|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
19-494 |
0e+00 |
|
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: 785.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 19 GQFIAGQREAGRGAPF-AVINPATGRAIAEVTAADSDQADRAMESARQAF-SQWREMPTLARGALLLKLADTLAEHREAL 96
Cdd:cd07113 1 GHFIDGRPVAGQSEKRlDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 97 AQLESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGETLDVSLPSMAGEKYTAFTRRQPLGVVVGIVPWNFSIMIAI 176
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSIPSMQGERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 177 WKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGgEIAQRLITHPACAKVSFTGSVATGEKVQQS 256
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 257 ASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDE 336
Cdd:cd07113 240 AASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 337 RTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEAL 416
Cdd:cd07113 320 SVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460872063 417 ARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMVRY 494
Cdd:cd07113 400 QLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIRY 477
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
16-494 |
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: 591.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 16 QPHGQFIAGQ-REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHRE 94
Cdd:COG1012 4 PEYPLFIGGEwVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 95 ALAQLESLCSGKTITLARMlELDQSVAFLRYFAGWAGKVTGETLDVSLPSMagekyTAFTRRQPLGVVVGIVPWNFSIMI 174
Cdd:COG1012 84 ELAALLTLETGKPLAEARG-EVDRAADFLRYYAGEARRLYGETIPSDAPGT-----RAYVRREPLGVVGAITPWNFPLAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 175 AIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQ 254
Cdd:COG1012 158 AAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 255 QSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPL 334
Cdd:COG1012 238 AAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 335 DERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGE-GYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEE 413
Cdd:COG1012 318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEgGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 414 EALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHT-FLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:COG1012 398 EAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTtGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
..
gi 1460872063 493 RY 494
Cdd:COG1012 478 RL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
28-490 |
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: 558.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 28 AGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKT 107
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 108 ITLARMlELDQSVAFLRYFAGWAGKVTGETLDVSlpsmagEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGC 187
Cdd:pfam00171 83 LAEARG-EVDRAIDVLRYYAGLARRLDGETLPSD------PGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 188 TIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLE 267
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 268 LGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQ 347
Cdd:pfam00171 236 LGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 348 QYDKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLA 427
Cdd:pfam00171 316 QLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460872063 428 ASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDP-AVPFGGMKGSGIGREFGSAFIDDYTELKSV 490
Cdd:pfam00171 396 AGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
16-490 |
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: 521.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 16 QPHGQFIAGQ-REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAF--SQWREMPTLARGALLLKLADTLAEH 92
Cdd:cd07091 2 QPTGLFINNEfVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFetGWWRKMDPRERGRLLNKLADLIERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 93 REALAQLESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGETLDVslpsmaGEKYTAFTRRQPLGVVVGIVPWNFSI 172
Cdd:cd07091 82 RDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPI------DGNFLAYTRREPIGVCGQIIPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 173 MIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEK 252
Cdd:cd07091 156 LMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 253 VQQSASASG-KRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPG 331
Cdd:cd07091 236 IMEAAAKSNlKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 332 SPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRS 411
Cdd:cd07091 316 DPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKT 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1460872063 412 EEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSV 490
Cdd:cd07091 396 EDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
57-492 |
7.56e-173 |
|
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: 493.26 E-value: 7.56e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 57 DRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMlELDQSVAFLRYFAGWAGKVTGE 136
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 137 TLdvsLPSMAGEKytAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDG 216
Cdd:cd07078 80 VI---PSPDPGEL--AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 217 VINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLN 296
Cdd:cd07078 155 VLNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 297 QGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGE 376
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 377 -GYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVN-M 454
Cdd:cd07078 315 kGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINdY 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 1460872063 455 HTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07078 395 SVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
36-492 |
3.76e-171 |
|
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: 489.75 E-value: 3.76e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAFSQ--WREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTI--TLA 111
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIreTRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 112 RMLELdqsVAFLRYFAGWAGKVTGETLDVSLPSMagekyTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVL 191
Cdd:cd07114 81 QVRYL---AEWYRYYAGLADKIEGAVIPVDKGDY-----LNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 192 KPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGK 271
Cdd:cd07114 153 KPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 272 NAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDK 351
Cdd:cd07114 233 SPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 352 VLRLIQTARDEGDTIVCGGEALPGE----GYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLA 427
Cdd:cd07114 313 VERYVARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460872063 428 ASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07114 393 AGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
36-492 |
6.89e-171 |
|
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: 488.96 E-value: 6.89e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMlE 115
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 116 LDQSVAFLRYFAGWAGKVtgETLDVSlpsmagEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSE 195
Cdd:cd07106 80 VGGAVAWLRYTASLDLPD--EVIEDD------DTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 196 YTPLTLLRVAELAKAVgIPDGVINVVNGaGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAAL 275
Cdd:cd07106 152 FTPLCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 276 FLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLallkDKLSAFAP----GSPLDERTLMGPLANRQQYDK 351
Cdd:cd07106 230 VLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFC----EALVALAKaavvGDGLDPGTTLGPVQNKMQYDK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 352 VLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVW 431
Cdd:cd07106 306 VKELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVW 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460872063 432 SDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07106 386 SSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
36-492 |
3.13e-168 |
|
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: 482.45 E-value: 3.13e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMLE 115
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 116 LDQSVAFLRYFAGWAGKVTGETLDVSlpsmagEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSE 195
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQD------GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 196 YTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAAL 275
Cdd:cd07093 155 WTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 276 FLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRL 355
Cdd:cd07093 235 VFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 356 IQTARDEGDTIVCGGEALP----GEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVW 431
Cdd:cd07093 315 VELARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460872063 432 SDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07093 395 TRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
36-490 |
3.16e-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: 459.21 E-value: 3.16e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMlE 115
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 116 LDQSVAFLRYFAGWAGKVTGETLDVSLPSMagekyTAFTRRQPLGVVVGIVPWNF-SIMIAiWKLAAALVCGCTIVLKPS 194
Cdd:cd07103 80 VDYAASFLEWFAEEARRIYGRTIPSPAPGK-----RILVIKQPVGVVAAITPWNFpAAMIT-RKIAPALAAGCTVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 195 EYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGkNA- 273
Cdd:cd07103 154 EETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG-NAp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 274 ALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVL 353
Cdd:cd07103 233 FIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 354 RLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSD 433
Cdd:cd07103 313 ALVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1460872063 434 NIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSV 490
Cdd:cd07103 393 DLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
36-493 |
2.00e-158 |
|
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: 457.54 E-value: 2.00e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARmLE 115
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-VD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 116 LDQSVAFLRYFAGWAGKVTGETLDvslpsMAGEKYtAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSE 195
Cdd:cd07090 80 IDSSADCLEYYAGLAPTLSGEHVP-----LPGGSF-AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 196 YTPLTLLRVAELAKAVGIPDGVINVVNGaGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAAL 275
Cdd:cd07090 154 FTPLTALLLAEILTEAGLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 276 FLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRL 355
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 356 IQTARDEGDTIVCGGEALPGE-----GYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASV 430
Cdd:cd07090 313 IESAKQEGAKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460872063 431 WSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMVR 493
Cdd:cd07090 393 FTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVE 455
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
17-493 |
7.95e-157 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 453.98 E-value: 7.95e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 17 PHGQFIAGQREAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREAL 96
Cdd:PRK13473 2 QTKLLINGELVAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 97 AQLESLCSGKTITLARMLELDQSVAFLRYFAGWA----GKVTGETLdvslpsmagEKYTAFTRRQPLGVVVGIVPWNFSI 172
Cdd:PRK13473 82 ARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAArcleGKAAGEYL---------EGHTSMIRRDPVGVVASIAPWNYPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 173 MIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVgIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEK 252
Cdd:PRK13473 153 MMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 253 VQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGS 332
Cdd:PRK13473 232 VLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 333 PLDERTLMGPLANRQQYDKVLRLIQTARDEGD-TIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRS 411
Cdd:PRK13473 312 PDDEDTELGPLISAAHRDRVAGFVERAKALGHiRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 412 EEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVM 491
Cdd:PRK13473 392 EDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVM 471
|
..
gi 1460872063 492 VR 493
Cdd:PRK13473 472 VK 473
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
36-492 |
7.78e-156 |
|
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: 450.74 E-value: 7.78e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMLE 115
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 116 LDQSVAFLRYFAGWAGKVTGETLDVSLPsmagekYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSE 195
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGP------FLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 196 YTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAAL 275
Cdd:cd07115 155 LTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 276 FLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRL 355
Cdd:cd07115 235 VFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 356 IQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNI 435
Cdd:cd07115 315 VDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1460872063 436 RQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07115 395 GRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
16-492 |
5.41e-154 |
|
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: 447.24 E-value: 5.41e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 16 QPHGQFIAGQ-REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAF-SQWREMPTLARGALLLKLADTLAEHR 93
Cdd:cd07144 6 QPTGLFINNEfVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFeSWWSKVTGEERGELLDKLADLVEKNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 94 EALAQLESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGETLDVSlpsmagEKYTAFTRRQPLGVVVGIVPWNFSIM 173
Cdd:cd07144 86 DLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTS------PNKLAYTLHEPYGVCGQIIPWNYPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 174 IAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKV 253
Cdd:cd07144 160 MAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 254 QQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKL-SAFAPGS 332
Cdd:cd07144 240 MKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 333 PLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALP---GEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGY 409
Cdd:cd07144 320 PFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPeglGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 410 RSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKS 489
Cdd:cd07144 400 KTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKA 479
|
...
gi 1460872063 490 VMV 492
Cdd:cd07144 480 VHI 482
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
36-492 |
6.81e-154 |
|
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: 445.62 E-value: 6.81e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMLE 115
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 116 LDQSVAFLRYFAGWA----GKVTGETLdvslpsmagEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVL 191
Cdd:cd07092 81 LPGAVDNFRFFAGAArtleGPAAGEYL---------PGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 192 KPSEYTPLTLLRVAELAKAVgIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGK 271
Cdd:cd07092 152 KPSETTPLTTLLLAELAAEV-LPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 272 NAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDK 351
Cdd:cd07092 231 APVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 352 VLRLIQTARdEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVW 431
Cdd:cd07092 311 VAGFVERAP-AHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVW 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460872063 432 SDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07092 390 TRDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
31-490 |
1.41e-153 |
|
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: 445.51 E-value: 1.41e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 31 GAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFS--QWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTI 108
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 109 TLARMLELDQSVAFLRYFAGWAGKVTGETldvslpSMAGEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCT 188
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEV------APTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 189 IVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASAS-GKRVTLE 267
Cdd:cd07112 155 VVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 268 LGGKNAALFLDD-----LTPEAMVNGIieagYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGP 342
Cdd:cd07112 235 CGGKSPNIVFADapdldAAAEAAAAGI----FWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 343 LANRQQYDKVLRLIQTARDEGDTIVCGGEAL--PGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMN 420
Cdd:cd07112 311 LVSEAHFDKVLGYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALAN 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 421 ASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSV 490
Cdd:cd07112 391 DSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
21-490 |
2.55e-151 |
|
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: 440.21 E-value: 2.55e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 21 FIAGQ-REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQ--WREMPTLARGALLLKLADTLAEHREALA 97
Cdd:cd07119 1 YIDGEwVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 98 QLESLCSGKTITLARmLELDQSVAFLRYFAGWAGKVTGETLDVSLPSMAgekytaFTRRQPLGVVVGIVPWNFSIMIAIW 177
Cdd:cd07119 81 RLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVIS------RTVREPVGVCGLITPWNYPLLQAAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 178 KLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSA 257
Cdd:cd07119 154 KLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 258 SASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDER 337
Cdd:cd07119 234 AGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDAD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 338 TLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPG----EGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEE 413
Cdd:cd07119 314 TEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460872063 414 EALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVN-MHTFLdPAVPFGGMKGSGIGREFGSAFIDDYTELKSV 490
Cdd:cd07119 394 EAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINdYHPYF-AEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
11-492 |
5.62e-148 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 432.00 E-value: 5.62e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 11 TAFLRQPHgqFIAGQR-EAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTL 89
Cdd:PRK13252 2 SRQPLQSL--YIDGAYvEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 90 AEHREALAQLESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGETLDVSlpsmaGEKYtAFTRRQPLGVVVGIVPWN 169
Cdd:PRK13252 80 RERNDELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLR-----GGSF-VYTRREPLGVCAGIGAWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 170 FSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGgEIAQRLITHPACAKVSFTGSVAT 249
Cdd:PRK13252 154 YPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 250 GEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFA 329
Cdd:PRK13252 233 GKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 330 PGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALP----GEGYFLQPTAVKVRSEESTLMREETFGPVCS 405
Cdd:PRK13252 313 IGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTeggfANGAFVAPTVFTDCTDDMTIVREEIFGPVMS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 406 FIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNmhTF-LDPA-VPFGGMKGSGIGREFGSAFIDD 483
Cdd:PRK13252 393 VLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWIN--TWgESPAeMPVGGYKQSGIGRENGIATLEH 470
|
....*....
