|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
34-523 |
0e+00 |
|
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: 763.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 34 NLLSGEWLDTSKYFDnIPDPVSGEYFIDIPDT--DDLSGFIQNLDICPKSGLHNPIKNVERYVMLGNVCAKAAALLSNKE 111
Cdd:cd07126 1 NLVAGKWKGASNYTT-LLDPLNGDKFISVPDTdeDEINEFVDSLRQCPKSGLHNPLKNPERYLLYGDVSHRVAHELRKPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 112 VEDFFVHLIQRVMPKSSNQCLGEVTVTRKFLENFSGDGVRFLARSFSNPGDHLGQESSGYRWPFGSVVIVAPFNFPLEIP 191
Cdd:cd07126 80 VEDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLARSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 192 ALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISAAsdKIRMVQFTGSCAVAERIA 271
Cdd:cd07126 160 ALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEA--NPRMTLFTGSSKVAERLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 272 ADTNGKVRVEDAGFNWKLIGPDYdpSWSDYVAWQCDEDAYNASGQKCSAQSILFVHKNW-EQDLLLKLKQLAERRKLENL 350
Cdd:cd07126 238 LELHGKVKLEDAGFDWKILGPDV--SDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWvQAGILDKLKALAEQRKLEDL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 351 SIGPVLTWNNDQLFNHINSLLEIPGTTCLFGGTELESHNIPKIYGSIKPTAVSIPVNQLL-GKDFELITSEVFGPVQVIV 429
Cdd:cd07126 316 TIGPVLTWTTERILDHVDKLLAIPGAKVLFGGKPLTNHSIPSIYGAYEPTAVFVPLEEIAiEENFELVTTEVFGPFQVVT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 430 VYEDQDLPTIMEALEKIPQNLTAAVVSNDVHFQQKVLGYTVNGTTYAGMRARTTGAPQNHWFGPSGDPRSAGIGTPEAIT 509
Cdd:cd07126 396 EYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTYAGIRARTTGAPQNHWFGPAGDPRGAGIGTPEAIR 475
|
490
....*....|....
gi 167041430 510 LTWSGHREIIKDVG 523
Cdd:cd07126 476 LVWSCHREIITDIG 489
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
90-519 |
2.83e-108 |
|
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: 330.35 E-value: 2.83e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 90 VERYVMLGNVCAKAAALLSNKEVEDFFVHLIQRVMPKSSNQCLGEVTVTRK---FLENFSGDGVRFLARSF--------S 158
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKgwmFAENICGDQVQLRARAFviysyripH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 159 NPGDHLGQ----ESSGYRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCG-LPATD 233
Cdd:cd07084 81 EPGNHLGQglkqQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 234 ADMVHCRGSKMGKLISAAsdKIRMVQFTGSCAVAERIAADTN-GKVRVEDAGFNWKLIGPDYDPswSDYVAWQCDEDAYN 312
Cdd:cd07084 161 VTLINGDGKTMQALLLHP--NPKMVLFTGSSRVAEKLALDAKqARIYLELAGFNWKVLGPDAQA--VDYVAWQCVQDMTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 313 ASGQKCSAQSILFVHKNWEQDLL-LKLKQLAERRKLENLSIGPVLTWNNDQLFNHINSLLeipGTTCLFGGTELESHNIP 391
Cdd:cd07084 237 CSGQKCTAQSMLFVPENWSKTPLvEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMENLL---GSVLLFSGKELKNHSIP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 392 KIYGSIKPTAVSIPVNQLLgKDFELITSEVFGPVQVIVVYEDQDLPTIMEALEKIPQNLTAAVVSND-VHFQQKVLGYTV 470
Cdd:cd07084 314 SIYGACVASALFVPIDEIL-KTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDpIFLQELIGNLWV 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 167041430 471 NGTTYAGMRARTTGAP-QNHWFGPSGDPRSAGIGTPEAITLTWSGHREII 519
Cdd:cd07084 393 AGRTYAILRGRTGVAPnQNHGGGPAADPRGAGIGGPEAIKLVWRCHAEQA 442
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
97-508 |
2.35e-56 |
|
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: 194.73 E-value: 2.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 97 GNVCAKAAALLsnKEVEDFFVHLIQRVMPKSSNQCLGEVTVTRKFLENFSGDGVRFLARSFSNPgdHLGQESSGYRWPFG 176
Cdd:cd07078 23 AAILRKLADLL--EERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSP--DPGELAIVRREPLG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 177 SVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLIsAASDKIR 256
Cdd:cd07078 99 VVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAAL-ASHPRVD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 257 MVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDPswsDYVAWQCDEDAYNASGQKCSAQSILFVHKNWEQD 333
Cdd:cd07078 178 KISFTGSTAVGKAImraAAENLKRVTLELGGKSPLIVFDDADL---DAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 334 LLLKLKQLAERRKLENLS-----IGPVLtwnNDQLFNHINSLLEI---PGTTCLFGGTELESHNIPKiygsIKPTAVSIP 405
Cdd:cd07078 255 FVERLVERVKALKVGNPLdpdtdMGPLI---SAAQLDRVLAYIEDakaEGAKLLCGGKRLEGGKGYF----VPPTVLTDV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 406 vnqllGKDFELITSEVFGPVQVIVVYEDQDlptimEALEKI---PQNLTAAVVSNDVHFQQKVLGYTVNGTTYAGMRART 482
Cdd:cd07078 328 -----DPDMPIAQEEIFGPVLPVIPFKDEE-----EAIELAndtEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVG 397
|
410 420
....*....|....*....|....*..
gi 167041430 483 TGAPQNHW-FGPSGDPRSAGigtPEAI 508
Cdd:cd07078 398 AEPSAPFGgVKQSGIGREGG---PYGL 421
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
97-509 |
2.48e-42 |
|
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: 155.08 E-value: 2.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 97 GNVCAKAAALLsnKEVEDFFVHLIQRVMPKSSNQCLGEVTVTRKFLENFSGDGVRFLARSFsnPGDHLGQESSGYRWPFG 176
Cdd:cd06534 19 AAILRKIADLL--EERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPEL--PSPDPGGEAYVRREPLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 177 SVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLIsAASDKIR 256
Cdd:cd06534 95 VVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAAL-LSHPRVD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 257 MVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDPswsDYVAWQCDEDAYNASGQKCSAQSILFVHKNweqd 333
Cdd:cd06534 174 KISFTGSTAVGKAImkaAAENLKPVTLELGGKSPVIVDEDADL---DAAVEGAVFGAFFNAGQICTAASRLLVHES---- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 334 lllklkqlaerrklenlsigpvltwnndqlfnhinslleipgttclfggteleshnipkIYGSIKPTAVSIPVNQllGKD 413
Cdd:cd06534 247 -----------------------------------------------------------IYDEFVEKLVTVLVDV--DPD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 414 FELITSEVFGPVQVIVVYEDQDlptimEALEKI---PQNLTAAVVSNDVHFQQKVLGYTVNGTTYAGMRARTTGAPQNHW 490
Cdd:cd06534 266 MPIAQEEIFGPVLPVIRFKDEE-----EAIALAndtEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFG 340
|
410 420
....*....|....*....|
gi 167041430 491 -FGPSGDPRSAGIGTPEAIT 509
Cdd:cd06534 341 gVKNSGIGREGGPYGLEEYT 360
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
102-459 |
1.15e-28 |
|
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: 118.79 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 102 KAAALLSNKEVEdfFVHLIQRVMPKSSNQCLGEVTVTRKFLENFSGDGVRFLARSFSNPGDHLgqeSSGYRWPFGSVVIV 181
Cdd:pfam00171 59 KAADLLEERKDE--LAELETLENGKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRL---AYTRREPLGVVGAI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 182 APFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLIsAASDKIRMVQFT 261
Cdd:pfam00171 134 TPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEAL-VEHPDVRKVSFT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 262 GSCAVAERIA--ADTNGK-VRVEDAGFNWKLIGPDYDPswsDYVAWQCDEDAYNASGQKCSAQSILFVHKNweqdlllkl 338
Cdd:pfam00171 213 GSTAVGRHIAeaAAQNLKrVTLELGGKNPLIVLEDADL---DAAVEAAVFGAFGNAGQVCTATSRLLVHES--------- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 339 kqLAER------RKLENLSIGPVLTWNND-------QLFNHINSLLEI---PGTTCLFGGTELESHNIPkiygsIKPTAV 402
Cdd:pfam00171 281 --IYDEfveklvEAAKKLKVGDPLDPDTDmgpliskAQLERVLKYVEDakeEGAKLLTGGEAGLDNGYF-----VEPTVL 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 403 SIPVNqllgkDFELITSEVFGPVQVIVVYEDQDlptimEALEKI---PQNLTAAVVSNDV 459
