPATTMGtLIDCAHADSVHSFIREGESKGQLLLDGR---NAGLAA 377
Cdd:cd07127 347 vprdGIQTDDGRKSFDEVAADLAAAID----GLLADPARAAA-LLGAIQSPDTLARIAEARQLGEVLLASEavaHPEFPD 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 378 AIGPT---IFVDVDPNASLSrEEIFGPVLVVTRFTSEEQALQLANDSQYGLGA---AVWTRD---LSRAHRMSRRLKA-- 446
Cdd:cd07127 422 ARVRTpllLKLDASDEAAYA-EERFGPIAFVVATDSTDHSIELARESVREHGAmtvGVYSTDpevVERVQEAALDAGVal 500
|
330
....*....|.
gi 16129261 447 -----GSVFVN 452
Cdd:cd07127 501 sinltGGVFVN 511
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
156-452 |
1.98e-08 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 57.12 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 156 EPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGL----AKEAGLPDGVLNVVTGFGHEAGQAL 231
Cdd:PRK13805 107 EPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQKSSIAAAKIvldaAVAAGAPKDIIQWIEEPSVELTNAL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 232 SRHNDIDAIAFTGstrtGKQLLKDAGDSnmkrvwleagGKSA------N--IVFADCPDLQQAA-----SATaagiFYNq 298
Cdd:PRK13805 187 MNHPGIALILATG----GPGMVKAAYSS----------GKPAlgvgagNvpAYIDKTADIKRAVndillSKT----FDN- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 299 GQVCIAGTRLLLEESIADEFLALLKqqaqnwqpghpldpatTMGTLidcahadsvhsFIREGESK--GQLLLDGRNAGLA 376
Cdd:PRK13805 248 GMICASEQAVIVDDEIYDEVKEEFA----------------SHGAY-----------FLNKKELKklEKFIFGKENGALN 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129261 377 AAI------------------GPTIFV----DVDPNASLSREEIFgPVLVVTRFTSEEQALQLAND--SQYGLG--AAVW 430
Cdd:PRK13805 301 ADIvgqsaykiaemagfkvpeDTKILIaevkGVGESEPLSHEKLS-PVLAMYKAKDFEDAVEKAEKlvEFGGLGhtAVIY 379
|
330 340
....*....|....*....|..
gi 16129261 431 TRDLSRAHRMSRRLKAGSVFVN 452
Cdd:PRK13805 380 TNDDELIKEFGLRMKACRILVN 401
|
|
| |