gi 1460872063 484 YTELKSVMV 492
Cdd:PRK13252 471 YTQIKSVQV 479
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
36-491 |
1.26e-145 |
|
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: 424.84 E-value: 1.26e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLArMLE 115
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 116 LDQSVAFLRYFAGWAGKVTgETLDVSLPsMAGEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSE 195
Cdd:cd07110 80 VDDVAGCFEYYADLAEQLD-AKAERAVP-LPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 196 YTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAAL 275
Cdd:cd07110 158 LTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 276 FLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRL 355
Cdd:cd07110 238 VFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 356 IQTARDEGDTIVCGGE--ALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSD 433
Cdd:cd07110 318 IARGKEEGARLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1460872063 434 NIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVM 491
Cdd:cd07110 398 DAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
31-493 |
5.86e-144 |
|
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: 421.76 E-value: 5.86e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 31 GAPFAVINPATGRAIAEVTAADSDQADRAMESARQAF---SQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKT 107
Cdd:cd07141 21 GKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 108 ITLARMLELDQSVAFLRYFAGWAGKVTGETLdvslpSMAGeKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGC 187
Cdd:cd07141 101 FSKSYLVDLPGAIKVLRYYAGWADKIHGKTI-----PMDG-DFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 188 TIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASG-KRVTL 266
Cdd:cd07141 175 TVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSNlKRVTL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 267 ELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANR 346
Cdd:cd07141 255 ELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 347 QQYDKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGL 426
Cdd:cd07141 335 EQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGL 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1460872063 427 AASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMVR 493
Cdd:cd07141 415 AAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
16-493 |
8.72e-143 |
|
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: 418.47 E-value: 8.72e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 16 QPHGQFIAGQREAG-RGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAF-SQW-REMPTLARGALLLKLADTLAEH 92
Cdd:cd07143 5 QPTGLFINGEFVDSvHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFeTDWgLKVSGSKRGRCLSKLADLMERN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 93 REALAQLESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGETLDVSlpsmagEKYTAFTRRQPLGVVVGIVPWNFSI 172
Cdd:cd07143 85 LDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETD------IKKLTYTRHEPIGVCGQIIPWNFPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 173 MIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEK 252
Cdd:cd07143 159 LMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 253 VQQSASASG-KRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPG 331
Cdd:cd07143 239 VMEAAAKSNlKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 332 SPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRS 411
Cdd:cd07143 319 DPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 412 EEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVM 491
Cdd:cd07143 399 EEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVH 478
|
..
gi 1460872063 492 VR 493
Cdd:cd07143 479 IN 480
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
18-492 |
9.47e-143 |
|
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: 418.19 E-value: 9.47e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 18 HGQFIAGQREAGrGAPFAVINPA-TGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREAL 96
Cdd:cd07097 1 YRNYIDGEWVAG-GDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 97 AQLESLCSGKTITLARMlELDQSVAFLRYFAGWAGKVTGETLDVSLPSMagekyTAFTRRQPLGVVVGIVPWNFSIMIAI 176
Cdd:cd07097 80 ARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPSTRPGV-----EVETTREPLGVVGLITPWNFPIAIPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 177 WKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQS 256
Cdd:cd07097 154 WKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 257 ASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDE 336
Cdd:cd07097 234 AAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 337 RTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPG--EGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEE 414
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRpdEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 415 ALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTF-LDPAVPFGGMKGSGIG-REFGSAFIDDYTELKSVMV 492
Cdd:cd07097 394 ALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTVYV 473
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
36-492 |
9.10e-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: 415.22 E-value: 9.10e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTI-TLARMl 114
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 115 ELDQSVAFLRYFAGWAGKVTGETLdvslPsmAGEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPS 194
Cdd:cd07108 80 EAAVLADLFRYFGGLAGELKGETL----P--FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 195 EYTPLTLLRVAELAKAVgIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAA 274
Cdd:cd07108 154 EDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 275 LFLDDLTPEAMVNGIIEA-GYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVL 353
Cdd:cd07108 233 IVFPDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 354 RLIQTARDE-GDTIVCGG----EALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAA 428
Cdd:cd07108 313 GYIDLGLSTsGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460872063 429 SVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFG-SAFIDDYTELKSVMV 492
Cdd:cd07108 393 YVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
21-488 |
1.19e-141 |
|
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: 415.36 E-value: 1.19e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 21 FIAGQR-EAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQL 99
Cdd:TIGR01804 1 FIDGEYvEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 100 ESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGETLDVSLPSMAgekytaFTRRQPLGVVVGIVPWNFSIMIAIWKL 179
Cdd:TIGR01804 81 ETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFA------YTIREPLGVCVGIGAWNYPLQIASWKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 180 AAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASA 259
Cdd:TIGR01804 155 APALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 260 SGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTL 339
Cdd:TIGR01804 235 HLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 340 MGPLANRQQYDKVLRLIQTARDEGDTIVCGGEAL----PGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEA 415
Cdd:TIGR01804 315 MGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPenvgLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEV 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460872063 416 LARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELK 488
Cdd:TIGR01804 395 IARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
20-490 |
2.22e-141 |
|
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: 414.59 E-value: 2.22e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 20 QFIAGQREAGRGAP-FAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQ 98
Cdd:cd07138 1 FYIDGAWVAPAGTEtIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 99 LESLCSGKTITLARMLELDQSVAFLRYFAGWAGkvtgetlDVSLPSMAGekyTAFTRRQPLGVVVGIVPWNFSI-MIAIw 177
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALK-------DFEFEERRG---NSLVVREPIGVCGLITPWNWPLnQIVL- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 178 KLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSA 257
Cdd:cd07138 150 KVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 258 SASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDER 337
Cdd:cd07138 230 ADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 338 TLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALP---GEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEE 414
Cdd:cd07138 310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPeglERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1460872063 415 ALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNmHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSV 490
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
21-490 |
2.77e-141 |
|
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: 414.28 E-value: 2.77e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 21 FIAGQ-REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQ--WREMPTLARGALLLKLADTLAEHREALA 97
Cdd:cd07139 2 FIGGRwVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 98 QLESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGETLdvsLPSMAGEkyTAFTRRQPLGVVVGIVPWNFSIMIAIW 177
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEER---RPGSGGG--HVLVRREPVGVVAAIVPWNAPLFLAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 178 KLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNgAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSA 257
Cdd:cd07139 157 KIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVP-ADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 258 SASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDER 337
Cdd:cd07139 236 GERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 338 TLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGE--ALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEA 415
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460872063 416 LARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNmHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSV 490
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
36-490 |
2.81e-139 |
|
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: 408.94 E-value: 2.81e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAF--SQWReMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARM 113
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFdtGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 114 LELDQSVAFLRYFAGWAGKVTGETlDVSLPSMAGEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKP 193
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEF-DLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 194 SEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNA 273
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 274 ALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVL 353
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 354 RLIQTARDEGDTIVCGGEALPG--EGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVW 431
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460872063 432 SDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSV 490
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
21-490 |
2.28e-138 |
|
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: 406.65 E-value: 2.28e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 21 FIAGQREAGR-GAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQL 99
Cdd:cd07088 1 YINGEFVPSSsGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 100 ESLCSGKTITLARMlELDQSVAFLRYFAGWAGKVTGETLDVSLPsmaGEKytAFTRRQPLGVVVGIVPWNFSIMIAIWKL 179
Cdd:cd07088 81 IVEEQGKTLSLARV-EVEFTADYIDYMAEWARRIEGEIIPSDRP---NEN--IFIFKVPIGVVAGILPWNFPFFLIARKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 180 AAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASA 259
Cdd:cd07088 155 APALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 260 SGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTL 339
Cdd:cd07088 235 NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 340 MGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGE-GYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALAR 418
Cdd:cd07088 315 MGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIEL 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460872063 419 MNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFlDPAVPF-GGMKGSGIGREFGSAFIDDYTELKSV 490
Cdd:cd07088 395 ANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENF-EAMQGFhAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
21-494 |
5.24e-138 |
|
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: 406.35 E-value: 5.24e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 21 FIAGQ-REAGRGAPFAVINPATGR-AIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQ 98
Cdd:cd07131 2 YIGGEwVDSASGETFDSRNPADLEeVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 99 LESLCSGKTITLARMlELDQSVAFLRYFAGWAGKVTGETLDVSLPsmagEKYtAFTRRQPLGVVVGIVPWNFSIMIAIWK 178
Cdd:cd07131 82 LVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETVPSELP----NKD-AMTRRQPIGVVALITPWNFPVAIPSWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 179 LAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSAS 258
Cdd:cd07131 156 IFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 259 ASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERT 338
Cdd:cd07131 236 RPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 339 LMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPG----EGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEE 414
Cdd:cd07131 316 DMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 415 ALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPA-VPFGGMKGSGIG-REFGSAFIDDYTELKSVMV 492
Cdd:cd07131 396 AIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVhLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
..
gi 1460872063 493 RY 494
Cdd:cd07131 476 DY 477
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
19-490 |
3.34e-136 |
|
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: 401.49 E-value: 3.34e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 19 GQFIagqrEAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQ--WREMPTLARGALLLKLADTLAEHREAL 96
Cdd:cd07142 10 GQFV----DAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 97 AQLESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGETLDVSLPsmagekYTAFTRRQPLGVVVGIVPWNFSIMIAI 176
Cdd:cd07142 86 AALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGP------HHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 177 WKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQS 256
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 257 ASASG-KRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLD 335
Cdd:cd07142 240 AAKSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 336 ERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEA 415
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460872063 416 LARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSV 490
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
37-492 |
7.25e-133 |
|
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: 392.47 E-value: 7.25e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 37 INPATGRAIAEVTAADSDQADRAMESARQAFSQ--WREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMl 114
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 115 ELDQSVAFLRYFAGWAGKVTGETLDVSLPSMagekyTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPS 194
Cdd:cd07118 81 EIEGAADLWRYAASLARTLHGDSYNNLGDDM-----LGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 195 EYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAA 274
Cdd:cd07118 156 EFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 275 LFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLR 354
Cdd:cd07118 236 IVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 355 LIQTARDEGDTIVCGGEALP-GEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSD 433
Cdd:cd07118 316 YVDAGRAEGATLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSK 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460872063 434 NIRQALRYSEAIEAGIVWVNmhTFLD--PAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07118 396 DIDTALTVARRIRAGTVWVN--TFLDgsPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
21-491 |
1.79e-132 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 393.03 E-value: 1.79e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 21 FIAGQ-REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQ--WREMPTLARGALLLKLADTLAEHREALA 97
Cdd:PLN02766 24 FINGEfVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 98 QLESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGETLDVSlpsmagEKYTAFTRRQPLGVVVGIVPWNFSIMIAIW 177
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMS------RQLQGYTLKEPIGVVGHIIPWNFPSTMFFM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 178 KLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSA 257
Cdd:PLN02766 178 KVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 258 SASG-KRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDE 336
Cdd:PLN02766 258 ATSNlKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 337 RTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEAL 416
Cdd:PLN02766 338 RARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAI 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460872063 417 ARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVM 491
Cdd:PLN02766 418 KKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVV 492
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
18-494 |
4.54e-132 |
|
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: 391.32 E-value: 4.54e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 18 HGQFIAGQ-REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREAL 96
Cdd:cd07559 1 YDNFINGEwVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 97 AQLESLCSGKTITLARMLELDQSVAFLRYFAG--WAGKVTGETLDvslpsmagEKYTAFTRRQPLGVVVGIVPWNFSIMI 174
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIPLAIDHFRYFAGviRAQEGSLSEID--------EDTLSYHFHEPLGVVGQIIPWNFPLLM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 175 AIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVgIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQ 254
Cdd:cd07559 153 AAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 255 QSASASGKRVTLELGGKNAALFLDDLTPE--AMVNGIIEA--GYL-NQGQICAAAERFYLPQGKLDAVLALLKDKLSAFA 329
Cdd:cd07559 232 QYAAENLIPVTLELGGKSPNIFFDDAMDAddDFDDKAEEGqlGFAfNQGEVCTCPSRALVQESIYDEFIERAVERFEAIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 330 PGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGE--ALPG--EGYFLQPTAVKVRSEESTLMREETFGPVCS 405
Cdd:cd07559 312 VGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGErlTLGGldKGYFYEPTLIKGGNNDMRIFQEEIFGPVLA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 406 FIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYT 485
Cdd:cd07559 392 VITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQ 471
|
....*....
gi 1460872063 486 ELKSVMVRY 494
Cdd:cd07559 472 QTKNILVSY 480
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
36-494 |
6.72e-131 |
|
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: 387.50 E-value: 6.72e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITlARMLE 115
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 116 LDQSVAFLRYFAGWAGKVTGETLDVSLPSMAgekytaFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSE 195
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKGETIPVGGRNLH------YTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 196 YTPLTLLRVAELAKAVgIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAAL 275
Cdd:cd07107 154 QAPLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 276 FLDDLTPEAMVNGIIEA-GYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLR 354
Cdd:cd07107 233 VFPDADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 355 LIQTARDEGDTIVCGGEALPGE----GYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASV 430
Cdd:cd07107 313 YIDSAKREGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAI 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1460872063 431 WSDNIRQALRYSEAIEAGIVWVNMHT--FLdpAVPFGGMKGSGIGREFGSAFIDDYTELKSVMVRY 494
Cdd:cd07107 393 WTNDISQAHRTARRVEAGYVWINGSSrhFL--GAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
19-477 |
4.34e-130 |
|
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: 385.98 E-value: 4.34e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 19 GQFIAGQ-REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALA 97
Cdd:cd07111 23 GHFINGKwVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 98 QLESLCSGKTITLARMLELDQSVAFLRYFAGWAgkvtgETLDvslpsmagekyTAFTRRQPLGVVVGIVPWNFSIMIAIW 177
Cdd:cd07111 103 VLESLDNGKPIRESRDCDIPLVARHFYHHAGWA-----QLLD-----------TELAGWKPVGVVGQIVPWNFPLLMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 178 KLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGgEIAQRLITHPACAKVSFTGSVATGEKVQQSA 257
Cdd:cd07111 167 KICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRAT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 258 SASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDER 337
Cdd:cd07111 246 AGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 338 TLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALA 417
Cdd:cd07111 326 IDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVA 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 418 RMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFG 477
Cdd:cd07111 406 LANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGG 465
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
36-492 |
1.72e-129 |
|
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: 383.51 E-value: 1.72e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAF-SQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMl 114
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFeSGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 115 ELDQSVAFLRYFAGWAGKVTGETLdvslPSMAGekYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPS 194
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETI----PLGPG--YFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 195 EYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAA 274
Cdd:cd07109 154 EDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 275 LFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTlMGPLANRQQYDKVLR 354
Cdd:cd07109 234 IVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPD-LGPLISAKQLDRVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 355 LIQTARDEGDTIVCGGEAL---PGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVW 431
Cdd:cd07109 313 FVARARARGARIVAGGRIAegaPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVW 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460872063 432 SDNIRQALRYSEAIEAGIVWVNMHTfldPA----VPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07109 393 TRDGDRALRVARRLRAGQVFVNNYG---AGggieLPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
61-492 |
4.57e-128 |
|
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: 376.95 E-value: 4.57e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 61 ESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMlELDQSVAFLRYFAGWAGKVTGETLDV 140
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLGGPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 141 SLPSMagekyTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINV 220
Cdd:cd06534 80 PDPGG-----EAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 221 VNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQI 300
Cdd:cd06534 155 VPGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 301 CAAAERFYLPQGKLDAVLALLKdklsafapgspldertlmgplanrqqydkvlrliqtardegdTIVcggealpgegyfl 380
Cdd:cd06534 235 CTAASRLLVHESIYDEFVEKLV------------------------------------------TVL------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 381 qpTAVkvrSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVN-MHTFLD 459
Cdd:cd06534 260 --VDV---DPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINdSSIGVG 334
|
410 420 430
....*....|....*....|....*....|...