Cdd:pfam00171 354 ANVTP-----DMRIAQEEIFGPVLSVIRFKDEE-----EAIEIAndtEYGLAAGVFTSDL 403
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
97-465 |
1.01e-27 |
|
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: 115.99 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 97 GNVCAKAAALLsNKEVEDFfVHLIQRVMPKSSNQCLGEVTVTRKFLENFSGDGVRFLARSFsnPGDHLGQESSGYRWPFG 176
Cdd:COG1012 68 AAILLRAADLL-EERREEL-AALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETI--PSDAPGTRAYVRREPLG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 177 SVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLIsAASDKIR 256
Cdd:COG1012 144 VVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAAL-VAHPDVD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 257 MVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDPswsDYVAWQCDEDAYNASGQKCSAQSILFVHKNweqd 333
Cdd:COG1012 223 KISFTGSTAVGRRIaaaAAENLKRVTLELGGKNPAIVLDDADL---DAAVEAAVRGAFGNAGQRCTAASRLLVHES---- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 334 lllklkqLAER------RKLENLSIGPVLTWNND-------QLFNHINSLLEI---PGTTCLFGGTELESHNipkiyGS- 396
Cdd:COG1012 296 -------IYDEfverlvAAAKALKVGDPLDPGTDmgpliseAQLERVLAYIEDavaEGAELLTGGRRPDGEG-----GYf 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167041430 397 IKPTAVSiPVNQllgkDFELITSEVFGPVQVIVVYEDQDlptimEALEKI---PQNLTAAVVSNDVHFQQKV 465
Cdd:COG1012 364 VEPTVLA-DVTP----DMRIAREEIFGPVLSVIPFDDEE-----EAIALAndtEYGLAASVFTRDLARARRV 425
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
102-509 |
6.59e-25 |
|
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: 107.82 E-value: 6.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 102 KAAALLsnKEVEDFFVHLIQRVMPKSSNQCLGEVTVTRKFLENFSGDGVRFLARSFsnPGDHLGQESSGYRWPFGSVVIV 181
Cdd:cd07131 67 RAAELL--KKRKEELARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETV--PSELPNKDAMTRRQPIGVVALI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 182 APFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISAASDkIRMVQFT 261
Cdd:cd07131 143 TPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPD-VDVVSFT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 262 GSCAVAERIA---ADTNGKVRVEDAGFNWKLIGPDYDPSWS-DYVAWqcdeDAYNASGQKCSAQSILFVHKNWEQDLLLK 337
Cdd:cd07131 222 GSTEVGERIGetcARPNKRVALEMGGKNPIIVMDDADLDLAlEGALW----SAFGTTGQRCTATSRLIVHESVYDEFLKR 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 338 LKQLAERRKL-----ENLSIGPVLtwNNDQLfNHINSLLEI---PGTTCLFGGTELESHNIPKIYgSIKPTAVSIPVNQL 409
Cdd:cd07131 298 FVERAKRLRVgdgldEETDMGPLI--NEAQL-EKVLNYNEIgkeEGATLLLGGERLTGGGYEKGY-FVEPTVFTDVTPDM 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 410 lgkdfELITSEVFGPVQVIVVYEdqdlpTIMEALE---KIPQNLTAAVVSNDVHFQQKVLGYTVNGTTYagMRARTTGAP 486
Cdd:cd07131 374 -----RIAQEEIFGPVVALIEVS-----SLEEAIEianDTEYGLSSAIYTEDVNKAFRARRDLEAGITY--VNAPTIGAE 441
|
410 420
....*....|....*....|....*..
gi 167041430 487 QNHWFG---PSGD-PRSAGIGTPEAIT 509
Cdd:cd07131 442 VHLPFGgvkKSGNgHREAGTTALDAFT 468
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
34-465 |
1.31e-23 |
|
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: 103.87 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 34 NLLSGEWLDtskyfdnipdPVSGEYFIDIPDTDDLSGFIQNLDIC-------------PKSGLHNPIknvERyvmlGNVC 100
Cdd:cd07097 3 NYIDGEWVA----------GGDGEENRNPSDTSDVVGKYARASAEdadaaiaaaaaafPAWRRTSPE---AR----ADIL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 101 AKAAALLSnKEVEDFfVHLIQRVMPKSSNQCLGEVTVTRKFLENFSGDGVRFLARSFsnPGDHLGQESSGYRWPFGSVVI 180
Cdd:cd07097 66 DKAGDELE-ARKEEL-ARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETL--PSTRPGVEVETTREPLGVVGL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 181 VAPFNFPLEIPALQFLGALFMGNRPLIKSAT-TVGIVFEqFLRLLIHCGLPATDADMVHCRGSKMGKLIsAASDKIRMVQ 259
Cdd:cd07097 142 ITPWNFPIAIPAWKIAPALAYGNTVVFKPAElTPASAWA-LVEILEEAGLPAGVFNLVMGSGSEVGQAL-VEHPDVDAVS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 260 FTGSCAVAERI--AADTNG-KVRVEDAGFNWKLIGPDYDPSwsdyVAWQCDED-AYNASGQKCSAQSILFVHKNweqDLL 335
Cdd:cd07097 220 FTGSTAVGRRIaaAAAARGaRVQLEMGGKNPLVVLDDADLD----LAVECAVQgAFFSTGQRCTASSRLIVTEG---IHD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 336 LKLKQLAER-RKL-------ENLSIGPVLtwNNDQLfNHINSLLEI---PGTTCLFGGTELESHNiPKIYgsIKPTAVSI 404
Cdd:cd07097 293 RFVEALVERtKALkvgdaldEGVDIGPVV--SERQL-EKDLRYIEIarsEGAKLVYGGERLKRPD-EGYY--LAPALFAG 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167041430 405 PVNqllgkDFELITSEVFGPVQVIVVYEDQDlptimEALEK---IPQNLTAAVVSNDV----HFQQKV 465
Cdd:cd07097 367 VTN-----DMRIAREEIFGPVAAVIRVRDYD-----EALAIandTEFGLSAGIVTTSLkhatHFKRRV 424
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
102-459 |
4.92e-23 |
|
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: 101.88 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 102 KAAALLsnKEVEDFFVHLIQRVMPKSSNQCLGEVTVTRKFLENFSGDGVRfLARSFSnPGD----HLGQESSGYRWPFGS 177
Cdd:cd07082 69 KFADLL--KENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKR-LDGDSL-PGDwfpgTKGKIAQVRREPLGV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 178 VVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLIsAASDKIRM 257
Cdd:cd07082 145 VLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPL-VTHGRIDV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 258 VQFTGSCAVAERIAaDTNGKVRV--EDAGFNWKLIGPDYDPSWSdyvAWQCDEDAYNASGQKCSAQSILFVHKNweqdll 335
Cdd:cd07082 224 ISFTGSTEVGNRLK-KQHPMKRLvlELGGKDPAIVLPDADLELA---AKEIVKGALSYSGQRCTAIKRVLVHES------ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 336 lklkqLAER------RKLENLSIGpvLTWNNDQLF---------NHINSLLE---IPGTTCLFGGTElESHNIpkiygsI 397
Cdd:cd07082 294 -----VADElvellkEEVAKLKVG--MPWDNGVDItplidpksaDFVEGLIDdavAKGATVLNGGGR-EGGNL------I 359
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167041430 398 KPTAVSiPVNqllgKDFELITSEVFGPVQVIVVYEDQDlptimEALEKIPQN---LTAAVVSNDV 459
Cdd:cd07082 360 YPTLLD-PVT----PDMRLAWEEPFGPVLPIIRVNDIE-----EAIELANKSnygLQASIFTKDI 414
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
102-485 |
1.61e-21 |
|
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: 97.65 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 102 KAAALLSNKEVEdfFVHLIQRVMPKSSNQCLGEVTVTRKFLENFSGDGVRFLARSFSNPGdHLGQESSGYRWPFGSVVIV 181
Cdd:cd07083 85 KAADLLRRRRRE--LIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVP-YPGEDNESFYVGLGAGVVI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 182 APFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISaASDKIRMVQFT 261
Cdd:cd07083 162 SPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLT-EHERIRGINFT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 262 GSCAVAERI------AADTNG---KVRVEDAGFNWKLIGPDYDPswsDYVAWQCDEDAYNASGQKCSAQSILFVHKNWEQ 332
Cdd:cd07083 241 GSLETGKKIyeaaarLAPGQTwfkRLYVETGGKNAIIVDETADF---ELVVEGVVVSAFGFQGQKCSAASRLILTQGAYE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 333 DLLLKLKQLAERRKLENLS-----IGPVLTW----NNDQLFNHINSLLEIpgttcLFGGTELESHNIpkiygSIKPTAVS 403
Cdd:cd07083 318 PVLERLLKRAERLSVGPPEengtdLGPVIDAeqeaKVLSYIEHGKNEGQL-----VLGGKRLEGEGY-----FVAPTVVE 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 404 IPVNQLlgkdfELITSEVFGPVQVIVVYEDQDLPTIMEALEKIPQNLTAAVVSN---------------DVHFQQKVLGY 468
Cdd:cd07083 388 EVPPKA-----RIAQEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRkrehleearrefhvgNLYINRKITGA 462
|
410
....*....|....*..
gi 167041430 469 TVNGTTYAGMRARTTGA 485
Cdd:cd07083 463 LVGVQPFGGFKLSGTNA 479
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
167-492 |
1.15e-19 |
|
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: 91.90 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 167 ESSGYRW-PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMG 245
Cdd:cd07124 158 EDNRYVYrPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 246 KLISAASDkIRMVQFTGSCAVAERI---AADTNG------KVRVEDAGFNWKLIGPDYDpswSDYVAWQCDEDAYNASGQ 316
Cdd:cd07124 238 DYLVEHPD-VRFIAFTGSREVGLRIyerAAKVQPgqkwlkRVIAEMGGKNAIIVDEDAD---LDEAAEGIVRSAFGFQGQ 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 317 KCSAQSILFVHKnweqdllLKLKQLAER--RKLENLSI----------GPVLtwnNDQLFNHINSLLEI--PGTTCLFGG 382
Cdd:cd07124 314 KCSACSRVIVHE-------SVYDEFLERlvERTKALKVgdpedpevymGPVI---DKGARDRIRRYIEIgkSEGRLLLGG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 383 TELESHN-----IPKIYGSIKPTAvsipvnqllgkdfELITSEVFGPVQVIVVYEDQDlptimEALEK---IPQNLTAAV 454
Cdd:cd07124 384 EVLELAAegyfvQPTIFADVPPDH-------------RLAQEEIFGPVLAVIKAKDFD-----EALEIandTEYGLTGGV 445
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 167041430 455 VSND-VHFQQKVLGYTVnGTTYAGmRaRTTGA-PQNHWFG 492
Cdd:cd07124 446 FSRSpEHLERARREFEV-GNLYAN-R-KITGAlVGRQPFG 482
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
167-465 |
2.79e-19 |
|
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: 90.72 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 167 ESSGYRW-PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMG 245
Cdd:cd07125 159 ELNGLELhGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 246 KLISAASDkIRMVQFTGSCAVAERIA--------------ADTNGKvrvedagfNWKLIGPDYDPswsDYVAWQCDEDAY 311
Cdd:cd07125 239 EALVAHPR-IDGVIFTGSTETAKLINralaerdgpilpliAETGGK--------NAMIVDSTALP---EQAVKDVVQSAF 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 312 NASGQKCSAQSILFVHKNweqdlllklkqLAER-RKL-----ENLSIGPVltWNndqLFNHINSLLEIPGTTCLFGGTEL 385
Cdd:cd07125 307 GSAGQRCSALRLLYLQEE-----------IAERfIEMlkgamASLKVGDP--WD---LSTDVGPLIDKPAGKLLRAHTEL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 386 ESHN--------IPKIYGS-IKPTAVSIPvnqllgKDFELiTSEVFGPVQVIVVYEDQDLPTIMEALEKIPQNLTAAVVS 456
Cdd:cd07125 371 MRGEawliapapLDDGNGYfVAPGIIEIV------GIFDL-TTEVFGPILHVIRFKAEDLDEAIEDINATGYGLTLGIHS 443
|
....*....
gi 167041430 457 NDVHFQQKV 465
Cdd:cd07125 444 RDEREIEYW 452
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
174-458 |
4.97e-19 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 89.99 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 174 PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGK-LISAAs 252
Cdd:PRK03137 171 PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDyLVDHP- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 253 dKIRMVQFTGSCAVAERI---AADTN--------------GK---VRVEDAgfnwkligpDYDPSWSDYVAwqcdeDAYN 312
Cdd:PRK03137 250 -KTRFITFTGSREVGLRIyerAAKVQpgqiwlkrviaemgGKdaiVVDEDA---------DLDLAAESIVA-----SAFG 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 313 ASGQKCSAQSILFVHKNWEQDLLLKLKQLAERRKL----ENLSIGPVLtwnNDQLFNHINSLLEIPGTT--CLFGGTELE 386
Cdd:PRK03137 315 FSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVgnpeDNAYMGPVI---NQASFDKIMSYIEIGKEEgrLVLGGEGDD 391
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167041430 387 SHNI---PKIYGSIKPTAVsipvnqllgkdfeLITSEVFGPVQVIVVYEDQDlptimEALEkIPQN----LTAAVVSND 458
Cdd:PRK03137 392 SKGYfiqPTIFADVDPKAR-------------IMQEEIFGPVVAFIKAKDFD-----HALE-IANNteygLTGAVISNN 451
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
134-459 |
2.79e-18 |
|
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: 87.50 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 134 EVTVTRKFLENFSGDGVRF----LARSFSNPGdhlGQESSGY--RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLI 207
Cdd:cd07113 99 EVGQSANFLRYFAGWATKIngetLAPSIPSMQ---GERYTAFtrREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 208 KSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISAAsdKIRMVQFTGSCAVAERI---AADTNGKVRVEDAG 284
Cdd:cd07113 176 KPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHP--DVAKVSFTGSVATGKKIgrqAASDLTRVTLELGG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 285 FNWKLIGPDYDPSWsdyVAWQCDEDAYNASGQKCSAQSILFVHKnweqdLLLKLKQLAERRKLENLSIGPVLT------- 357
Cdd:cd07113 254 KNAAAFLKDADIDW---VVEGLLTAGFLHQGQVCAAPERFYVHR-----SKFDELVTKLKQALSSFQVGSPMDesvmfgp 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 358 WNNDQLFNHINSLLEIP---GTTCLFGGTELEShniPKIYgsIKPTAVSIPvnqllGKDFELITSEVFGPVQVIVVYEDQ 434
Cdd:cd07113 326 LANQPHFDKVCSYLDDAraeGDEIVRGGEALAG---EGYF--VQPTLVLAR-----SADSRLMREETFGPVVSFVPYEDE 395
|
330 340
....*....|....*....|....*...
gi 167041430 435 DlptimEALEKI---PQNLTAAVVSNDV 459
Cdd:cd07113 396 E-----ELIQLIndtPFGLTASVWTNNL 418
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
91-458 |
1.50e-17 |
|
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: 85.18 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 91 ERYvmlgNVCAKAAALLsnKEVEDFFVHLIQRVMPKSSNQCLGEVTVTRKFLENFSGDGVRFlaRSFSNPGDhLGQESSG 170
Cdd:cd07094 44 ERM----AILERAADLL--KKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRLAAEEAERI--RGEEIPLD-ATQGSDN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 171 -----YRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMG 245
Cdd:cd07094 115 rlawtIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 246 KLIsAASDKIRMVQFTGSCAVAERIAADTNGK-VRVEDAGFNWKLIGPDYDpswSDYVAWQCDEDAYNASGQKCSAQSIL 324
Cdd:cd07094 195 DAF-AADERVAMLSFTGSAAVGEALRANAGGKrIALELGGNAPVIVDRDAD---LDAAIEALAKGGFYHAGQVCISVQRI 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 325 FVHKNWEQDLLLKLKQLAERRKL-----ENLSIGPVL-----TWNNDqlfnHINSLLEIPGTtcLFGGTELEshnipkiy 394
Cdd:cd07094 271 YVHEELYDEFIEAFVAAVKKLKVgdpldEDTDVGPLIseeaaERVER----WVEEAVEAGAR--LLCGGERD-------- 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167041430 395 GSI-KPTAVSIPvnqllGKDFELITSEVFGPVQVIVVYEDQDlptimEALE---KIPQNLTAAVVSND 458
Cdd:cd07094 337 GALfKPTVLEDV-----PRDTKLSTEETFGPVVPIIRYDDFE-----EAIRianSTDYGLQAGIFTRD 394
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
133-460 |
4.61e-17 |
|
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: 83.53 E-value: 4.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 133 GEVTVTRKFLENFSGDGVRFLARSFsnPGDHLGQESSGYRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIK--SA 210
Cdd:cd07150 80 FETTFTPELLRAAAGECRRVRGETL--PSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKpsEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 211 TTVGIVfeQFLRLLIHCGLPATDADMVHCRGSKMGKLIsAASDKIRMVQFTGSCAVAERIAADTNG---KVRVEDAGFNW 287
Cdd:cd07150 158 TPVIGL--KIAEIMEEAGLPKGVFNVVTGGGAEVGDEL-VDDPRVRMVTFTGSTAVGREIAEKAGRhlkKITLELGGKNP 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 288 KLIGPDYDPswsDYVAWQCDEDAYNASGQKCSAQSILFVHKNWEQDLLLKLKQLAERRKLENLS-----IGPVLTWNN-D 361
Cdd:cd07150 235 LIVLADADL---DYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRdpdtvIGPLISPRQvE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 362 QLFNHINSLLEiPGTTCLFGGTELESHNIPKIYGSIKPtavsipvnqllgkDFELITSEVFGPVQVIVVYEDQDlptimE 441
Cdd:cd07150 312 RIKRQVEDAVA-KGAKLLTGGKYDGNFYQPTVLTDVTP-------------DMRIFREETFGPVTSVIPAKDAE-----E 372
|
330 340
....*....|....*....|..