gi 1460872063 460 PAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd06534 335 PEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
14-494 |
4.55e-125 |
|
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: 373.37 E-value: 4.55e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 14 LRQPHGQFIAGQ-REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAF--SQWREMPTLARGALLLKLADTLA 90
Cdd:cd07140 2 LKMPHQLFINGEfVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFenGEWGKMNARDRGRLMYRLADLME 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 91 EHREALAQLESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGETLDVSlPSMAGEKYTaFTRRQPLGVVVGIVPWNF 170
Cdd:cd07140 82 EHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPIN-QARPNRNLT-LTKREPIGVCGIVIPWNY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 171 SIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATG 250
Cdd:cd07140 160 PLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 251 EKVQQSASASG-KRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFA 329
Cdd:cd07140 240 KHIMKSCAVSNlKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 330 PGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGY 409
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 410 RSE--EEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTEL 487
Cdd:cd07140 400 DDGdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKT 479
|
....*..
gi 1460872063 488 KSVMVRY 494
Cdd:cd07140 480 KTVTIEY 486
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
21-494 |
2.21e-124 |
|
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: 371.51 E-value: 2.21e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 21 FIAGQREAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLE 100
Cdd:cd07086 2 VIGGEWVGSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 101 SLCSGKTITLARMlELDQSVAFLRYFAGWAGKVTGETLDVSLPSMAgekytAFTRRQPLGVVVGIVPWNFSIMIAIWKLA 180
Cdd:cd07086 82 SLEMGKILPEGLG-EVQEMIDICDYAVGLSRMLYGLTIPSERPGHR-----LMEQWNPLGVVGVITAFNFPVAVPGWNAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 181 AALVCGCTIVLKPSEYTPLTLLRVAELAKAV----GIPDGVINVVNGaGGEIAQRLITHPACAKVSFTGSVATGEKVQQS 256
Cdd:cd07086 156 IALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 257 ASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDE 336
Cdd:cd07086 235 VARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 337 RTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPG--EGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEE 414
Cdd:cd07086 315 GTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 415 ALARMNASPYGLAASVWSDNIRQALRYSEA--IEAGIVWVNMHTflDPA---VPFGGMKGSGIGREFGSAFIDDYTELKS 489
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNIPT--SGAeigGAFGGEKETGGGRESGSDAWKQYMRRST 472
|
....*
gi 1460872063 490 VMVRY 494
Cdd:cd07086 473 CTINY 477
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
56-492 |
5.45e-124 |
|
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: 368.78 E-value: 5.45e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 56 ADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLArMLELDQSVAFLRYFAGWAGKVTG 135
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKA-AFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 136 ETLdvslPSMAGEKyTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTL-LRVAELAKAVGIP 214
Cdd:cd07104 81 EIL----PSDVPGK-ESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 215 DGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGY 294
Cdd:cd07104 156 KGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 295 LNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEAlp 374
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 375 gEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNM 454
Cdd:cd07104 314 -EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 1460872063 455 HTFLD-PAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07104 393 QTVNDePHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
34-492 |
1.29e-123 |
|
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: 368.60 E-value: 1.29e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 34 FAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARm 113
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 114 LELDQSVAFLRYFAGWAGKVTGETLDVSlPSMAGEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKP 193
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPVD-AYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 194 SEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNA 273
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 274 ALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVL 353
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 354 RLIQTARDEGDTIVCGGEALpgEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSD 433
Cdd:cd07145 319 NLVNDAVEKGGKILYGGKRD--EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTN 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 434 NIRQALRYSEAIEAGIVWVNMHTFLDP-AVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07145 397 DINRALKVARELEAGGVVINDSTRFRWdNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
34-492 |
2.73e-123 |
|
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: 367.81 E-value: 2.73e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 34 FAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLArM 113
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA-W 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 114 LELDQSVAFLRYFAGWAGKVTGETLdvslPS-MAGEKYTAFtrRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLK 192
Cdd:cd07150 80 FETTFTPELLRAAAGECRRVRGETL----PSdSPGTVSMSV--RRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 193 PSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKN 272
Cdd:cd07150 154 PSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 273 AALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKV 352
Cdd:cd07150 234 PLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 353 LRLIQTARDEGDTIVCGGEalpGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWS 432
Cdd:cd07150 314 KRQVEDAVAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILT 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460872063 433 DNIRQALRYSEAIEAGIVWVNMHTFLD-PAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07150 391 NDLQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
18-492 |
4.32e-123 |
|
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: 367.94 E-value: 4.32e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 18 HGQFIAGQ-REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREAL 96
Cdd:cd07117 1 YGLFINGEwVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 97 AQLESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGETldvslpSMAGEKYTAFTRRQPLGVVVGIVPWNFSIMIAI 176
Cdd:cd07117 81 AMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSA------NMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 177 WKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVgIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQS 256
Cdd:cd07117 155 WKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 257 ASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDE 336
Cdd:cd07117 234 AAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 337 RTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGE----GYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSE 412
Cdd:cd07117 314 DTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 413 EEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07117 394 DEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
19-494 |
2.05e-121 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 364.82 E-value: 2.05e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 19 GQFIAGQ-REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQ-----WREMPTLARGALLLKLADTLAEH 92
Cdd:PLN02467 9 QLFIGGEwREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 93 REALAQLESLCSGKTITLArMLELDQSVAFLRYFAGWAGKVTG-ETLDVSLPsMagEKYTAFTRRQPLGVVVGIVPWNFS 171
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEALDAkQKAPVSLP-M--ETFKGYVLKEPLGVVGLITPWNYP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 172 IMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGE 251
Cdd:PLN02467 165 LLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 252 KVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPG 331
Cdd:PLN02467 245 KIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKIS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 332 SPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPG--EGYFLQPTAVKVRSEESTLMREETFGPVCSFIGY 409
Cdd:PLN02467 325 DPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 410 RSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKS 489
Cdd:PLN02467 405 STEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQ 484
|
....*
gi 1460872063 490 VmVRY 494
Cdd:PLN02467 485 V-TKY 488
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
21-490 |
2.58e-120 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 361.70 E-value: 2.58e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 21 FIAGQ-REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQL 99
Cdd:PLN02278 28 LIGGKwTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 100 ESLCSGKTITLARMlELDQSVAFLRYFAGWAGKVTGETLdvslPSMAGEKyTAFTRRQPLGVVVGIVPWNFSIMIAIWKL 179
Cdd:PLN02278 108 MTLEQGKPLKEAIG-EVAYGASFLEYFAEEAKRVYGDII----PSPFPDR-RLLVLKQPVGVVGAITPWNFPLAMITRKV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 180 AAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASA 259
Cdd:PLN02278 182 GPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 260 SGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTL 339
Cdd:PLN02278 262 TVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 340 MGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARM 419
Cdd:PLN02278 342 QGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIA 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460872063 420 NASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSV 490
Cdd:PLN02278 422 NDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
36-488 |
3.73e-116 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 349.42 E-value: 3.73e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMlE 115
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKG-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 116 LDQSVAFLRYFAGWAGKVTGETLdvslPSMAGEKYtAFTRRQPLGVVVGIVPWNF-SIMIAiWKLAAALVCGCTIVLKPS 194
Cdd:TIGR01780 80 ILYAASFLEWFAEEAKRVYGDTI----PSPQSDKR-LIVIKQPVGVCAAITPWNFpAAMIT-RKAGAALAAGCTVVVKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 195 EYTPLTLLRVAELAKAVGIPDGVINVVNG-AGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNA 273
Cdd:TIGR01780 154 EQTPLSALALARLAEQAGIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 274 ALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVL 353
Cdd:TIGR01780 234 FIVFDDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 354 RLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSD 433
Cdd:TIGR01780 314 KHIADAVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSR 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1460872063 434 NIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELK 488
Cdd:TIGR01780 394 DLSRIWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
36-490 |
1.22e-115 |
|
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: 348.05 E-value: 1.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMlE 115
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK-E 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 116 LDQSVAFLRYFAGWAGKVTGETLDVSlPSMAGEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSE 195
Cdd:cd07149 82 VDRAIETLRLSAEEAKRLAGETIPFD-ASPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 196 YTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASAsgKRVTLELGGKNAAL 275
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGL--KKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 276 FLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRL 355
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 356 IQTARDEGDTIVCGGEAlpgEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNI 435
Cdd:cd07149 319 VEEAVEGGARLLTGGKR---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1460872063 436 RQALRYSEAIEAGIVWVN-MHTFLDPAVPFGGMKGSGIGREfGSAF-IDDYTELKSV 490
Cdd:cd07149 396 QKALKAARELEVGGVMINdSSTFRVDHMPYGGVKESGTGRE-GPRYaIEEMTEIKLV 451
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
19-491 |
1.59e-114 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 348.34 E-value: 1.59e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 19 GQFIagqrEAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQ--WREMPTLARGALLLKLADTLAEHREAL 96
Cdd:PLN02466 64 GQFV----DAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 97 AQLESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGETLDVSLPsmagekYTAFTRRQPLGVVVGIVPWNFSIMIAI 176
Cdd:PLN02466 140 AALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGP------HHVQTLHEPIGVAGQIIPWNFPLLMFA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 177 WKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQS 256
Cdd:PLN02466 214 WKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLEL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 257 ASASG-KRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLD 335
Cdd:PLN02466 294 AAKSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFK 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 336 ERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEA 415
Cdd:PLN02466 374 KGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEV 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1460872063 416 LARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVM 491
Cdd:PLN02466 454 IRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
37-490 |
1.88e-114 |
|
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: 345.10 E-value: 1.88e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 37 INPATGRAIAEVTAADSDQADRAMESARQAF--SQWREMPTLaRGALLLKLADTLAEHREALAQLESLCSGKTITLARmL 114
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEAR-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 115 ELDQSVAFLRYFAGWAGKVTGETLDVSLPSMAgekytaFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPS 194
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFS------LVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 195 EYTPLTLLRVAE-LAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNA 273
Cdd:cd07120 154 GQTAQINAAIIRiLAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 274 ALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVL 353
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 354 RLIQTARDEGDTIVCGGEALPGE---GYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASV 430
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTEGlakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 431 WSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSV 490
Cdd:cd07120 394 WTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
37-492 |
5.43e-112 |
|
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: 338.81 E-value: 5.43e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 37 INPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARmLEL 116
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-LEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 117 DQSVAFLRYFAGWAGKVTGETlDVSLPSMAGEKyTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEY 196
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPR-KVPTGLLMPNK-KATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 197 TPLTLLRVAELAKAVGIPDGVINVVNGAGgEIAQRLITHPAcAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALF 276
Cdd:cd07099 158 TPLVGELLAEAWAAAGPPQGVLQVVTGDG-ATGAALIDAGV-DKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 277 LDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRLI 356
Cdd:cd07099 236 LADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 357 QTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIR 436
Cdd:cd07099 316 DDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1460872063 437 QALRYSEAIEAGIVWVNMH--TFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07099 396 RAEAIARRLEAGAVSINDVllTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
26-492 |
2.46e-110 |
|
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: 335.04 E-value: 2.46e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 26 REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSG 105
Cdd:cd07151 4 RDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 106 KTITLArMLELDQSVAFLRYFAGWAGKVTGETLDVSLPSMAGEKYtaftrRQPLGVVVGIVPWNFSIMIAIWKLAAALVC 185
Cdd:cd07151 84 STRIKA-NIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVY-----REPLGVVGVISPWNFPLHLSMRSVAPALAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 186 GCTIVLKPSEYTPLT--LLrVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKR 263
Cdd:cd07151 158 GNAVVLKPASDTPITggLL-LAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 264 VTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPL 343
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 344 ANRQQYDKVLRLIQTARDEGDTIVCGGEAlpgEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASP 423
Cdd:cd07151 317 INESQVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 424 YGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLD-PAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07151 394 YGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDePHVPFGGEKNSGLGRFNGEWALEEFTTDKWISV 463
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
56-492 |
7.33e-110 |
|
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: 332.50 E-value: 7.33e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 56 ADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARmLELDQSVAFLRYFAGwagkvTG 135
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEAR-AEVEKCAWICRYYAE-----NA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 136 ETL--DVSLPSMAGEkytAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGI 213
Cdd:cd07100 75 EAFlaDEPIETDAGK---AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 214 PDGVINVVNGAGGEIAQrLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAG 293
Cdd:cd07100 152 PEGVFQNLLIDSDQVEA-IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 294 YLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEAL 373
Cdd:cd07100 231 LQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 374 PGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVN 453
Cdd:cd07100 311 DGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
|
410 420 430
....*....|....*....|....*....|....*....