gi 167041430 442 ALEKIPQN---LTAAVVSNDVH 460
Cdd:cd07150 373 ALELANDTeygLSAAILTNDLQ 394
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
162-456 |
1.02e-16 |
|
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: 83.04 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 162 DHLGQESSGyrwPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRG 241
Cdd:TIGR01238 151 DVLGEFSVE---SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRG 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 242 SKMGKLISaASDKIRMVQFTGSCAVAERIA------ADTNGKVRVEDAGFNWKLIGpdydpswSDYVAWQCDED----AY 311
Cdd:TIGR01238 228 ADVGAALT-SDPRIAGVAFTGSTEVAQLINqtlaqrEDAPVPLIAETGGQNAMIVD-------STALPEQVVRDvlrsAF 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 312 NASGQKCSAQSILFVHKNWEQDLLLKLKQLAERRKLEN-----LSIGPVLTWNNDQ-LFNHINSLleiPGTTCLFGGTEL 385
Cdd:TIGR01238 300 DSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVphlltTDVGPVIDAEAKQnLLAHIEHM---SQTQKKIAQLTL 376
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167041430 386 ESHNIPKIYGSIKPTAVSIpvnqllgKDFELITSEVFGPVQVIVVYEDQDLPTIMEALEKIPQNLTAAVVS 456
Cdd:TIGR01238 377 DDSRACQHGTFVAPTLFEL-------DDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHS 440
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
102-460 |
1.70e-16 |
|
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: 81.81 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 102 KAAALLsnKEVEDFFVHLIQR----VMPKSSnqclGEVTVTRKFLENFSGDGVRFLARSFsnPGDHLGQESSGYRWPFGS 177
Cdd:cd07104 30 KAAEIL--EERRDEIADWLIResgsTRPKAA----FEVGAAIAILREAAGLPRRPEGEIL--PSDVPGKESMVRRVPLGV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 178 VVIVAPFNFPLEIPALQFLGALFMGNRPLIK--SATTV--GIVFEqflRLLIHCGLPATDADMVHCRGSKMGKLISAASD 253
Cdd:cd07104 102 VGVISPFNFPLILAMRSVAPALALGNAVVLKpdSRTPVtgGLLIA---EIFEEAGLPKGVLNVVPGGGSEIGDALVEHPR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 254 kIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDPswsDYVAwqcDEDAYNA---SGQKCSAQSILFVH 327
Cdd:cd07104 179 -VRMISFTGSTAVGRHIgelAGRHLKKVALELGGNNPLIVLDDADL---DLAV---SAAAFGAflhQGQICMAAGRILVH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 328 knwEQDLLLKLKQLAER-RKL-------ENLSIGPVLtwNNDQLFN---HINSLLEiPGTTCLFGGTE----LEshniPK 392
Cdd:cd07104 252 ---ESVYDEFVEKLVAKaKALpvgdprdPDTVIGPLI--NERQVDRvhaIVEDAVA-AGARLLTGGTYeglfYQ----PT 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167041430 393 IYGSIKPtavsipvnqllgkDFELITSEVFGPVQVIVVYEDQDlptimEALEKI---PQNLTAAVVSNDVH 460
Cdd:cd07104 322 VLSDVTP-------------DMPIFREEIFGPVAPVIPFDDDE-----EAVELAndtEYGLSAAVFTRDLE 374
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
125-459 |
2.53e-16 |
|
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: 81.68 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 125 PKSSNqCLGEVTVTRKFLENFSGDGVRFLARSFSNpgdhlGQESSGY--RWPFGSVVIVAPFNFPLEIPALQFLGALFMG 202
Cdd:cd07144 99 PYHSN-ALGDLDEIIAVIRYYAGWADKIQGKTIPT-----SPNKLAYtlHEPYGVCGQIIPWNYPLAMAAWKLAPALAAG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 203 NRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLIsAASDKIRMVQFTGSCAVAERI--AADTNGK-VR 279
Cdd:cd07144 173 NTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSAL-AEHPDVDKIAFTGSTATGRLVmkAAAQNLKaVT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 280 VEDAGFNWKLIGPDYDPSWSdyVAWQCDEDAYNaSGQKCSAQSILFVHKN-WEQDLLLKLKQLAERRKL-----ENLSIG 353
Cdd:cd07144 252 LECGGKSPALVFEDADLDQA--VKWAAAGIMYN-SGQNCTATSRIYVQESiYDKFVEKFVEHVKQNYKVgspfdDDTVVG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 354 PVLtwNNDQlFNHINSLLEI---PGTTCLFGGTELESHNIPKIYgsIKPTAVSiPVNQllgkDFELITSEVFGPVQVIVV 430
Cdd:cd07144 329 PQV--SKTQ-YDRVLSYIEKgkkEGAKLVYGGEKAPEGLGKGYF--IPPTIFT-DVPQ----DMRIVKEEIFGPVVVISK 398
|
330 340 350
....*....|....*....|....*....|..
gi 167041430 431 YEDQDlptimEALEKI---PQNLTAAVVSNDV 459
Cdd:cd07144 399 FKTYE-----EAIKKAndtTYGLAAAVFTKDI 425
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
172-459 |
2.65e-16 |
|
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: 81.46 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 172 RW-PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATT---VGIVFEQ-FLRLLIHCGLPATDADMVHCRGsKMGK 246
Cdd:cd07086 130 QWnPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETtplTAIAVTKiLAEVLEKNGLPPGVVNLVTGGG-DGGE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 247 LIsAASDKIRMVQFTGSCAVAERIA---ADTNGKVRVEDAGFNWKLIGPDYD-----PSwsdyVAWQcdedAYNASGQKC 318
Cdd:cd07086 209 LL-VHDPRVPLVSFTGSTEVGRRVGetvARRFGRVLLELGGNNAIIVMDDADldlavRA----VLFA----AVGTAGQRC 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 319 SAQSILFVHKNWEQDLLLKLKQLAERRKL-----ENLSIGPVLTWNNDQLFNHINSLLEIPGTTCLFGGtELESHNIPKI 393
Cdd:cd07086 280 TTTRRLIVHESVYDEFLERLVKAYKQVRIgdpldEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGG-KRIDGGEPGN 358
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167041430 394 YgsIKPTAVSIPvnqllGKDFELITSEVFGPVQVIVVYEDQDlptimEALE---KIPQNLTAAVVSNDV 459
Cdd:cd07086 359 Y--VEPTIVTGV-----TDDARIVQEETFAPILYVIKFDSLE-----EAIAinnDVPQGLSSSIFTEDL 415
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
102-446 |
6.98e-16 |
|
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: 80.00 E-value: 6.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 102 KAAALLsnKEVEDFFVHLIQRVMPKSSNQCLGEVTVTRKFLENFSGdgvrfLARSF-------SNPGDHLGQessgYRWP 174
Cdd:cd07088 65 KLADLI--RENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAE-----WARRIegeiipsDRPNENIFI----FKVP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 175 FGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIK-SATTVGIVFEqFLRLLIHCGLPATDADMVHCRGSKMGKLIsAASD 253
Cdd:cd07088 134 IGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKpSEETPLNALE-FAELVDEAGLPAGVLNIVTGRGSVVGDAL-VAHP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 254 KIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDPSwsdyVAWQCDEDA-YNASGQKCSAQSILFVHKN 329
Cdd:cd07088 212 KVGMISLTGSTEAGQKImeaAAENITKVSLELGGKAPAIVMKDADLD----LAVKAIVDSrIINCGQVCTCAERVYVHED 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 330 WEQDLLLKLKQLAERRKL-----ENLSIGPVLtwNNDQLfNHINSLLEIP---GTTCLFGGTELESHNipkiyGSIKPTA 401
Cdd:cd07088 288 IYDEFMEKLVEKMKAVKVgdpfdAATDMGPLV--NEAAL-DKVEEMVERAveaGATLLTGGKRPEGEK-----GYFYEPT 359
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167041430 402 VSIPVNQllgkDFELITSEVFGPVQVIVVYED---------------------QDLPTIMEALEKI 446
Cdd:cd07088 360 VLTNVRQ----DMEIVQEEIFGPVLPVVKFSSldeaielandseygltsyiytENLNTAMRATNEL 421
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
171-458 |
1.10e-15 |
|
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: 79.55 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 171 YRWPFGSVVIVAPFNF-------PLEiPALqflgalfMGNRPLIKSATTVgiVFEQFL--RLLIHCGLPATDADMVHCRG 241
Cdd:cd07123 167 YRPLEGFVYAVSPFNFtaiggnlAGA-PAL-------MGNVVLWKPSDTA--VLSNYLvyKILEEAGLPPGVINFVPGDG 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 242 SKMGKLIsAASDKIRMVQFTGSCAV--------AE---------RIAADTNGKvrvedagfNWKLIGPDYDPSWsdyVAW 304
Cdd:cd07123 237 PVVGDTV-LASPHLAGLHFTGSTPTfkslwkqiGEnldryrtypRIVGETGGK--------NFHLVHPSADVDS---LVT 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 305 QCDEDAYNASGQKCSAQSILFVHKNWEQDLLLKLKqlaerRKLENLSIGPVLTWNN-------DQLFNHINSLLEI---- 373
Cdd:cd07123 305 ATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLL-----EELKEIKMGDPDDFSNfmgavidEKAFDRIKGYIDHaksd 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 374 PGTTCLFGGTELEShnipKIYgSIKPTAVsipvnqlLGKD--FELITSEVFGPVQVIVVYEDQDLPTIMEALEKI-PQNL 450
Cdd:cd07123 380 PEAEIIAGGKCDDS----VGY-FVEPTVI-------ETTDpkHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTsPYAL 447
|
....*...
gi 167041430 451 TAAVVSND 458
Cdd:cd07123 448 TGAIFAQD 455
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
102-460 |
2.62e-15 |
|
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: 78.02 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 102 KAAALL-SNKEVedfFVHLIQRVMPKSSNQCLGEVTVTRKFLEnFSGDGVRFLARSF----SNPGdhlGQESSGY--RWP 174
Cdd:cd07149 51 RAAQLLeERREE---FARTIALEAGKPIKDARKEVDRAIETLR-LSAEEAKRLAGETipfdASPG---GEGRIGFtiREP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 175 FGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLIsAASDK 254
Cdd:cd07149 124 IGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDAL-VTDPR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 255 IRMVQFTGSCAVAERIAAdTNG--KVRVEDAGFNWKLIGPDYDpswSDYVAWQCDEDAYNASGQKC-SAQSIlFVHKnwE 331
Cdd:cd07149 203 VRMISFTGSPAVGEAIAR-KAGlkKVTLELGSNAAVIVDADAD---LEKAVERCVSGAFANAGQVCiSVQRI-FVHE--D 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 332 QDLLLKLKQLAERRKL-------ENLSIGPVLTWNN-DQLFNHINSLLEiPGTTCLFGGTeleshnipKIYGSIKPTAVS 403
Cdd:cd07149 276 IYDEFLERFVAATKKLvvgdpldEDTDVGPMISEAEaERIEEWVEEAVE-GGARLLTGGK--------RDGAILEPTVLT 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167041430 404 -IPvnqllgKDFELITSEVFGPVQVIVVYEDQDlptimEALEKI---PQNLTAAVVSNDVH 460
Cdd:cd07149 347 dVP------PDMKVVCEEVFAPVVSLNPFDTLD-----EAIAMAndsPYGLQAGVFTNDLQ 396
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
172-501 |
7.58e-15 |
|
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: 76.97 E-value: 7.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 172 RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLIsAA 251
Cdd:cd07119 132 REPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAEL-AE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 252 SDKIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDPSWS-DYvawqcdedAYNA----SGQKCSAQSI 323
Cdd:cd07119 211 SPDVDLVSFTGGTATGRSImraAAGNVKKVALELGGKNPNIVFADADFETAvDQ--------ALNGvffnAGQVCSAGSR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 324 LFVHKNWEQDLLLKLKQLAERRKLEN-----LSIGPVLtwnNDQLFNHINSLLEI---PGTTCLFGGTELESHNIPKIYg 395
Cdd:cd07119 283 LLVEESIHDKFVAALAERAKKIKLGNgldadTEMGPLV---SAEHREKVLSYIQLgkeEGARLVCGGKRPTGDELAKGY- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 396 SIKPTAVSiPVNQllgkDFELITSEVFGPVQVIVVYEDQDlptimEALEK---IPQNLTAAVVSNDVHFQQKVLGYTVNG 472
Cdd:cd07119 359 FVEPTIFD-DVDR----TMRIVQEEIFGPVLTVERFDTEE-----EAIRLandTPYGLAGAVWTKDIARANRVARRLRAG 428
|
330 340 350
....*....|....*....|....*....|.
gi 167041430 473 TTYAGMRARTTgaPQNHW--FGPSGDPRSAG 501
Cdd:cd07119 429 TVWINDYHPYF--AEAPWggYKQSGIGRELG 457
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
91-459 |
1.13e-14 |
|
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: 76.23 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 91 ERYvmlgNVCAKAAALLSNKEVEdfFVHLIQRVMPKSSNQCLGEVTVTRKFLEnFSGDGVRFLARSFSNPGDHLGQESS- 169
Cdd:cd07145 44 KRY----KILMKVAELIERRKEE--LAKLLTIEVGKPIKQSRVEVERTIRLFK-LAAEEAKVLRGETIPVDAYEYNERRi 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 170 --GYRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKL 247
Cdd:cd07145 117 afTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 248 ISaASDKIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDpswSDYVAWQCDEDAYNASGQKCSAQSIL 324
Cdd:cd07145 197 IV-TNPKVNMISFTGSTAVGLLIaskAGGTGKKVALELGGSDPMIVLKDAD---LERAVSIAVRGRFENAGQVCNAVKRI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 325 FVHKnwEQDLLLKLKQLAERRKL-------ENLSIGPVLT-----WNNDQLFNHINSlleipGTTCLFGGTELESHNIPk 392
Cdd:cd07145 273 LVEE--EVYDKFLKLLVEKVKKLkvgdpldESTDLGPLISpeaveRMENLVNDAVEK-----GGKILYGGKRDEGSFFP- 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 393 iygsikPTAVSIPvnqllGKDFELITSEVFGPVQVIVVYEDQDlptimEALE---KIPQNLTAAVVSNDV 459
Cdd:cd07145 345 ------PTVLEND-----TPDMIVMKEEVFGPVLPIAKVKDDE-----EAVEianSTEYGLQASVFTNDI 398
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
156-460 |
1.44e-14 |
|
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: 75.86 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 156 SFSNPGDHLGQESSGY--RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATD 233
Cdd:cd07146 100 SFSCDLTANGKARKIFtlREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDM 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 234 ADMVHCRGSKMG-KLIsaASDKIRMVQFTGSCAVAERIAADTNGKVRVEDAGFNWKLI-GPDYDpswSDYVAWQCDEDAY 311
Cdd:cd07146 180 LSVVTGEPGEIGdELI--THPDVDLVTFTGGVAVGKAIAATAGYKRQLLELGGNDPLIvMDDAD---LERAATLAVAGSY 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 312 NASGQKCSAQSILFVHKNWEQDLLLKLKQLAERRKL-----ENLSIGPVLTWN-NDQLFNHINSLLEiPGTTCLFGGTEL 385
Cdd:cd07146 255 ANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVgdpmdPATDMGTVIDEEaAIQIENRVEEAIA-QGARVLLGNQRQ 333
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167041430 386 ESHNIPKIYGSIKPTAvsipvnqllgkdfELITSEVFGPVQVIVVYEdqDLPTIMEALEKIPQNLTAAVVSNDVH 460
Cdd:cd07146 334 GALYAPTVLDHVPPDA-------------ELVTEETFGPVAPVIRVK--DLDEAIAISNSTAYGLSSGVCTNDLD 393
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
174-459 |
1.65e-14 |
|
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: 75.71 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 174 PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISAASD 253
Cdd:cd07091 141 PIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMD 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 254 kIRMVQFTGSCAVAERI---AADTN-GKVRVEDAGFNWKLIGPDYDPSWSDYVAWQcdeDAYNASGQKCSAQSILFVHKN 329
Cdd:cd07091 221 -VDKIAFTGSTAVGRTImeaAAKSNlKKVTLELGGKSPNIVFDDADLDKAVEWAAF---GIFFNQGQCCCAGSRIFVQES 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 330 WEQDLLLKLKQLAERRKL-----ENLSIGPVltwNNDQLFNHINSLLEI---PGTTCLFGGTELEShnipKIYgSIKPTa 401
Cdd:cd07091 297 IYDEFVEKFKARAEKRVVgdpfdPDTFQGPQ---VSKAQFDKILSYIESgkkEGATLLTGGERHGS----KGY-FIQPT- 367
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167041430 402 VSIPVNqllgKDFELITSEVFGPVQVIVVYEDQDlptimEALEKIPQN---LTAAVVSNDV 459
Cdd:cd07091 368 VFTDVK----DDMKIAKEEIFGPVVTILKFKTED-----EVIERANDTeygLAAGVFTKDI 419
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
162-475 |
1.82e-14 |
|
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: 75.75 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 162 DHLGQESSGY-----RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADM 236
Cdd:cd07102 99 DIRVPEKDGFeryirREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 237 VHCRGSKMGKLISAAsdKIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDPSWSdyVAWQCDEDAYNa 313
Cdd:cd07102 179 LHLSHETSAALIADP--RIDHVSFTGSVAGGRAIqraAAGRFIKVGLELGGKDPAYVRPDADLDAA--AESLVDGAFFN- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 314 SGQKCSAQSILFVHKNWEQDLLLKLKQLAERRKL-----ENLSIGPVLTWNN-DQLFNHINSLLEiPGTTCLFGGTELES 387
Cdd:cd07102 254 SGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLgdpldPSTTLGPVVSARAaDFVRAQIADAIA-KGARALIDGALFPE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 388 HNIPKIYgsIKPTaVSIPVNQllgkDFELITSEVFGPVQVIVVYEDQDlptimEALEKI---PQNLTAAVVSNDVHFQQK 464
Cdd:cd07102 333 DKAGGAY--LAPT-VLTNVDH----SMRVMREETFGPVVGIMKVKSDA-----EAIALMndsEYGLTASVWTKDIARAEA 400
|
330
....*....|.