gi 1460872063 454 MHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07100 391 GMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
21-494 |
5.11e-108 |
|
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: 329.48 E-value: 5.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 21 FIAGQREAGRGAPFA-VINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQL 99
Cdd:cd07085 4 FINGEWVESKTTEWLdVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 100 ESLCSGKTIT-----LARMLELDQ---SVAFLryfagwagkVTGETLDVSLPSMagekyTAFTRRQPLGVVVGIVPWNFS 171
Cdd:cd07085 84 ITLEHGKTLAdargdVLRGLEVVEfacSIPHL---------LKGEYLENVARGI-----DTYSYRQPLGVVAGITPFNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 172 IMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGaGGEIAQRLITHPACAKVSFTGSVATGE 251
Cdd:cd07085 150 AMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 252 KVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPG 331
Cdd:cd07085 229 YIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 332 SPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGE--ALPG--EGYFLQPTAVKVRSEESTLMREETFGPVCSFI 407
Cdd:cd07085 309 AGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRgvKVPGyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 408 GYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMhtfldP-AVP-----FGGMKGS--GIGREFGSA 479
Cdd:cd07085 389 RVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINV-----PiPVPlaffsFGGWKGSffGDLHFYGKD 463
|
490
....*....|....*
gi 1460872063 480 FIDDYTELKSVMVRY 494
Cdd:cd07085 464 GVRFYTQTKTVTSRW 478
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
55-490 |
1.68e-106 |
|
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: 324.15 E-value: 1.68e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 55 QADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARmLELDQSVAFLRYFAGWAGKVT 134
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAG-FNVDLAAGMLREAASLITQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 135 GETLDVSLPSMagekyTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIP 214
Cdd:cd07105 80 GGSIPSDKPGT-----LAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 215 DGVINVVNGA---GGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIE 291
Cdd:cd07105 155 KGVLNVVTHSpedAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 292 AGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSplderTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGE 371
Cdd:cd07105 235 GAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 372 A-LPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIV 450
Cdd:cd07105 310 AdESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1460872063 451 WVNMHTFLD-PAVPFGGMKGSGIGREFGSAFIDDYTELKSV 490
Cdd:cd07105 390 HINGMTVHDePTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
21-492 |
6.80e-106 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 324.54 E-value: 6.80e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 21 FIAGQ-REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQ--WREMPTLARGALLLKLADTLAEHREALA 97
Cdd:PRK09847 23 FINGEyTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 98 QLESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGETldvslpSMAGEKYTAFTRRQPLGVVVGIVPWNFSIMIAIW 177
Cdd:PRK09847 103 LLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEV------ATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 178 KLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSA 257
Cdd:PRK09847 177 KLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 258 SASG-KRVTLELGGKNAAL-FLD----DLTPEAMVNGIieagYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPG 331
Cdd:PRK09847 257 GDSNmKRVWLEAGGKSANIvFADcpdlQQAASATAAGI----FYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 332 SPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGE-ALPGegyFLQPTAVKVRSEESTLMREETFGPVCSFIGYR 410
Cdd:PRK09847 333 HPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNaGLAA---AIGPTIFVDVDPNASLSREEIFGPVLVVTRFT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 411 SEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSV 490
Cdd:PRK09847 410 SEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
..
gi 1460872063 491 MV 492
Cdd:PRK09847 490 WI 491
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
35-492 |
1.41e-105 |
|
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: 322.46 E-value: 1.41e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 35 AVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMl 114
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 115 ELDQSVAFLRYFAGWAGKVTGETLDVSLpSMAGEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPS 194
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDA-TQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 195 EYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVqqSASASGKRVTLELGGKNAA 274
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 275 LFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLR 354
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 355 LIQTARDEGDTIVCGGEAlpgEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDN 434
Cdd:cd07094 318 WVEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460872063 435 IRQALRYSEAIEAGIVWVNMHTFLD-PAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVNDSSAFRtDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
18-494 |
1.06e-102 |
|
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: 315.93 E-value: 1.06e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 18 HGQFIAGQ-REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREAL 96
Cdd:cd07116 1 YDNFIGGEwVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 97 AQLESLCSGKTI--TLARMLELdqSVAFLRYFAGWAGKVTGETLDVSlpsmagEKYTAFTRRQPLGVVVGIVPWNFSIMI 174
Cdd:cd07116 81 AVAETWDNGKPVreTLAADIPL--AIDHFRYFAGCIRAQEGSISEID------ENTVAYHFHEPLGVVGQIIPWNFPLLM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 175 AIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVgIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQ 254
Cdd:cd07116 153 ATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 255 QSASASGKRVTLELGGKNAALFLDDLTPE--AMVNGIIEaGY----LNQGQICAAAERFYLPQGKLDAVLALLKDKLSAF 328
Cdd:cd07116 232 QYASENIIPVTLELGGKSPNIFFADVMDAddAFFDKALE-GFvmfaLNQGEVCTCPSRALIQESIYDRFMERALERVKAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 329 APGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEA--LPG--EGYFLQPTAVKVRSEestlMR---EETFG 401
Cdd:cd07116 311 KQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERneLGGllGGGYYVPTTFKGGNK----MRifqEEIFG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 402 PVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFI 481
Cdd:cd07116 387 PVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMML 466
|
490
....*....|...
gi 1460872063 482 DDYTELKSVMVRY 494
Cdd:cd07116 467 DHYQQTKNLLVSY 479
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
37-491 |
6.63e-100 |
|
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: 307.64 E-value: 6.63e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 37 INPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMlEL 116
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG-EI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 117 DQSVAFLRYFAGWAGKVTgetLDVSLPSMAGekYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEY 196
Cdd:cd07102 80 RGMLERARYMISIAEEAL---ADIRVPEKDG--FERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 197 TPLTLLRVAELAKAVGIPDGVINVVNGaGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALF 276
Cdd:cd07102 155 TPLCGERFAAAFAEAGLPEGVFQVLHL-SHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 277 LDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRLI 356
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 357 QTARDEGDTIVCGGEALP---GEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSD 433
Cdd:cd07102 314 ADAIAKGARALIDGALFPedkAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTK 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1460872063 434 NIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVM 491
Cdd:cd07102 394 DIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSYH 451
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
36-492 |
1.62e-99 |
|
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: 306.86 E-value: 1.62e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARmLE 115
Cdd:cd07147 3 VTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR-GE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 116 LDQSVAFLRYFAGWAGKVTGETLDVSLpSMAGEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSE 195
Cdd:cd07147 82 VARAIDTFRIAAEEATRIYGEVLPLDI-SARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 196 YTPLTLLRVAELAKAVGIPDGVINVVNgAGGEIAQRLITHPACAKVSFTGSVATGEKVqqSASASGKRVTLELGGKNAAL 275
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLP-CSRDDADLLVTDERIKLLSFTGSPAVGWDL--KARAGKKKVVLELGGNAAVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 276 FLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRL 355
Cdd:cd07147 238 VDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 356 IQTARDEGDTIVCGGEAlpgEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNI 435
Cdd:cd07147 318 VNEAVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1460872063 436 RQALRYSEAIEAGIVWVN-MHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07147 395 EKALRAWDELEVGGVVINdVPTFRVDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
7-488 |
7.02e-96 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 298.36 E-value: 7.02e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 7 LAEVTAFLRQphgQFIAGQ-REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKL 85
Cdd:PRK11241 3 LNDSTLFRQQ---ALINGEwLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 86 ADTLAEHREALAQLESLCSGKTITLARMlELDQSVAFLRYFAGWAGKVTGETLdvslPSMAGEKyTAFTRRQPLGVVVGI 165
Cdd:PRK11241 80 FNLMMEHQDDLARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTI----PGHQADK-RLIVIKQPIGVTAAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 166 VPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTG 245
Cdd:PRK11241 154 TPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 246 SVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKL 325
Cdd:PRK11241 234 STEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 326 SAFAPGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCS 405
Cdd:PRK11241 314 SKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 406 FIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYT 485
Cdd:PRK11241 394 LFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYL 473
|
...
gi 1460872063 486 ELK 488
Cdd:PRK11241 474 EIK 476
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
20-490 |
1.86e-95 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 297.06 E-value: 1.86e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 20 QFIAGQREAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAF--SQWREMPTLaRGALLLKLADTLAEHREALA 97
Cdd:TIGR04284 3 LLIDGKLVAGSAGTFPTVNPATEEVLGVAADATAADMDAAIAAARRAFdeTDWSRDTAL-RVRCLRQLRDALRAHVEELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 98 QLESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGETlDVSLPSMAGEKYTAFTRRQPLGVVVGIVPWNFSIMIAIW 177
Cdd:TIGR04284 82 ELTIAEVGAPRMLTAGAQLEGPVDDLGFAADLAESYAWTT-DLGVASPMGIPTRRTLRREAVGVVGAITPWNFPHQINLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 178 KLAAALVCGCTIVLKPSEYTPLTLLRVAEL-AKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQS 256
Cdd:TIGR04284 161 KLGPALAAGNTVVLKPAPDTPWCAAVLGELiAEHTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRAVMAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 257 ASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDE 336
Cdd:TIGR04284 241 AAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 337 RTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGeALPGE---GYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEE 413
Cdd:TIGR04284 321 GTVCGPVISARQRDRVQSYLDLAVAEGGRFACGG-GRPADrdrGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDD 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1460872063 414 EALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSV 490
Cdd:TIGR04284 400 DAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETKLI 476
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
7-473 |
7.08e-94 |
|
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: 294.13 E-value: 7.08e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 7 LAEVTAFLRQPHGQFIAGQREAGRGApFAVINPA-TGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKL 85
Cdd:cd07124 22 LARVREELGREYPLVIGGKEVRTEEK-IESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 86 ADTLAEHREALAQLESLCSGKTITLArMLELDQSVAFLRYFAGWAGKVTGETLdvslPSMAGEKYTAFTRrqPLGVVVGI 165
Cdd:cd07124 101 AALLRRRRFELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPV----EMVPGEDNRYVYR--PLGVGAVI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 166 VPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTG 245
Cdd:cd07124 174 SPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 246 SVATGEKVQQSAS--ASG----KRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLA 319
Cdd:cd07124 254 SREVGLRIYERAAkvQPGqkwlKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 320 LLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGdTIVCGGEALPG--EGYFLQPTAVKVRSEESTLMRE 397
Cdd:cd07124 334 RLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460872063 398 ETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMH-TFLDPAV-PFGGMKGSGIG 473
Cdd:cd07124 413 EIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKiTGALVGRqPFGGFKMSGTG 490
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
21-475 |
1.21e-92 |
|
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: 289.47 E-value: 1.21e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 21 FIAGQREAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAF-SQWREMPTLARGALLLKLADTLAEHREALAQL 99
Cdd:cd07082 5 LINGEWKESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGrGWWPTMPLEERIDCLHKFADLLKENKEEVANL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 100 ESLCSGKTITLARMlELDQSVAFLRYFAGWAGKVTGETLDVSLPSMAGEKYtAFTRRQPLGVVVGIVPWNFSIMIAIWKL 179
Cdd:cd07082 85 LMWEIGKTLKDALK-EVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKI-AQVRREPLGVVLAIGPFNYPLNLTVSKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 180 AAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQsaSA 259
Cdd:cd07082 163 IPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK--QH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 260 SGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTL 339
Cdd:cd07082 241 PMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 340 MGPLANRQQYDKVLRLIQTARDEGDTIVCGGEalpGEGY-FLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALAR 418
Cdd:cd07082 321 ITPLIDPKSADFVEGLIDDAVAKGATVLNGGG---REGGnLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1460872063 419 MNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAV-PFGGMKGSGIGRE 475
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQ 455
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
42-486 |
3.65e-92 |
|
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: 287.27 E-value: 3.65e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 42 GRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARmLELDQSVA 121
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAG-FEVGAAIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 122 FLRYFAGWAGKVTGETLdvslPSMAGEkyTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTL 201
Cdd:cd07152 80 ELHEAAGLPTQPQGEIL----PSAPGR--LSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 202 -LRVAELAKAVGIPDGVINVVNGaGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDL 280
Cdd:cd07152 154 gVVIARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 281 TPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRLIQTAR 360
Cdd:cd07152 233 DLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 361 DEGDTIVCGGEAlpgEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALR 440
Cdd:cd07152 313 AAGARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1460872063 441 YSEAIEAGIVWVNMHTFLD-PAVPFGGMKGSGIGREFGS-AFIDDYTE 486
Cdd:cd07152 390 LADRLRTGMLHINDQTVNDePHNPFGGMGASGNGSRFGGpANWEEFTQ 437
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
22-490 |
3.86e-91 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 287.16 E-value: 3.86e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 22 IAGQREAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLES 101
Cdd:PRK09407 22 LTARVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 102 LCSGKtitlARMLELD--QSVAFL-RYFAGWAGK------VTGetldvSLPSMAgekyTAFTRRQPLGVVVGIVPWNFSI 172
Cdd:PRK09407 102 LETGK----ARRHAFEevLDVALTaRYYARRAPKllaprrRAG-----ALPVLT----KTTELRQPKGVVGVISPWNYPL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 173 MIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHpaCAKVSFTGSVATGEK 252
Cdd:PRK09407 169 TLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 253 VqqsASASGKR---VTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFA 329
Cdd:PRK09407 247 L---AEQAGRRligFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 330 PGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGEG-YFLQPTAVKVRSEESTLMREETFGPVCSFIG 408
Cdd:PRK09407 324 LGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 409 YRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVN---MHTFLDPAVPFGGMKGSGIGREFGSAFIDDYT 485
Cdd:PRK09407 404 VADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyAAAWGSVDAPMGGMKDSGLGRRHGAEGLLKYT 483
|
....*
gi 1460872063 486 ELKSV 490
Cdd:PRK09407 484 ESQTI 488
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
36-490 |
6.45e-91 |
|
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: 284.64 E-value: 6.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARqafsqwREMPTLA---RGALLLKLADTLAEHREALAQLESLCSGKTITLAR 112
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALAA------SYRSTLTryqRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 113 MlELDQSVAFLRYFAGWAGKVTGETLDVSLPSMAGEKyTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLK 192
Cdd:cd07146 77 Y-EVGRAADVLRFAAAEALRDDGESFSCDLTANGKAR-KIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 193 PSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVqqSASASGKRVTLELGGKN 272
Cdd:cd07146 155 PSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 273 AALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKV 352
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 353 LRLIQTARDEGDTIVCGGEAlpgEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWS 432
Cdd:cd07146 313 ENRVEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 433 DNIRQALRYSEAIEAGIVWVN-MHTFLDPAVPFGGMKGSGIG-REFGSAFIDDYTELKSV 490
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNeVPGFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
82-494 |
1.40e-90 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 282.40 E-value: 1.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 82 LLKLADTLAEHREALAQLESLCSGKTITLARmLELDQSVAFLRYFAGWAGKVTGETLDVSLPsmaGEKYTAFtrRQPLGV 161
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAE-VEVAFTADYIDYMAEWARRYEGEIIQSDRP---GENILLF--KRALGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 162 VVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKV 241
Cdd:PRK10090 75 TTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 242 SFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALL 321
Cdd:PRK10090 155 SMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 322 KDKLSAFAPGSPLDERTL-MGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETF 400
Cdd:PRK10090 235 GEAMQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 401 GPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAF 480
Cdd:PRK10090 315 GPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHG 394
|
410
....*....|....