gi 167041430 465 VLGYTVNGTTY 475
Cdd:cd07102 401 LGEQLETGTVF 411
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
153-460 |
3.58e-14 |
|
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: 74.68 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 153 LAR-----SFSNPG-DHLGQESsgyRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIK-----SATTVGIVfeqfl 221
Cdd:cd07118 95 LARtlhgdSYNNLGdDMLGLVL---REPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKpseftSGTTLMLA----- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 222 RLLIHCGLPATDADMVHCRGSKMGKLISAASDkIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDpsW 298
Cdd:cd07118 167 ELLIEAGLPAGVVNIVTGYGATVGQAMTEHPD-VDMVSFTGSTRVGKAIaaaAARNLKKVSLELGGKNPQIVFADAD--L 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 299 SDYVawqcdeDA------YNAsGQKCSAQSILFVHKNWEQDLLLKLKQLAERRKL-----ENLSIGPVLTWN-NDQLFNH 366
Cdd:cd07118 244 DAAA------DAvvfgvyFNA-GECCNSGSRLLVHESIADAFVAAVVARSRKVRVgdpldPETKVGAIINEAqLAKITDY 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 367 INSLLEiPGTTCLFGGTELESHN----IPKIYGSIKPtavsipvnqllgkDFELITSEVFGPVQVIVVYEDQDlptimEA 442
Cdd:cd07118 317 VDAGRA-EGATLLLGGERLASAAglfyQPTIFTDVTP-------------DMAIAREEIFGPVLSVLTFDTVD-----EA 377
|
330 340
....*....|....*....|.
gi 167041430 443 LE---KIPQNLTAAVVSNDVH 460
Cdd:cd07118 378 IAlanDTVYGLSAGVWSKDID 398
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
172-459 |
8.06e-14 |
|
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: 73.55 E-value: 8.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 172 RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSAttvgivfEQ----FLRL--LIHCGLPATDADMVHCRGSKMG 245
Cdd:cd07108 115 REPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAA-------EDaplaVLLLaeILAQVLPAGVLNVITGYGEECG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 246 KLISAASDkIRMVQFTGSCAVAERIAADTNGK---VRVEDAGFNWKLIGPDYDPSWSdyVAWQCDEDAYNASGQKCSAQS 322
Cdd:cd07108 188 AALVDHPD-VDKVTFTGSTEVGKIIYRAAADRlipVSLELGGKSPMIVFPDADLDDA--VDGAIAGMRFTRQGQSCTAGS 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 323 ILFVHKNweqdlLLKLKQLAERRKLENLSIGPVL-------TWNNDQLFNHINSLLEI----PGTTCLFGGTE-LESHNI 390
Cdd:cd07108 265 RLFVHED-----IYDAFLEKLVAKLSKLKIGDPLdeatdigAIISEKQFAKVCGYIDLglstSGATVLRGGPLpGEGPLA 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167041430 391 PKIYgsIKPTAVSIPVNqllgkDFELITSEVFGPVQVIVVYEDQDlpTIMEALEKIPQNLTAAVVSNDV 459
Cdd:cd07108 340 DGFF--VQPTIFSGVDN-----EWRLAREEIFGPVLCAIPWKDED--EVIAMANDSHYGLAAYVWTRDL 399
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
143-460 |
8.54e-13 |
|
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: 70.29 E-value: 8.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 143 ENFsgdgvRFLA--------RSFSNPGDHLgqeSSGYRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIK------ 208
Cdd:cd07093 86 ANF-----RFFAdyilqldgESYPQDGGAL---NYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKpsewtp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 209 -SATTVGIVFEQflrllihCGLPATDADMVHCRGSKMGKLISAASDkIRMVQFTGSCAVAERI---AADTNGKVRVEDAG 284
Cdd:cd07093 158 lTAWLLAELANE-------AGLPPGVVNVVHGFGPEAGAALVAHPD-VDLISFTGETATGRTImraAAPNLKPVSLELGG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 285 FNWKLIGPDYD-PSWSDYVAWQcdedAYNASGQKCSAQSILFVHKNWEQDLLLKLKQLAERRKL-----ENLSIGPVLTw 358
Cdd:cd07093 230 KNPNIVFADADlDRAVDAAVRS----SFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVgdpldPDTEVGPLIS- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 359 nnDQLFNHINSLLEIP---GTTCLFGGTELESHNIPKIYgSIKPTAVSIPVNqllgkDFELITSEVFGPVQVIVVYEDQD 435
Cdd:cd07093 305 --KEHLEKVLGYVELAraeGATILTGGGRPELPDLEGGY-FVEPTVITGLDN-----DSRVAQEEIFGPVVTVIPFDDEE 376
|
330 340
....*....|....*....|....*...
gi 167041430 436 lptimEALEK---IPQNLTAAVVSNDVH 460
Cdd:cd07093 377 -----EAIELandTPYGLAAYVWTRDLG 399
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
102-459 |
1.14e-12 |
|
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: 70.02 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 102 KAAALLSNK--EVEDFFVHLIQRVMPKSsnqcLGEVTVTRKFLENFSGdgvrfLArsfSNPGDHL-----GQESSGYRWP 174
Cdd:cd07152 43 RAADLLEEHadEIADWIVRESGSIRPKA----GFEVGAAIGELHEAAG-----LP---TQPQGEIlpsapGRLSLARRVP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 175 FGSVVIVAPFNFPLeIPALQFLG-ALFMGNRPLIK----SATTVGIVFEqflRLLIHCGLPatdADMVHCR--GSKMGKL 247
Cdd:cd07152 111 LGVVGVISPFNFPL-ILAMRSVApALALGNAVVLKpdprTPVSGGVVIA---RLFEEAGLP---AGVLHVLpgGADAGEA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 248 ISAASDkIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDPSW-SDYVAWqcdeDAYNASGQKCSAQSI 323
Cdd:cd07152 184 LVEDPN-VAMISFTGSTAVGRKVgeaAGRHLKKVSLELGGKNALIVLDDADLDLaASNGAW----GAFLHQGQICMAAGR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 324 LFVHknwEQDLLLKLKQLAER-RKL-------ENLSIGPVLtwNNDQLfNHINSLLEIP---GTTCLFGGTELESHNIPK 392
Cdd:cd07152 259 HLVH---ESVADAYTAKLAAKaKHLpvgdpatGQVALGPLI--NARQL-DRVHAIVDDSvaaGARLEAGGTYDGLFYRPT 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 393 IYGSIKPtavsipvnqllgkDFELITSEVFGPVQVIVVYEDQDlptimEALE---KIPQNLTAAVVSNDV 459
Cdd:cd07152 333 VLSGVKP-------------GMPAFDEEIFGPVAPVTVFDSDE-----EAVAlanDTEYGLSAGIISRDV 384
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
132-508 |
2.22e-12 |
|
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: 68.94 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 132 LGEVTVTRKFLENFSGDGVRFLARSFSNPGDHLgqeSSGYRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSAT 211
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNL---HYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 212 TVGIvfeQFLRL--LIHCGLPATDADMVHCRGSKMGKLISAASDkIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFN 286
Cdd:cd07107 154 QAPL---SALRLaeLAREVLPPGVFNILPGDGATAGAALVRHPD-VKRIALIGSVPTGRAImraAAEGIKHVTLELGGKN 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 287 WKLIGPDYDPswsDYVAwqcdeDA------YNASGQKCSAQSILFVHKNWEQDLLLKLKQLAERRKL-----ENLSIGPV 355
Cdd:cd07107 230 ALIVFPDADP---EAAA-----DAavagmnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVgdptdPATTMGPL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 356 ltwNNDQLFNHINSLLEIP---GTTCLFGGTELESHNIPKIYgSIKPTavsipVNQLLGKDFELITSEVFGPVQVIVVYE 432
Cdd:cd07107 302 ---VSRQQYDRVMHYIDSAkreGARLVTGGGRPEGPALEGGF-YVEPT-----VFADVTPGMRIAREEIFGPVLSVLRWR 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 433 DQDlpTIMEALEKIPQNLTAAVVSNDVHFQQKVL-----GYT-VNGTTyagmrarttgapqNHWFG-PSGDPRSAGIGTP 505
Cdd:cd07107 373 DEA--EMVAQANGVEYGLTAAIWTNDISQAHRTArrveaGYVwINGSS-------------RHFLGaPFGGVKNSGIGRE 437
|
...