gi 1460872063 481 IDDYTELKSVMVRY 494
Cdd:PRK10090 395 LHEYLQTQVVYLQS 408
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
37-492 |
1.81e-87 |
|
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: 275.73 E-value: 1.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 37 INPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLArMLEL 116
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHA-FEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 117 DQSVAFLRYFAGWAGKVTGETLDVS-LPSMAgekyTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSE 195
Cdd:cd07101 80 LDVAIVARYYARRAERLLKPRRRRGaIPVLT----RTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 196 YTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHpaCAKVSFTGSVATGEKVQQSAsasGKRVT---LELGGKN 272
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERA---GRRLIgcsLELGGKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 273 AALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKV 352
Cdd:cd07101 231 PMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 353 LRLIQTARDEGDTIVCGGEALPGEG-YFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVW 431
Cdd:cd07101 311 TAHVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVW 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460872063 432 SDNIRQALRYSEAIEAGIVWVN---MHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07101 391 TRDGARGRRIAARLRAGTVNVNegyAAAWASIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
29-478 |
2.55e-84 |
|
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: 268.31 E-value: 2.55e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 29 GRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTI 108
Cdd:cd07130 9 GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 109 TLAR-----MLEL-DQSVAFLRYFAGwagkvtgetldvslPSMAGEKYTAFTRRQ--PLGVVVGIVPWNFSIMIAIWKLA 180
Cdd:cd07130 89 PEGLgevqeMIDIcDFAVGLSRQLYG--------------LTIPSERPGHRMMEQwnPLGVVGVITAFNFPVAVWGWNAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 181 AALVCGCTIVLKPSEYTPLTLLRV----AELAKAVGIPDGVINVVNGaGGEIAQRLITHPACAKVSFTGSVATGEKVQQS 256
Cdd:cd07130 155 IALVCGNVVVWKPSPTTPLTAIAVtkivARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 257 ASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDE 336
Cdd:cd07130 234 VAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 337 RTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSeESTLMREETFGPVCSFIGYRSEEEAL 416
Cdd:cd07130 314 GTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLS-DAPIVKEETFAPILYVLKFDTLEEAI 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1460872063 417 ARMNASPYGLAASVWSDNIRQALRYSEAI--EAGIVWVNMHTF---LDPAvpFGGMKGSGIGREFGS 478
Cdd:cd07130 393 AWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGTSgaeIGGA--FGGEKETGGGRESGS 457
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
21-494 |
8.61e-83 |
|
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: 264.44 E-value: 8.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 21 FIAGQREAGRGAPFA-VINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQL 99
Cdd:TIGR01722 4 WIGGKFAEGASGTYIpVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 100 ESLCSGKTITLARMlELDQSVAFLRYFAGWAGKVTGETLdvslPSMAgEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKL 179
Cdd:TIGR01722 84 ITAEHGKTHSDALG-DVARGLEVVEHACGVNSLLKGETS----TQVA-TRVDVYSIRQPLGVCAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 180 AAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGaGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASA 259
Cdd:TIGR01722 158 PIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 260 SGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLpQGKLDAVLALLKDKLSAFAPGSPLDERTL 339
Cdd:TIGR01722 237 HGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVL-VGAADEWVPEIRERAEKIRIGPGDDPGAE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 340 MGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGEGY----FLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEA 415
Cdd:TIGR01722 316 MGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 416 LARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLD-PAVPFGGMKGSGIG--REFGSAFIDDYTELKSVMV 492
Cdd:TIGR01722 396 IALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPlPYFSFTGWKDSFFGdhHIYGKQGTHFYTRGKTVTT 475
|
..
gi 1460872063 493 RY 494
Cdd:TIGR01722 476 RW 477
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
7-494 |
2.77e-82 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 264.10 E-value: 2.77e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 7 LAEVTAFLRQPHGQFIAGQREAGRGApFAVINPA-TGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKL 85
Cdd:PRK03137 26 LKKVEKELGQDYPLIIGGERITTEDK-IVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 86 ADTLAEHREALAQLESLCSGKTITlarmlELDQSVA----FLRYFAGwagkvtgETLD----VSLPSMAGEKYTAFTrrQ 157
Cdd:PRK03137 105 AAIIRRRKHEFSAWLVKEAGKPWA-----EADADTAeaidFLEYYAR-------QMLKladgKPVESRPGEHNRYFY--I 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 158 PLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPA 237
Cdd:PRK03137 171 PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 238 CAKVSFTGSVATGEKVQQSAS--ASG----KRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQ 311
Cdd:PRK03137 251 TRFITFTGSREVGLRIYERAAkvQPGqiwlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 312 GKLDAVLALLKDKLSAFAPGSPlDERTLMGPLANRQQYDKVLRLIQTARDEGDtIVCGGEALPGEGYFLQPTAVKVRSEE 391
Cdd:PRK03137 331 DVYDEVLEKVVELTKELTVGNP-EDNAYMGPVINQASFDKIMSYIEIGKEEGR-LVLGGEGDDSKGYFIQPTIFADVDPK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 392 STLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWS---DNIRQA--------LRYSEAIEAGIVWVNmhtfldp 460
Cdd:PRK03137 409 ARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISnnrEHLEKArrefhvgnLYFNRGCTGAIVGYH------- 481
|
490 500 510
....*....|....*....|....*....|....*...
gi 1460872063 461 avPFGGMKGSGIGREFGSAfidDY----TELKSVMVRY 494
Cdd:PRK03137 482 --PFGGFNMSGTDSKAGGP---DYlllfLQAKTVSEMF 514
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
33-492 |
1.82e-81 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 260.06 E-value: 1.82e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 33 PFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLAR 112
Cdd:PRK09406 2 PIATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 113 MlELDQSVAFLRYFAGWAgkvtgETLDVSLPSMAGE--KYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIV 190
Cdd:PRK09406 82 A-EALKCAKGFRYYAEHA-----EALLADEPADAAAvgASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 191 LKPSEYTPLTLLRVAELAKAVGIPDGVI-NVVNGAGGeiAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELG 269
Cdd:PRK09406 156 LKHASNVPQTALYLADLFRRAGFPDGCFqTLLVGSGA--VEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 270 GKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQY 349
Cdd:PRK09406 234 GSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 350 DKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAAS 429
Cdd:PRK09406 314 DEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSN 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460872063 430 VWSDNIRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:PRK09406 394 AWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
21-473 |
4.63e-81 |
|
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: 260.98 E-value: 4.63e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 21 FIAGQREAgRGAPFAVINPA-TGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHRE---AL 96
Cdd:cd07125 36 IINGEETE-TGEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGeliAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 97 AQLESlcsGKTI--TLArmlELDQSVAFLRYFAGWAGKVTGetlDVSLPSMAGEkyTAFTRRQPLGVVVGIVPWNFSIMI 174
Cdd:cd07125 115 AAAEA---GKTLadADA---EVREAIDFCRYYAAQARELFS---DPELPGPTGE--LNGLELHGRGVFVCISPWNFPLAI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 175 AIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQ 254
Cdd:cd07125 184 FTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLIN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 255 QS-ASASGKRVTL--ELGGKNA------ALflddltPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKL 325
Cdd:cd07125 264 RAlAERDGPILPLiaETGGKNAmivdstAL------PEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 326 SAFAPGSPLDERTLMGPLAnRQQYDKVLR-LIQTARDEGdTIVCGGEALPGEGYFLQPTAVKVrsEESTLMREETFGPVC 404
Cdd:cd07125 338 ASLKVGDPWDLSTDVGPLI-DKPAGKLLRaHTELMRGEA-WLIAPAPLDDGNGYFVAPGIIEI--VGIFDLTTEVFGPIL 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460872063 405 SFIGYRSE--EEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFldPAV----PFGGMKGSGIG 473
Cdd:cd07125 414 HVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNIT--GAIvgrqPFGGWGLSGTG 486
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
38-478 |
1.45e-79 |
|
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: 255.69 E-value: 1.45e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 38 NPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMLELD 117
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 118 QSVAFLRYFAGwAGKVTGETLDVSLPSMAGEKyTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYT 197
Cdd:cd07098 82 VTCEKIRWTLK-HGEKALRPESRPGGLLMFYK-RARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 198 P------LTLLRvaELAKAVGIPDGVINVVNGAGgEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGK 271
Cdd:cd07098 160 AwssgffLSIIR--ECLAACGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 272 NAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDK 351
Cdd:cd07098 237 DPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 352 VLRLIQTARDEGDTIVCGGEALPG----EGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLA 427
Cdd:cd07098 317 LEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1460872063 428 ASVWSDNIRQALRYSEAIEAGIVWVN--MHTFLDPAVPFGGMKGSGIGReFGS 478
Cdd:cd07098 397 ASVFGKDIKRARRIASQLETGMVAINdfGVNYYVQQLPFGGVKGSGFGR-FAG 448
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
7-494 |
5.19e-78 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 252.86 E-value: 5.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 7 LAEVTAFLRQPHGQFIAGQREAGRGApFAVINPA-TGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKL 85
Cdd:TIGR01237 22 LATVKEQLGKTYPLVINGERVETENK-IVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 86 ADTLAEHREALAQLESLCSGKTITLARMlELDQSVAFLRYFAGWAGKVTGETLDVSLPsmaGEKYTAFTrrQPLGVVVGI 165
Cdd:TIGR01237 101 AAIVRRRRHEFSALLVKEVGKPWNEADA-EVAEAIDFMEYYARQMIELAKGKPVNSRE---GETNQYVY--TPTGVTVVI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 166 VPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTG 245
Cdd:TIGR01237 175 SPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 246 SVATGEKVQQSASASG------KRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLA 319
Cdd:TIGR01237 255 SREVGTRIFERAAKVQpgqkhlKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 320 LLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGDtIVCGGEALPGEGYFLQPTAVKVRSEESTLMREET 399
Cdd:TIGR01237 335 RFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGR-LVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 400 FGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNmHTFLDPAV---PFGGMKGSGIGREF 476
Cdd:TIGR01237 414 FGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFN-RNITGAIVgyqPFGGFKMSGTDSKA 492
|
490
....*....|....*....
gi 1460872063 477 GSA-FIDDYTELKSVMVRY 494
Cdd:TIGR01237 493 GGPdYLALFMQAKTVTEMF 511
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
18-490 |
6.64e-78 |
|
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: 252.11 E-value: 6.64e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 18 HGQFIAGQREAGRGAPFAVINP-ATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREAL 96
Cdd:cd07083 18 AYPLVIGGEWVDTKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRREL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 97 AQLESLCSGKTITLArMLELDQSVAFLRYFAGWAGKVTGETldVSLPSMAGEKYTAFTrrQPLGVVVGIVPWNFSIMIAI 176
Cdd:cd07083 98 IATLTYEVGKNWVEA-IDDVAEAIDFIRYYARAALRLRYPA--VEVVPYPGEDNESFY--VGLGAGVVISPWNFPVAIFT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 177 WKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQS 256
Cdd:cd07083 173 GMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 257 AS------ASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAP 330
Cdd:cd07083 253 AArlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 331 GSPLDERTLMGPLANRQQYDKVLRLIQTARDEGdTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYR 410
Cdd:cd07083 333 GPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 411 SEE--EALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTF--LDPAVPFGGMKGSGIGREFGSA-FIDDYT 485
Cdd:cd07083 412 DDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITgaLVGVQPFGGFKLSGTNAKTGGPhYLRRFL 491
|
....*
gi 1460872063 486 ELKSV 490
Cdd:cd07083 492 EMKAV 496
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
55-482 |
7.26e-72 |
|
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: 234.47 E-value: 7.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 55 QADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMlELdqsvaflryfAGWAGKVt 134
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQT-EV----------AAMAGKI- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 135 getlDVSLPSM---AGEKYT------AFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVA 205
Cdd:cd07095 69 ----DISIKAYherTGERATpmaqgrAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 206 ELAKAVGIPDGVINVVNGaGGEIAQRLITHPACAKVSFTGSVATGEKV-QQSASASGKRVTLELGGKNAALFLDDLTPEA 284
Cdd:cd07095 145 ELWEEAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLhRQFAGRPGKILALEMGGNNPLVVWDVADIDA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 285 MVNGIIEAGYLNQGQICAAAERFYLPQGKL-DAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRLIQTARDEG 363
Cdd:cd07095 224 AAYLIVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 364 DTIVCGGEALPGEGYFLQPTAVKVrSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSE 443
Cdd:cd07095 304 GEPLLAMERLVAGTAFLSPGIIDV-TDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLA 382
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1460872063 444 AIEAGIV-WVNMHTFLDPAVPFGGMKGSGIGREFGSAFID 482
Cdd:cd07095 383 RIRAGIVnWNRPTTGASSTAPFGGVGLSGNHRPSAYYAAD 422
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
37-475 |
2.65e-71 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 233.99 E-value: 2.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 37 INPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMlEL 116
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-EV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 117 DQSVAFLRYFA--GWAGKVTGETLDvslpsmagEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPS 194
Cdd:PRK13968 91 AKSANLCDWYAehGPAMLKAEPTLV--------ENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 195 EYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQrLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAA 274
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 275 LFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLR 354
Cdd:PRK13968 242 IVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 355 LIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDN 434
Cdd:PRK13968 322 QVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTD 401
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1460872063 435 IRQALRYSEAIEAGIVWVNMHTFLDPAVPFGGMKGSGIGRE 475
Cdd:PRK13968 402 ETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRE 442
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
36-473 |
4.34e-69 |
|
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: 227.69 E-value: 4.34e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAF---SQWreMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLAR 112
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFldrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 113 mLELDQSVAFLRYFAGWAGKVTGETLDVSLpSMAGEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLK 192
Cdd:cd07148 81 -VEVTRAIDGVELAADELGQLGGREIPMGL-TPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 193 PSEYTPLTLLRVAELAKAVGIPDGVINVVnGAGGEIAQRLITHPACAKVSFTGSVATGEKVQqSASASGKRVTLELGGKN 272
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAV-PCENAVAEKLVTDPRVAFFSFIGSARVGWMLR-SKLAPGTRCALEHGGAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 273 AALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKV 352
Cdd:cd07148 237 PVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 353 LRLIQTARDEGDTIVCGGEALPGEGYflQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWS 432
Cdd:cd07148 317 EEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFT 394
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1460872063 433 DNIRQALRYSEAIEAGIVWVNMHT-FLDPAVPFGGMKGSGIG 473
Cdd:cd07148 395 KDLDVALKAVRRLDATAVMVNDHTaFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
78-492 |
3.23e-64 |
|
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: 214.31 E-value: 3.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 78 RGALLLKLADTLAEHREALAqlESLCS--GKTITLARMLE----LDQSVAFLRYFAGWAgkvtgETLDVSLPSMAGEkYT 151
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIA--AALYAdlGKPPAEAYLTEiavvLGEIDHALKHLKKWM-----KPRRVSVPLLLQP-AK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 152 AFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTllrVAELAKAVG--IPDGVINVVNGaGGEIA 229
Cdd:cd07087 94 AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPAT---SALLAKLIPkyFDPEAVAVVEG-GVEVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 230 QRLITHPAcAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYL 309
Cdd:cd07087 170 TALLAEPF-DHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 310 PQGKLDAVLALLKDKLSAFAPGSPLDERTLmGPLANRQQYDKVLRLIqtardEGDTIVCGGEALPGEGYFlQPTAVKVRS 389
Cdd:cd07087 249 HESIKDELIEELKKAIKEFYGEDPKESPDY-GRIINERHFDRLASLL-----DDGKVVIGGQVDKEERYI-APTILDDVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 390 EESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVN---MHtFLDPAVPFGG 466
Cdd:cd07087 322 PDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdvlLH-AAIPNLPFGG 400
|
410 420
....*....|....*....|....*.