gi 167041430 506 EAI 508
Cdd:cd07107 438 ECL 440
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
171-444 |
2.66e-12 |
|
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: 68.80 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 171 YRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISA 250
Cdd:cd07109 114 VREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 251 ASDkIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDydpswsdyvawqCDEDA----------YNAsGQK 317
Cdd:cd07109 194 HPG-VDHISFTGSVETGIAVmraAAENVVPVTLELGGKSPQIVFAD------------ADLEAalpvvvnaiiQNA-GQT 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 318 CSAQSILFVHKNWEQDLLLKLKQLAERRK----LENLSIGPVltwNNDQLFNHINSLLEIP---GTTCLFGGTELESHNI 390
Cdd:cd07109 260 CSAGSRLLVHRSIYDEVLERLVERFRALRvgpgLEDPDLGPL---ISAKQLDRVEGFVARArarGARIVAGGRIAEGAPA 336
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 167041430 391 PKIYgsIKPTAVSiPVNqllgKDFELITSEVFGPVQVIVVYEDQDlptimEALE 444
Cdd:cd07109 337 GGYF--VAPTLLD-DVP----PDSRLAQEEIFGPVLAVMPFDDEA-----EAIA 378
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
119-443 |
4.03e-12 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 69.23 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 119 LIQRVMPKSSNQCLGEVTVTRKFLENFSGDgVRflaRSFSNpgdhlgqesSGYRwPFGSVVIVAPFNFPLEIPALQFLGA 198
Cdd:PRK11809 727 LLVREAGKTFSNAIAEVREAVDFLRYYAGQ-VR---DDFDN---------DTHR-PLGPVVCISPWNFPLAIFTGQVAAA 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 199 LFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISaASDKIRMVQFTGSCAVAERIAADTNGkv 278
Cdd:PRK11809 793 LAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALV-ADARVRGVMFTGSTEVARLLQRNLAG-- 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 279 RVEDAGFNWKLIGPD-------YDPSW------SDYVAwqcdeDAYNASGQKCSAQSILFVHKNweqdlllklkqLAER- 344
Cdd:PRK11809 870 RLDPQGRPIPLIAETggqnamiVDSSAlteqvvADVLA-----SAFDSAGQRCSALRVLCLQDD-----------VADRt 933
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 345 --------RKL-----ENLS--IGPVLTWN-NDQLFNHINSL---------LEIPGTTCLFGGTeleshnipkiygSIKP 399
Cdd:PRK11809 934 lkmlrgamAECrmgnpDRLStdIGPVIDAEaKANIERHIQAMrakgrpvfqAARENSEDWQSGT------------FVPP 1001
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 167041430 400 TAVSIpvnqllgKDFELITSEVFGPVQVIVVYEDQDLPTIMEAL 443
Cdd:PRK11809 1002 TLIEL-------DSFDELKREVFGPVLHVVRYNRNQLDELIEQI 1038
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
148-459 |
8.06e-12 |
|
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: 67.35 E-value: 8.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 148 DGVRFLA---RSFSNP--GDHL-GQESSGYRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFL 221
Cdd:cd07092 86 DNFRFFAgaaRTLEGPaaGEYLpGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 222 RLLIHcGLPATDADMVHCRGSKMGKLIsAASDKIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDpsw 298
Cdd:cd07092 166 ELAAE-VLPPGVVNVVCGGGASAGDAL-VAHPRVRMVSLTGSVRTGKKVaraAADTLKRVHLELGGKAPVIVFDDAD--- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 299 SDYVAWQCDEDAYNASGQKCSAQSILFVHKNWEQDLLLKLKQLAERRKL-----ENLSIGPVltwNNDQLFNHINSLLE- 372
Cdd:cd07092 241 LDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVgdpddEDTEMGPL---NSAAQRERVAGFVEr 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 373 IPGTTC-LFGGTELEShniPKIYgsIKPTAVSiPVNQllgkDFELITSEVFGPVQVIVVYEDQDlptimEALEK---IPQ 448
Cdd:cd07092 318 APAHARvLTGGRRAEG---PGYF--YEPTVVA-GVAQ----DDEIVQEEIFGPVVTVQPFDDED-----EAIELandVEY 382
|
330
....*....|.
gi 167041430 449 NLTAAVVSNDV 459
Cdd:cd07092 383 GLASSVWTRDV 393
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
171-459 |
1.66e-11 |
|
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: 66.18 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 171 YRWPFGSVVIVAPFNFPLEIPALQFLGALFMGN----RPLIKSATTVGIVFEqflrLLIHCGLPATDADMVHCRGSKMGK 246
Cdd:cd07101 115 NRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNavvlKPDSQTALTALWAVE----LLIEAGLPRDLWQVVTGPGSEVGG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 247 LISAASDkirMVQFTGSCA----VAERIAADTNGkVRVEDAGFNWKLIGPDYDPswsDYVAWQCDEDAYNASGQKCSAQS 322
Cdd:cd07101 191 AIVDNAD---YVMFTGSTAtgrvVAERAGRRLIG-CSLELGGKNPMIVLEDADL---DKAAAGAVRACFSNAGQLCVSIE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 323 ILFVHknwEQDLLLKLKQLAERrkLENLSIGPVLTWNND--------QL---FNHINSLLEiPGTTCLFGGtelesHNIP 391
Cdd:cd07101 264 RIYVH---ESVYDEFVRRFVAR--TRALRLGAALDYGPDmgslisqaQLdrvTAHVDDAVA-KGATVLAGG-----RARP 332
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167041430 392 KI----YgsiKPTAvsipvnqLLG--KDFELITSEVFGPVQVIVVYEDQDlptimEALEK---IPQNLTAAVVSNDV 459
Cdd:cd07101 333 DLgpyfY---EPTV-------LTGvtEDMELFAEETFGPVVSIYRVADDD-----EAIELandTDYGLNASVWTRDG 394
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
110-475 |
1.77e-11 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 65.91 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 110 KEVEDFFVHLIQRVMPKSSNQCLGEVTVTRKFLENFSGdgvrfLARSFSN---PGDHLGQESSGYRWPFGSVVIVAPFNF 186
Cdd:PRK10090 9 RERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAE-----WARRYEGeiiQSDRPGENILLFKRALGVTTGILPWNF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 187 PLEIPALQFLGALFMGNRPLIK-SATTVGIVFEqFLRLLIHCGLPATDADMVHCRGSKMGKLIsAASDKIRMVQFTGSCA 265
Cdd:PRK10090 84 PFFLIARKMAPALLTGNTIVIKpSEFTPNNAIA-FAKIVDEIGLPKGVFNLVLGRGETVGQEL-AGNPKVAMVSMTGSVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 266 VAERI--AADTN-GKVRVEDAGFNWKLIGPDYDPSWSdyVAWQCDEDAYNaSGQKCSAQSILFVHKNW---------EQD 333
Cdd:PRK10090 162 AGEKImaAAAKNiTKVCLELGGKAPAIVMDDADLDLA--VKAIVDSRVIN-SGQVCNCAERVYVQKGIydqfvnrlgEAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 334 LLLKLKQLAERRKLEnlsIGPVLtwnNDQLFNHINSLLEIP---GTTCLFGGTELESHnipkiyGSIKPTAVSIPVNQll 410
Cdd:PRK10090 239 QAVQFGNPAERNDIA---MGPLI---NAAALERVEQKVARAveeGARVALGGKAVEGK------GYYYPPTLLLDVRQ-- 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167041430 411 gkDFELITSEVFGPVQVIVVYEdqdlpTIMEALEKIPQN---LTAAVVSNDVHFQQKVLGYTVNGTTY 475
Cdd:PRK10090 305 --EMSIMHEETFGPVLPVVAFD-----TLEEAIAMANDSdygLTSSIYTQNLNVAMKAIKGLKFGETY 365
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
174-459 |
2.12e-11 |
|
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: 66.01 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 174 PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISAASD 253
Cdd:cd07143 144 PIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMD 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 254 kIRMVQFTGSCAVAERI---AADTN-GKVRVEDAGFNWKLIGPDYDpsWSDYVAWQCDEDAYNaSGQKCSAQSILFVHKN 329
Cdd:cd07143 224 -IDKVAFTGSTLVGRKVmeaAAKSNlKKVTLELGGKSPNIVFDDAD--LESAVVWTAYGIFFN-HGQVCCAGSRIYVQEG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 330 WEQDLLLKLKQLAERRKL-----ENLSIGP-VLTWNNDQLFNHINSLLEiPGTTCLFGGTEL--ESHNI-PKIYGSIKPt 400
Cdd:cd07143 300 IYDKFVKRFKEKAKKLKVgdpfaEDTFQGPqVSQIQYERIMSYIESGKA-EGATVETGGKRHgnEGYFIePTIFTDVTE- 377
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167041430 401 avsipvnqllgkDFELITSEVFGPVQVIVVYEDQDlptimEALEKIPQN---LTAAVVSNDV 459
Cdd:cd07143 378 ------------DMKIVKEEIFGPVVAVIKFKTEE-----EAIKRANDStygLAAAVFTNNI 422
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
172-460 |
2.82e-11 |
|
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: 65.65 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 172 RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIK-----SATTVgivfeQFLRLLIHCGLPATDADMVHCRGSKMGK 246
Cdd:cd07114 117 REPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKpsehtPASTL-----ELAKLAEEAGFPPGVVNVVTGFGPETGE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 247 LISAASDkIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDPswsdyvawqcdEDAYN--------ASG 315
Cdd:cd07114 192 ALVEHPL-VAKIAFTGGTETGRHIaraAAENLAPVTLELGGKSPNIVFDDADL-----------DAAVNgvvagifaAAG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 316 QKCSAQSILFVHKNWEQDLLLKLKQLAERRKL-----ENLSIGPVLTwnnDQLFNHINSLLEI---PGTTCLFGGTELES 387