gi 1460872063 467 MKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07087 401 VGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
6-473 |
3.98e-63 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 222.00 E-value: 3.98e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 6 LLAEVTAFLRQphgQFIAGQREAGRGAPFAVINPA-TGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLK 84
Cdd:PRK11904 539 LAAAIAAFLEK---QWQAGPIINGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILER 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 85 LADTLAEHRE---ALAQLESlcsGKTITLArMLELDQSVAFLRYFAGWAGKVTGETldVSLPSMAGEkyTAFTRRQPLGV 161
Cdd:PRK11904 616 AADLLEANRAeliALCVREA---GKTLQDA-IAEVREAVDFCRYYAAQARRLFGAP--EKLPGPTGE--SNELRLHGRGV 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 162 VVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKV 241
Cdd:PRK11904 688 FVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGV 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 242 SFTGSVATGEKVQQS-ASASGKRVTL--ELGGKNA------ALflddltPEAMVNGIIEAGYLNQGQICAAAERFYLPQG 312
Cdd:PRK11904 768 AFTGSTETARIINRTlAARDGPIVPLiaETGGQNAmivdstAL------PEQVVDDVVTSAFRSAGQRCSALRVLFVQED 841
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 313 KLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGdTIVCGGEaLPGE---GYFLQPTAVKVRS 389
Cdd:PRK11904 842 IADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREA-RLLAQLP-LPAGtenGHFVAPTAFEIDS 919
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 390 EEstLMREETFGPVCSFIGYRSEE--EALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFldPAV----P 463
Cdd:PRK11904 920 IS--QLEREVFGPILHVIRYKASDldKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQI--GAVvgvqP 995
|
490
....*....|
gi 1460872063 464 FGGMKGSGIG 473
Cdd:PRK11904 996 FGGQGLSGTG 1005
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
19-480 |
1.79e-62 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 211.36 E-value: 1.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 19 GQFIAGQREAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQ 98
Cdd:PRK09457 2 TLWINGDWIAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 99 LESLCSGKTITLARMlELdQSVaflryfagwAGKV----------TGETLDvslPSMAGekyTAFTRRQPLGVVVGIVPW 168
Cdd:PRK09457 82 VIARETGKPLWEAAT-EV-TAM---------INKIaisiqayherTGEKRS---EMADG---AAVLRHRPHGVVAVFGPY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 169 NFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGaGGEIAQRLITHPACAKVSFTGSVA 248
Cdd:PRK09457 145 NFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSAN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 249 TGEKV-QQSASASGKRVTLELGGKNaALFLDDLTP-EAMVNGIIEAGYLNQGQICAAAERFYLPQGKL-DAVLALLKDKL 325
Cdd:PRK09457 224 TGYLLhRQFAGQPEKILALEMGGNN-PLVIDEVADiDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 326 SAFAPGSPLDERT-LMGPLANRQQYDKVLRLIQtardegDTIVCGGEAL-------PGEGyFLQP-----TAVKVRSEes 392
Cdd:PRK09457 303 KRLTVGRWDAEPQpFMGAVISEQAAQGLVAAQA------QLLALGGKSLlemtqlqAGTG-LLTPgiidvTGVAELPD-- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 393 tlmrEETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIV-WVNMHTFLDPAVPFGGMKGSG 471
Cdd:PRK09457 374 ----EEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASG 449
|
....*....
gi 1460872063 472 IGREfgSAF 480
Cdd:PRK09457 450 NHRP--SAY 456
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
36-494 |
1.29e-61 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 211.91 E-value: 1.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMlE 115
Cdd:PLN02419 133 VINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG-D 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 116 LDQSVAFLRYFAGWAGKVTGETLdvslPSMAGEKYTaFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSE 195
Cdd:PLN02419 212 IFRGLEVVEHACGMATLQMGEYL----PNVSNGVDT-YSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 196 YTPLTLLRVAELAKAVGIPDGVINVVNGAgGEIAQRLITHPACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAAL 275
Cdd:PLN02419 287 KDPGASVILAELAMEAGLPDGVLNIVHGT-NDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 276 FLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLpQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRL 355
Cdd:PLN02419 366 VLPDANIDATLNALLAAGFGAAGQRCMALSTVVF-VGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 356 IQTARDEGDTIVCGGE--ALPG--EGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVW 431
Cdd:PLN02419 445 IQSGVDDGAKLLLDGRdiVVPGyeKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIF 524
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1460872063 432 SDNIRQALRYSEAIEAGIVWVNMHTFLD-PAVPFGGMKGSGIG--REFGSAFIDDYTELKSVMVRY 494
Cdd:PLN02419 525 TSSGAAARKFQMDIEAGQIGINVPIPVPlPFFSFTGNKASFAGdlNFYGKAGVDFFTQIKLVTQKQ 590
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
22-471 |
6.26e-58 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 200.40 E-value: 6.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 22 IAGQREAGRGAPFAVINPAT-GRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLA-EHREALAQL 99
Cdd:TIGR01236 36 IGGEEVYDSNERIPQVNPHNhQAVLAKATNATEEDAMKAVEAALDAKKDWSNLPFYDRAAIFLKAADLLSgPYRYEILAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 100 ESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGETlDVSLPsmaGEKYTAFTRrqPL-GVVVGIVPWNFSIMIAIWK 178
Cdd:TIGR01236 116 TMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQ-PISAP---GEWNRTEYR--PLeGFVYAISPFNFTAIAGNLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 179 LAAALVcGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVAT-GEKVQQSA 257
Cdd:TIGR01236 190 GAPALM-GNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTfKHLWKKVA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 258 SASGK-----RVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGS 332
Cdd:TIGR01236 269 QNLDRyhnfpRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 333 PLDERTLMGPLANRQQYDKVLRLIQTARD--EGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYR 410
Cdd:TIGR01236 349 PDDFRGFMGAVIDEQSFDKIVKYIEDAKKdpEALTILYGGKYDDSQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVYVYP 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460872063 411 SE--EEALARM-NASPYGLAASVWSDNiRQALRYSEAI---EAGIVWVNmhtflDP---AV----PFGGMKGSG 471
Cdd:TIGR01236 429 DDkyKEILDLVdSTSQYGLTGAVFAKD-RKAILEADKKlrfAAGNFYIN-----DKctgAVvgqqPFGGARMSG 496
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
64-492 |
2.67e-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: 193.47 E-value: 2.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 64 RQAFSQWReMPTLA-RGALLLKLADTLAEHREALAQ-----------LESLcsgktitlarMLELDQSVAFLRY----FA 127
Cdd:cd07133 8 KAAFLANP-PPSLEeRRDRLDRLKALLLDNQDALAEaisadfghrsrHETL----------LAEILPSIAGIKHarkhLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 128 GWAgKVtgETLDVSLPSMAGekyTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAEL 207
Cdd:cd07133 77 KWM-KP--SRRHVGLLFLPA---KAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 208 AKAVGIPDgVINVVNGaGGEIAQR--------LIthpacakvsFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDD 279
Cdd:cd07133 151 LAEYFDED-EVAVVTG-GADVAAAfsslpfdhLL---------FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 280 LTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPL-DERTlmgPLANRQQYDKVLRLIQT 358
Cdd:cd07133 220 ADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADnPDYT---SIINERHYARLQGLLED 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 359 ARDEGDTIV-CGGEA-LPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIR 436
Cdd:cd07133 297 ARAKGARVIeLNPAGeDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKA 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460872063 437 QALRYSEAIEAGIVWVN---MHTFLDPAvPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07133 377 EQDRVLRRTHSGGVTINdtlLHVAQDDL-PFGGVGASGMGAYHGKEGFLTFSHAKPVFK 434
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
139-491 |
3.99e-56 |
|
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: 193.21 E-value: 3.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 139 DVSLPSMAGekyTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAvGIPDGVI 218
Cdd:cd07135 92 DGPLAFMFG---KPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPK-YLDPDAF 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 219 NVVNGAGGEiAQRLITHPaCAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQG 298
Cdd:cd07135 168 QVVQGGVPE-TTALLEQK-FDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 299 QICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTlMGPLANRQQYDKVLRLIQTARDEgdtIVCGGEALPGEgY 378
Cdd:cd07135 246 QICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPD-YTRIVNPRHFNRLKSLLDTTKGK---VVIGGEMDEAT-R 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 379 FLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVN---MH 455
Cdd:cd07135 321 FIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdtlIH 400
|
330 340 350
....*....|....*....|....*....|....*.
gi 1460872063 456 TFLDPAvPFGGMKGSGIGREFGSAFIDDYTELKSVM 491
Cdd:cd07135 401 VGVDNA-PFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
26-492 |
4.40e-55 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 191.89 E-value: 4.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 26 REAGRGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSG 105
Cdd:PLN00412 25 RTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 106 KTITLARMlELDQSVAFLRYFAGWAGKVTGE---TLDVSLPSMAGEKYtAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAA 182
Cdd:PLN00412 105 KPAKDAVT-EVVRSGDLISYTAEEGVRILGEgkfLVSDSFPGNERNKY-CLTSKIPLGVVLAIPPFNYPVNLAVSKIAPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 183 LVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSvATGEKVQQSASASGk 262
Cdd:PLN00412 183 LIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISKKAGMVP- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 263 rVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMgP 342
Cdd:PLN00412 261 -LQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDIT-P 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 343 LANRQQYDKVLRLIQTARDEGDTIVcggEALPGEGYFLQPTAV-KVRSEestlMR---EETFGPVCSFIGYRSEEEALAR 418
Cdd:PLN00412 339 VVSESSANFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLdNVRPD----MRiawEEPFGPVLPVIRINSVEEGIHH 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460872063 419 MNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFLDP-AVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:PLN00412 412 CNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQGITNSINMMTKVKSTVI 486
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
36-480 |
9.82e-55 |
|
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: 190.89 E-value: 9.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 36 VINPATGRAI-AEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLArML 114
Cdd:TIGR01238 55 VTNPADRRDIvGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNA-IA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 115 ELDQSVAFLRYFAGWAGKVTGEtldvslpsmagekytaFTRRqPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPS 194
Cdd:TIGR01238 134 EVREAVDFCRYYAKQVRDVLGE----------------FSVE-SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 195 EYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQS-ASASGKRVTL--ELGGK 271
Cdd:TIGR01238 197 EQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTlAQREDAPVPLiaETGGQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 272 NAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDK 351
Cdd:TIGR01238 277 NAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQN 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 352 VLRLIQTARDEGDTI---VCGGEALPGEGYFLQPTAVKVRSEEStlMREETFGPVCSFIGYRSEE--EALARMNASPYGL 426
Cdd:TIGR01238 357 LLAHIEHMSQTQKKIaqlTLDDSRACQHGTFVAPTLFELDDIAE--LSEEVFGPVLHVVRYKAREldQIVDQINQTGYGL 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1460872063 427 AASVWSDNIRQALRYSEAIEAGIVWVNMHTFldPAV----PFGGMKGSGIGREFGSAF 480
Cdd:TIGR01238 435 TMGVHSRIETTYRWIEKHARVGNCYVNRNQV--GAVvgvqPFGGQGLSGTGPKAGGPH 490
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
3-478 |
1.31e-54 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 190.82 E-value: 1.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 3 EITLLAEVTAFLRQPhGQFIAGQREAGrGAPFAVINPATGRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALL 82
Cdd:PLN02315 7 EYEFLSEIGLSSRNL-GCYVGGEWRAN-GPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 83 LKLADTLAEHREALAQLESLCSGKtITLARMLELDQSVAFLRYFAGWAGKVTGETLDVSLPS-MAGEKYtaftrrQPLGV 161
Cdd:PLN02315 85 RQIGDALRAKLDYLGRLVSLEMGK-ILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNhMMMEVW------NPLGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 162 VVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAV----GIPDGVINVVNGaGGEIAQRLITHPA 237
Cdd:PLN02315 158 VGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 238 CAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAV 317
Cdd:PLN02315 237 IPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 318 LALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGEALPGEGYFLQPTAVKVrSEESTLMRE 397
Cdd:PLN02315 317 LEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVEI-SPDADVVKE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 398 ETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRY--SEAIEAGIVWVNMHTF-LDPAVPFGGMKGSGIGR 474
Cdd:PLN02315 396 ELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWigPLGSDCGIVNVNIPTNgAEIGGAFGGEKATGGGR 475
|
....
gi 1460872063 475 EFGS 478
Cdd:PLN02315 476 EAGS 479
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
42-481 |
2.03e-54 |
|
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: 190.49 E-value: 2.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 42 GRAIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLA-EHREALAQLESLCSGKTITLArmlELD--- 117
Cdd:cd07123 57 AHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQGKNVWQA---EIDaac 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 118 QSVAFLRYFAGWAGKVTGETLDVSLPSMagekyTAFTRRQPL-GVVVGIVPWNFSIMIAIWKLAAALVcGCTIVLKPSEY 196
Cdd:cd07123 134 ELIDFLRFNVKYAEELYAQQPLSSPAGV-----WNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 197 TPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASA------SGKRVTLELGG 270
Cdd:cd07123 208 AVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGEnldryrTYPRIVGETGG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 271 KNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYD 350
Cdd:cd07123 288 KNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFD 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 351 KVLRLIQTAR-DEGDTIVCGGEALPGEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSE--EEALARMN-ASPYGL 426
Cdd:cd07123 368 RIKGYIDHAKsDPEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSdfEETLELVDtTSPYAL 447
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460872063 427 AASVWSDN---IRQA---LRYSeaieAGIVWVNmhtflDP---AV----PFGGMKGSGIGREFGSAFI 481
Cdd:cd07123 448 TGAIFAQDrkaIREAtdaLRNA----AGNFYIN-----DKptgAVvgqqPFGGARASGTNDKAGSPLN 506
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
6-473 |
5.04e-54 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 195.93 E-value: 5.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 6 LLAEVTAFLRQPH--GQFIAGQREAGRGAPfaVINPATGR-AIAEVTAADSDQADRAMESARQAFSQWREMPTLARGALL 82
Cdd:COG4230 544 LSAALAAAAEKQWqaAPLIAGEAASGEARP--VRNPADHSdVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAIL 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 83 LKLADTLAEHRE---ALAQLESlcsGKTITLArMLELDQSVAFLRYFAGwagkvtgetldvslpsMAGEKYTAFTRRQPL 159
Cdd:COG4230 622 ERAADLLEAHRAelmALLVREA---GKTLPDA-IAEVREAVDFCRYYAA----------------QARRLFAAPTVLRGR 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 160 GVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACA 239
Cdd:COG4230 682 GVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIA 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 240 KVSFTGSVATGEKVQQS-ASASGKRVTL--ELGGKNA------ALflddltPEAMVNGIIEAGYLNQGQICAAAERFYLP 310
Cdd:COG4230 762 GVAFTGSTETARLINRTlAARDGPIVPLiaETGGQNAmivdssAL------PEQVVDDVLASAFDSAGQRCSALRVLCVQ 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 311 QGKLDAVLALLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTI-VCGGEALPGEGYFLQPTAVKVRS 389
Cdd:COG4230 836 EDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLIEIDS 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 390 EEStlMREETFGPVCSFIGYRSEE--EALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVN--MHTfldpAV--- 462
Cdd:COG4230 916 ISD--LEREVFGPVLHVVRYKADEldKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNrnIIG----AVvgv 989
|
490
....*....|..
gi 1460872063 463 -PFGGMKGSGIG 473
Cdd:COG4230 990 qPFGGEGLSGTG 1001
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
57-492 |
4.15e-50 |
|
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: 177.03 E-value: 4.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 57 DRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAqlESLC-----SGKTITLARMLELDQSVAF-LRYFAGWA 130
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEII--AALAadfrkPAAEVDLTEILPVLSEINHaIKHLKKWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 131 GKVtgetlDVSLP-SMAGEKytAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAK 209
Cdd:cd07134 79 KPK-----RVRTPlLLFGTK--SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 210 AVGIPDGViNVVNGaGGEIAQRLITHPAcAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGI 289
Cdd:cd07134 152 EAFDEDEV-AVFEG-DAEVAQALLELPF-DHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 290 IEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTL-MGPLANRQQYDKVLRLIQTARDEGDTIVC 368
Cdd:cd07134 229 AWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPdLARIVNDRHFDRLKGLLDDAVAKGAKVEF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 369 GGEALPGEGYFlQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAG 448
Cdd:cd07134 309 GGQFDAAQRYI-APTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSG 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1460872063 449 IVWVN---MHtFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMV 492
Cdd:cd07134 388 GVVVNdvvLH-FLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVLR 433
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
31-473 |
5.86e-50 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 183.91 E-value: 5.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 31 GAPFAVINPATGRAI-AEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTIT 109
Cdd:PRK11905 566 GGTRPVLNPADHDDVvGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLA 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 110 LArMLELDQSVAFLRYFAGWAgkvtgetldvslpsmagEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTI 189
Cdd:PRK11905 646 NA-IAEVREAVDFLRYYAAQA-----------------RRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTV 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 190 VLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQS-ASASGKRVTL-- 266
Cdd:PRK11905 708 LAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTlAKRSGPPVPLia 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 267 ELGGKNA------ALflddltPEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLM 340
Cdd:PRK11905 788 ETGGQNAmivdssAL------PEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDV 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 341 GPLANRQQYDKVLRLIQTARDEGDTI-VCGGEALPGEGYFLQPTAVKVRSEEStlMREETFGPVCSFIGYRSEE--EALA 417
Cdd:PRK11905 862 GPVIDAEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLIEIDSISD--LEREVFGPVLHVVRFKADEldRVID 939
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 418 RMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVNMHTFldPAV----PFGGMKGSGIG 473
Cdd:PRK11905 940 DINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNII--GAVvgvqPFGGEGLSGTG 997
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
64-493 |
1.21e-48 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 174.45 E-value: 1.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 64 RQAFSQWREMPTLARGALLLKLADTLAEHREAL--AQLESLcsGKTITLARMLELDQSVA----FLRYFAGWAGKVTGET 137
Cdd:PTZ00381 17 KESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFseAVHKDL--GRHPFETKMTEVLLTVAeiehLLKHLDEYLKPEKVDT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 138 LDVSLPSmagekyTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVgIPDGV 217
Cdd:PTZ00381 95 VGVFGPG------KSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 218 INVVNGaGGEIAQRLITHPAcAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQ 297
Cdd:PTZ00381 168 VRVIEG-GVEVTTELLKEPF-DHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 298 GQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLmGPLANRQQYDKVLRLIQtarDEGDTIVCGGEALPGEG 377
Cdd:PTZ00381 246 GQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDY-SRIVNEFHTKRLAELIK---DHGGKVVYGGEVDIENK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 378 YfLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVN---M 454
Cdd:PTZ00381 322 Y-VAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcvF 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 1460872063 455 HtFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMVR 493
Cdd:PTZ00381 401 H-LLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
152-491 |
1.39e-46 |
|
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: 167.68 E-value: 1.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 152 AFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVgIPDGVINVVNGaGGEIAQR 231
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 232 LITHPAcAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYLPQ 311
Cdd:cd07136 172 LLDQKF-DYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 312 GKLDAVLALLKDKLSAFAPGSPLDERTlMGPLANRQQYDKVLRLIqtardEGDTIVCGGEALPGEGYFlQPTAVKVRSEE 391
Cdd:cd07136 251 SVKEKFIKELKEEIKKFYGEDPLESPD-YGRIINEKHFDRLAGLL-----DNGKIVFGGNTDRETLYI-EPTILDNVTWD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 392 STLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVN---MHtFLDPAVPFGGMK 468
Cdd:cd07136 324 DPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtiMH-LANPYLPFGGVG 402
|
330 340
....*....|....*....|...
gi 1460872063 469 GSGIGREFGSAFIDDYTELKSVM 491
Cdd:cd07136 403 NSGMGSYHGKYSFDTFSHKKSIL 425
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
21-434 |
4.97e-41 |
|
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: 153.96 E-value: 4.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 21 FIAGQREAGRGAPFAVINPATGRAIAEVTAADSDQADrAMESARQAFSQ-WREMPTLARGALLLKLADTLAEHREALAQL 99
Cdd:cd07128 4 YVAGQWHAGTGDGRTLHDAVTGEVVARVSSEGLDFAA-AVAYAREKGGPaLRALTFHERAAMLKALAKYLMERKEDLYAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 100 eSLCSGKTITLArMLELDQSVAFLRYFAGWAGK--------VTGETLDVSlpsmageKYTAFTRRQPL----GVVVGIVP 167
Cdd:cd07128 83 -SAATGATRRDS-WIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPLS-------KDGTFVGQHILtprrGVAVHINA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 168 WNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGI-PDGVINVVNGAGGEIAQRLiTHPACakVSFTGS 246
Cdd:cd07128 154 FNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHL-GEQDV--VAFTGS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 247 VATGEKVQQSAS--ASGKRVTLELGGKNAALFLDDLTP-----EAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLA 319
Cdd:cd07128 231 AATAAKLRAHPNivARSIRFNAEADSLNAAILGPDATPgtpefDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 320 LLKDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGE------ALPGEGYFLQPTAVKVRS-EES 392
Cdd:cd07128 311 ALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDrfevvgADAEKGAFFPPTLLLCDDpDAA 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1460872063 393 TLMRE-ETFGPVCSFIGYRSEEEA--LARM-NASpygLAASVWSDN 434
Cdd:cd07128 391 TAVHDvEAFGPVATLMPYDSLAEAieLAARgRGS---LVASVVTND 433
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
22-473 |
9.71e-41 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 156.67 E-value: 9.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 22 IAGQREAGRGAPfaVINPATGRAI-AEVTAADSDQADRAMESARQAFSQWREMPTLARGALLLKLADtLAEhrealAQLE 100
Cdd:PRK11809 651 LEDPVAAGEMSP--VINPADPRDIvGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAAD-LME-----AQMQ 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 101 SLC------SGKTITLArMLELDQSVAFLRYFAGwagkvtgetldvslpsMAGEKYTAFTRRqPLGVVVGIVPWNFSIMI 174
Cdd:PRK11809 723 TLMgllvreAGKTFSNA-IAEVREAVDFLRYYAG----------------QVRDDFDNDTHR-PLGPVVCISPWNFPLAI 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 175 AIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQ 254
Cdd:PRK11809 785 FTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQ 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 255 QSAS----ASGKRVTL--ELGGKNaALFLDD--LTpEAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALLKDKLS 326
Cdd:PRK11809 865 RNLAgrldPQGRPIPLiaETGGQN-AMIVDSsaLT-EQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMA 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 327 AFAPGSPldER--TLMGPLANRQQYDKVLRLIQTARDEGDTI---VCGGEALPGEGYFLQPTAVKVRSEEStlMREETFG 401
Cdd:PRK11809 943 ECRMGNP--DRlsTDIGPVIDAEAKANIERHIQAMRAKGRPVfqaARENSEDWQSGTFVPPTLIELDSFDE--LKREVFG 1018
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 402 PVCSFIGYRSEE--EALARMNASPYGLAASVWS---DNIRQAlrySEAIEAGIVWVNMHtfLDPAV----PFGGMKGSGI 472
Cdd:PRK11809 1019 PVLHVVRYNRNQldELIEQINASGYGLTLGVHTridETIAQV---TGSAHVGNLYVNRN--MVGAVvgvqPFGGEGLSGT 1093
|
.
gi 1460872063 473 G 473
Cdd:PRK11809 1094 G 1094
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
157-492 |
2.47e-39 |
|
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: 147.56 E-value: 2.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 157 QPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTllrVAELAKAVG--IPDGVINVVNGaGGEIAQRLIT 234
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPAT---SALLAKLIPeyLDTKAIKVIEG-GVPETTALLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 235 HpACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGY-LNQGQICAAAERFYLPQGK 313
Cdd:cd07137 176 Q-KWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESF 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 314 LDAVLALLKDKLSAFAPGSPLdERTLMGPLANRQQYDKVLRLIQTARDEgDTIVCGGEaLPGEGYFLQPTAVKVRSEEST 393
Cdd:cd07137 255 APTLIDALKNTLEKFFGENPK-ESKDLSRIVNSHHFQRLSRLLDDPSVA-DKIVHGGE-RDEKNLYIEPTILLDPPLDSS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 394 LMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVN--MHTFLDPAVPFGGMKGSG 471
Cdd:cd07137 332 IMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdtVVQYAIDTLPFGGVGESG 411
|
330 340
....*....|....*....|.
gi 1460872063 472 IGREFGSAFIDDYTELKSVMV 492
Cdd:cd07137 412 FGAYHGKFSFDAFSHKKAVLY 432
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
21-434 |
3.52e-39 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 149.08 E-value: 3.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 21 FIAGQREAGRGAPFAVINPATGRAIAEVTAADSDQAdRAMESAR-QAFSQWREMPTLARGALLLKLADTLAEHREALAQL 99
Cdd:PRK11903 8 YVAGRWQAGSGAGTPLFDPVTGEELVRVSATGLDLA-AAFAFAReQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 100 ESLCSGKTITLARmLELDQSVAFLRYFAGWaGKVTGETL------DVSL---PSMAGEKYTAFTRrqplGVVVGIVPWNF 170
Cdd:PRK11903 87 ATANSGTTRNDSA-VDIDGGIFTLGYYAKL-GAALGDARllrdgeAVQLgkdPAFQGQHVLVPTR----GVALFINAFNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 171 SIMiAIW-KLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGI-PDGVINVVNGAGGEIAQRLithPACAKVSFTGSVA 248
Cdd:PRK11903 161 PAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHL---QPFDVVSFTGSAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 249 TGEKVQQSAS--ASGKRVTLELGGKNAALFLDDLTP-----EAMVNGIIEAGYLNQGQICAAAERFYLPQGKLDAVLALL 321
Cdd:PRK11903 237 TAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAAPgseafDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 322 KDKLSAFAPGSPLDERTLMGPLANRQQYDKVLRLIQTARDEGDTIVCGGE-----ALPGEGYFLQPTAVKVR-SEESTLM 395
Cdd:PRK11903 317 AARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGfalvdADPAVAACVGPTLLGASdPDAATAV 396
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1460872063 396 RE-ETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDN 434
Cdd:PRK11903 397 HDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
151-493 |
1.65e-37 |
|
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: 142.75 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 151 TAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELakavgIPDGVIN----VVNGaGG 226
Cdd:cd07132 93 DVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLDKecypVVLG-GV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 227 EIAQRLITHpACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAER 306
Cdd:cd07132 167 EETTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 307 FYLPQGKLDAVLALLKDKLSAFAPGSPLDERTLmGPLANRQQYDKVLRLIqtardEGDTIVCGGEALPGEGYfLQPTAVK 386
Cdd:cd07132 246 VLCTPEVQEKFVEALKKTLKEFYGEDPKESPDY-GRIINDRHFQRLKKLL-----SGGKVAIGGQTDEKERY-IAPTVLT 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 387 VRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVN---MHTFLDpAVP 463
Cdd:cd07132 319 DVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNdtiMHYTLD-SLP 397
|
330 340 350
....*....|....*....|....*....|
gi 1460872063 464 FGGMKGSGIGREFGSAFIDDYTELKSVMVR 493
Cdd:cd07132 398 FGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
58-479 |
4.55e-31 |
|
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: 124.66 E-value: 4.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 58 RAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGKTITLARMLELDQSVAFLRYFAGWAGKVTGET 137
Cdd:cd07084 3 RALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPHEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 138 LDvSLPSmaGEKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGI-PDG 216
Cdd:cd07084 83 GN-HLGQ--GLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 217 VINVVNGAgGEIAQRLITHPACAKVSFTGSVATGEKVqqSASASGKRVTLELGGKNAA-LFLDDLTPEAMVNGIIEAGYL 295
Cdd:cd07084 160 DVTLINGD-GKTMQALLLHPNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKvLGPDAQAVDYVAWQCVQDMTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 296 NQGQICAAAERFYLPQG-KLDAVLALLKDKLSafapgspldERTLMGPLANRQQYDKVLRLIQTARDEGDTIVC-GGEAL 373
Cdd:cd07084 237 CSGQKCTAQSMLFVPENwSKTPLVEKLKALLA---------RRKLEDLLLGPVQTFTTLAMIAHMENLLGSVLLfSGKEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 374 PGEGYF-----LQPTAVKVRSEES----TLMREETFGPVCSFIGYRSEEEALA-----RMNASpygLAASVWSDNIRQAL 439
Cdd:cd07084 308 KNHSIPsiygaCVASALFVPIDEIlktyELVTEEIFGPFAIVVEYKKDQLALVlelleRMHGS---LTAAIYSNDPIFLQ 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1460872063 440 RYSEAIE-AGIVWVNM--HTFLDPA-VPFGGMKGSGIGREFGSA 479
Cdd:cd07084 385 ELIGNLWvAGRTYAILrgRTGVAPNqNHGGGPAADPRGAGIGGP 428
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
58-493 |
5.78e-31 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 125.22 E-value: 5.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 58 RAMESARQAFSQWREMPTlarGALLLKLADTLAEHREALAQleSLcsGKTITLARMLE---LDQSVAF-LRYFAGWAGKV 133
Cdd:PLN02203 17 ETYESGRTRSLEWRKSQL---KGLLRLLKDNEEAIFKALHQ--DL--GKHRVEAYRDEvgvLTKSANLaLSNLKKWMAPK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 134 TGETLDVSLPSmagekyTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTllrVAELAKAVG- 212
Cdd:PLN02203 90 KAKLPLVAFPA------TAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPAT---SAFLAANIPk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 213 -IPDGVINVVNGaGGEIAQRLITHPaCAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFlDDLTP----EAMVN 287
Cdd:PLN02203 161 yLDSKAVKVIEG-GPAVGEQLLQHK-WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIV-DSLSSsrdtKVAVN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 288 GIIEAGYLN-QGQICAAAERFYLPQGKLDAVLALLKDKLSAFAPGSPLDERTlMGPLANRQQYDKVLRLIQTARDEGdTI 366
Cdd:PLN02203 238 RIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLKDPRVAA-SI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 367 VCGGEALPgEGYFLQPTAVKVRSEESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIE 446
Cdd:PLN02203 316 VHGGSIDE-KKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETS 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1460872063 447 AGIVWVN--MHTFLDPAVPFGGMKGSGIGREFGSAFIDDYTELKSVMVR 493
Cdd:PLN02203 395 SGSVTFNdaIIQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRR 443
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
157-493 |
8.57e-30 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 121.69 E-value: 8.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 157 QPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVgIPDGVINVVNGAGGEIAQRLitHP 236
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALL--EQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 237 ACAKVSFTGSVATGEKVQQSASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEAGY-LNQGQICAAAERFYLPQGKLD 315
Cdd:PLN02174 188 KWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAP 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 316 AVLALLKDKLSAFAPGSPLDERTlMGPLANRQQYDKVLRLIQtARDEGDTIVCGGEAlPGEGYFLQPTAVKVRSEESTLM 395
Cdd:PLN02174 268 KVIDAMKKELETFYGKNPMESKD-MSRIVNSTHFDRLSKLLD-EKEVSDKIVYGGEK-DRENLKIAPTILLDVPLDSLIM 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 396 REETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSDNIRQALRYSEAIEAGIVWVN---MHTFLDpAVPFGGMKGSGI 472
Cdd:PLN02174 345 SEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiaVHLALH-TLPFGGVGESGM 423
|
330 340
....*....|....*....|.
gi 1460872063 473 GREFGSAFIDDYTELKSVMVR 493
Cdd:PLN02174 424 GAYHGKFSFDAFSHKKAVLYR 444
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
57-433 |
1.06e-28 |
|
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: 118.03 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 57 DRAMESARQAFSQWREMPTLARGALLLKLADTLAEHREALAQLESLCSGktITLARML-ELDQSVAFLRYFAGWA--GKV 133
Cdd:cd07129 2 DAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARLQgELGRTTGQLRLFADLVreGSW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 134 TGETLDVSLPSMAGEKYTAFTRRQ-PLGVVVGIVPWNF--SIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKA 210
Cdd:cd07129 80 LDARIDPADPDRQPLPRPDLRRMLvPLGPVAVFGASNFplAFSVAGGDTASALAAGCPVVVKAHPAHPGTSELVARAIRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 211 V----GIPDGVINVVNGAGGEIAQRLITHPACAKVSFTGSVATGEKVQQSASA--SGKRVTLELGGKNAALflddLTPEA 284
Cdd:cd07129 160 AlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVF----ILPGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 285 MVN--GIIEAGY-----LNQGQICAAAERFYLPQGK-LDAVLALLKDKLSAFAPGSPLDERTlmgplanRQQYDKVLRLI 356
Cdd:cd07129 236 LAErgEAIAQGFvgsltLGAGQFCTNPGLVLVPAGPaGDAFIAALAEALAAAPAQTMLTPGI-------AEAYRQGVEAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 357 QTARDeGDTIVCGGEALPGEGYflQPTAVKVRSE---ESTLMREETFGPVCSFIGYRSEEEALARMNASPYGLAASVWSD 433
Cdd:cd07129 309 AAAPG-VRVLAGGAAAEGGNQA--APTLFKVDAAaflADPALQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHGE 385
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
23-453 |
9.97e-17 |
|
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: 82.91 E-value: 9.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 23 AGQR--EAGRGAPFAVINP-ATGRAIAEVTAADSD--------QADRAMESARQAFSQWREMPTLARGALLLKLADTLAE 91
Cdd:cd07127 42 AGKAafEALLGQRFDLDQPgASGWVGGEVSPYGVElgvtypqcDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 92 HREALAQLESLCSGKTITLARML----ELDQSVAFLRYFAGWAGKVTGETLDVS----LPSMAGEK-YTAFTRRQPLGVV 162
Cdd:cd07127 122 RSFEMAHAVMHTTGQAFMMAFQAggphAQDRGLEAVAYAWREMSRIPPTAEWEKpqgkHDPLAMEKtFTVVPRGVALVIG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 163 VGIVP-WNfsimiAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAV----GI-PDGVINVVNGAGGEIAQRLITHP 236
Cdd:cd07127 202 CSTFPtWN-----GYPGLFASLATGNPVIVKPHPAAILPLAITVQVAREVlaeaGFdPNLVTLAADTPEEPIAQTLATRP 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 237 ACAKVSFTGSVATGEKVQQsaSASGKRVTLELGGKNAALF--LDDLtpEAMVNGIIEAGYLNQGQICAAAERFYLP---- 310
Cdd:cd07127 277 EVRIIDFTGSNAFGDWLEA--NARQAQVYTEKAGVNTVVVdsTDDL--KAMLRNLAFSLSLYSGQMCTTPQNIYVPrdgi 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 311 ---QGKL--DAVLALLKDKLSAFApGSPLDERTLMGPLanrqQYDKVLRLIQTARDEGDTIVCGGE----ALPGeGYFLQ 381
Cdd:cd07127 353 qtdDGRKsfDEVAADLAAAIDGLL-ADPARAAALLGAI----QSPDTLARIAEARQLGEVLLASEAvahpEFPD-ARVRT 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 382 PTAVKVRSEESTLMREETFGPVCSFIGYRSEEEA--LARMNASPYG-LAASVWSDNIRQALRYSEAIEA----------G 448
Cdd:cd07127 427 PLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSieLARESVREHGaMTVGVYSTDPEVVERVQEAALDagvalsinltG 506
|
....*
gi 1460872063 449 IVWVN 453
Cdd:cd07127 507 GVFVN 511
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
85-325 |
1.94e-09 |
|
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: 59.54 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 85 LADTLAEHREALAQLESLCSGKTIT------LARML----ELDQSVAFLRYFAGWAGKVTGETLdvslpsmaGEKYTAFT 154
Cdd:cd07077 25 IANALYDTRQRLASEAVSERGAYIRslianwIAMMGcsesKLYKNIDTERGITASVGHIQDVLL--------PDNGETYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 155 RRQPLGVVVGIVPWNFSIMiAIWKLAAALVCGCTIVLKPSEYTP-----LTLLRVAelAKAVGIPDGVINVVNGAGGEIA 229
Cdd:cd07077 97 RAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAPftnraLALLFQA--ADAAHGPKILVLYVPHPSDELA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 230 QRLITHPACAKVSFTGSVATGEKVQQsaSASGKRVtLELGGKNAALFLDDLTPEAMVNGIIEAGYLNQGQICAAAERFYL 309
Cdd:cd07077 174 EELLSHPKIDLIVATGGRDAVDAAVK--HSPHIPV-IGFGAGNSPVVVDETADEERASGSVHDSKFFDQNACASEQNLYV 250
|
250
....*....|....*.
gi 1460872063 310 PQGKLDAVLALLKDKL 325
Cdd:cd07077 251 VDDVLDPLYEEFKLKL 266
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
156-436 |
7.34e-08 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 54.81 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 156 RQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAELAKAVGIPDGVINVVNGaGGEIAQRLITH 235
Cdd:cd07126 140 RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHS-DGPTMNKILLE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 236 PACAKVSFTGSVATGEKVqqsASASGKRVTLELGGKNAALFLDDLTPEAMVNGIIEA-GYLNQGQICAAAERFYLPQGKL 314
Cdd:cd07126 219 ANPRMTLFTGSSKVAERL---ALELHGKVKLEDAGFDWKILGPDVSDVDYVAWQCDQdAYACSGQKCSAQSILFAHENWV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 315 DAVLAllkDKLSAFAPGSPLDERTLmGP---LANRQQYDKVLRLIQTardEGDTIVCGGEALPGEGY-----FLQPTAVK 386
Cdd:cd07126 296 QAGIL---DKLKALAEQRKLEDLTI-GPvltWTTERILDHVDKLLAI---PGAKVLFGGKPLTNHSIpsiygAYEPTAVF 368
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460872063 387 VRSEEST------LMREETFGPVCSFIGYRSEE-----EALARMNASpygLAASVWSDNIR 436
Cdd:cd07126 369 VPLEEIAieenfeLVTTEVFGPFQVVTEYKDEQlplvlEALERMHAH---LTAAVVSNDIR 426
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
148-302 |
2.26e-06 |
|
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: 49.96 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 148 EKYTAFTRRQPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAEL----AKAVGIPDGVINVVNG 223
Cdd:cd07081 85 ENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLllqaAVAAGAPENLIGWIDN 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 224 AGGEIAQRLITHPACAKVSFTGsvatGEKVQQSASASGKRVtLELGGKNAALFLDDLTPEAM-VNGIIEAGYLNQGQICA 302
Cdd:cd07081 165 PSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPA-IGVGAGNTPVVIDETADIKRaVQSIVKSKTFDNGVICA 239
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
157-262 |
2.72e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 46.33 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460872063 157 QPLGVVVGIVPWNFSIMIAIWKLAAALVCGCTIVLKPSEYTPLTLLRVAEL----AKAVGIPDGVINVVNGAGGEIAQRL 232
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKImreaAVAAGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110
....*....|....*....|....*....|
gi 1460872063 233 ITHPACAKVSFTGsvatGEKVQQSASASGK 262
Cdd:cd07122 174 MKHPDVDLILATG----GPGMVKAAYSSGK 199
|
|
| PRK10854 |
PRK10854 |
exopolyphosphatase; Provisional |
37-91 |
5.02e-03 |
|
exopolyphosphatase; Provisional
Pssm-ID: 182781 [Multi-domain] Cd Length: 513 Bit Score: 39.33 E-value: 5.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1460872063 37 INPATGRAIAEVTAADSDQADRAMESARQAFSQWREM-PTLARGAL--LLKLADTLAE 91
Cdd:PRK10854 314 IRSRTAKSLANHYNIDREQARRVLETTMQLYEQWREQnPKLAHPQLeaLLKWAAMLHE 371
|
|
| |