Cdd:cd07114 260 QTCVAGSRLLVQRSIYDEFVERLVARARAIRVgdpldPETQMGPLAT---ERQLEKVERYVARareEGARVLTGGERPSG 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167041430 388 HNIPKIYgSIKPTAVSIPVNqllgkDFELITSEVFGPVQVIVVYEDQDlptimEALEK---IPQNLTAAVVSNDVH 460
Cdd:cd07114 337 ADLGAGY-FFEPTILADVTN-----DMRIAQEEVFGPVLSVIPFDDEE-----EAIALandSEYGLAAGIWTRDLA 401
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
172-459 |
6.31e-11 |
|
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: 64.45 E-value: 6.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 172 RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIK----SATTVGIVFEqflrlLIH-CGLPATDADMVHCRGSKMGK 246
Cdd:cd07138 128 REPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKpsevAPLSAIILAE-----ILDeAGLPAGVFNLVNGDGPVVGE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 247 LISAASDkIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDpswSDYVAWQCDEDAYNASGQKCSAQSI 323
Cdd:cd07138 203 ALSAHPD-VDMVSFTGSTRAGKRVaeaAADTVKRVALELGGKSANIILDDAD---LEKAVPRGVAACFANSGQSCNAPTR 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 324 LFVHKNWEQDLLLKLKQLAERRKL-----ENLSIGPVLtwnNDQLFNHINSLLEI---PGTTCLFGGTELeSHNIPKIYg 395
Cdd:cd07138 279 MLVPRSRYAEAEEIAAAAAEAYVVgdprdPATTLGPLA---SAAQFDRVQGYIQKgieEGARLVAGGPGR-PEGLERGY- 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167041430 396 SIKPTAVSiPVNqllgKDFELITSEVFGPVQVIVVYEDQDlptimEALEkI----PQNLTAAVVSNDV 459
Cdd:cd07138 354 FVKPTVFA-DVT----PDMTIAREEIFGPVLSIIPYDDED-----EAIA-IandtPYGLAGYVWSADP 410
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
174-465 |
6.92e-11 |
|
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: 64.24 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 174 PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIK---SATTVGIVFEQFLR-LLIHCGLPATDADMVHCRGSKMGKLIS 249
Cdd:cd07098 120 PLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKvseQVAWSSGFFLSIIReCLAACGHDPDLVQLVTCLPETAEALTS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 250 aaSDKIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDPSWSDYVaWQCDedAYNASGQKCSAQSILFV 326
Cdd:cd07098 200 --HPVIDHITFIGSPPVGKKVmaaAAESLTPVVLELGGKDPAIVLDDADLDQIASI-IMRG--TFQSSGQNCIGIERVIV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 327 HKNweqDLLLKLKQLAERrkLENLSIGPVLTWNND-------QLFNHINSLLE---IPGTTCLFGGTELESHNIPKiyGS 396
Cdd:cd07098 275 HEK---IYDKLLEILTDR--VQALRQGPPLDGDVDvgamispARFDRLEELVAdavEKGARLLAGGKRYPHPEYPQ--GH 347
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167041430 397 IKPTAVSIPVNQllgkDFELITSEVFGPVQVIVVYEDQDlptimEALE---KIPQNLTAAVVSNDVHFQQKV 465
Cdd:cd07098 348 YFPPTLLVDVTP----DMKIAQEEVFGPVMVVMKASDDE-----EAVEianSTEYGLGASVFGKDIKRARRI 410
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
33-460 |
9.70e-11 |
|
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: 63.90 E-value: 9.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 33 QNLLSGEWLDTSK--YFDNIpDPVSGEYFIDIPDTDDlsgfiqnldicpksglhnpiKNVERYVMLGNVCAKAAALLSNK 110
Cdd:cd07559 2 DNFINGEWVAPSKgeYFDNY-NPVNGKVLCEIPRSTA--------------------EDVDLAVDAAHEAFKTWGKTSVA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 111 EVEDFFVHLIQRVMpksSNQclgEVTVTRKFLENfsGDGVR-FLARSFSNPGDH--------LGQESSG----------- 170
Cdd:cd07559 61 ERANILNKIADRIE---ENL---ELLAVAETLDN--GKPIReTLAADIPLAIDHfryfagviRAQEGSLseidedtlsyh 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 171 YRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCgLPATDADMVHCRGSKMGKLIsA 250
Cdd:cd07559 133 FHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPL-A 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 251 ASDKIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPD---YDPSWSDYVAWQCDEDAYNaSGQKCSAQSIL 324
Cdd:cd07559 211 SHPRIAKLAFTGSTTVGRLImqyAAENLIPVTLELGGKSPNIFFDDamdADDDFDDKAEEGQLGFAFN-QGEVCTCPSRA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 325 FVHknwEQDLLLKLKQLAERrkLENLSIGPVL--------TWNNDQLfNHINSLLEI---PGTTCLFGGTELESHNIPKI 393
Cdd:cd07559 290 LVQ---ESIYDEFIERAVER--FEAIKVGNPLdpetmmgaQVSKDQL-EKILSYVDIgkeEGAEVLTGGERLTLGGLDKG 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 394 YgSIKPTAVSIPVNqllgkDFELITSEVFGPVQVIVVYEDQDlptimEALE---KIPQNLTAAVVSNDVH 460
Cdd:cd07559 364 Y-FYEPTLIKGGNN-----DMRIFQEEIFGPVLAVITFKDEE-----EAIAianDTEYGLGGGVWTRDIN 422
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
165-459 |
1.48e-10 |
|
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: 63.52 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 165 GQESSGYRWPFGSVVIVAPFNFP--LEIPALQflGALFMGNRPLIKSATTVGIVFEQFLRLLIHC-GLPATDADMVHCRG 241
Cdd:cd07120 108 GSFSLVLREPMGVAGIIVPWNSPvvLLVRSLA--PALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 242 SKMGKLIsAASDKIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDpswSDYVAWQCDEDAYNASGQKC 318
Cdd:cd07120 186 SEGAAHL-VASPDVDVISFTGSTATGRAImaaAAPTLKRLGLELGGKTPCIVFDDAD---LDAALPKLERALTIFAGQFC 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 319 SAQSILFVHKNWEQDLLLKLKQLAERRKLENLS-----IGPVLTWNN-DQLFNHINSLLEIPGTTCLFGGTELESHNIPK 392
Cdd:cd07120 262 MAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLdpasdMGPLIDRANvDRVDRMVERAIAAGAEVVLRGGPVTEGLAKGA 341
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 393 IYgsiKPTAVSIPVNQLLgkdfeLITSEVFGPVQVIVVYEDQDlptimEALEKIPQN---LTAAVVSNDV 459
Cdd:cd07120 342 FL---RPTLLEVDDPDAD-----IVQEEIFGPVLTLETFDDEA-----EAVALANDTdygLAASVWTRDL 398
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
172-459 |
2.14e-10 |
|
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: 62.65 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 172 RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISaa 251
Cdd:cd07147 121 RFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVT-- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 252 SDKIRMVQFTGSCAVAERIAADTnGKVRV--EDAGFNWKLIGPDYDpswSDYVAWQCDEDAYNASGQKC-SAQSIlFVHK 328
Cdd:cd07147 199 DERIKLLSFTGSPAVGWDLKARA-GKKKVvlELGGNAAVIVDSDAD---LDFAAQRIIFGAFYQAGQSCiSVQRV-LVHR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 329 NWEQDLLLKLKQLAERRKL-----ENLSIGPVLTWNN-DQLFNHINSLLEiPGTTCLFGGTELEShnipkiygSIKPTav 402
Cdd:cd07147 274 SVYDEFKSRLVARVKALKTgdpkdDATDVGPMISESEaERVEGWVNEAVD-AGAKLLTGGKRDGA--------LLEPT-- 342
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167041430 403 sIPVNqlLGKDFELITSEVFGPVQVIVVYED---------------------QDLPTIMEALEKIPqnlTAAVVSNDV 459
Cdd:cd07147 343 -ILED--VPPDMEVNCEEVFGPVVTVEPYDDfdealaavndskfglqagvftRDLEKALRAWDELE---VGGVVINDV 414
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
172-503 |
3.33e-10 |
|
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: 62.07 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 172 RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISAA 251
Cdd:cd07115 115 REPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 252 SDkIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYD-PSWSDYVAWQCdedaYNASGQKCSAQSILFVH 327
Cdd:cd07115 195 PD-VDKITFTGSTAVGRKImqgAAGNLKRVSLELGGKSANIVFADADlDAAVRAAATGI----FYNQGQMCTAGSRLLVH 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 328 KNWEQDLLLKLKQLAERRKLEN-----LSIGPVLTwnnDQLFNHINSLLEI---PGTTCLFGGTELESHNI---PKIYGS 396
Cdd:cd07115 270 ESIYDEFLERFTSLARSLRPGDpldpkTQMGPLVS---QAQFDRVLDYVDVgreEGARLLTGGKRPGARGFfvePTIFAA 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 397 IKPtavsipvnqllgkDFELITSEVFGPVQVIVVYEDQDlptimEAL---EKIPQNLTAAVVSNDVHFQQKVLGYTVNGT 473
Cdd:cd07115 347 VPP-------------EMRIAQEEIFGPVVSVMRFRDEE-----EALriaNGTEYGLAAGVWTRDLGRAHRVAAALKAGT 408
|
330 340 350
....*....|....*....|....*....|.
gi 167041430 474 TYAGMRART-TGAPqnhwFGPSGDprsAGIG 503
Cdd:cd07115 409 VWINTYNRFdPGSP----FGGYKQ---SGFG 432
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
160-460 |
6.26e-10 |
|
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: 61.55 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 160 PGDHLGQESSGYRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSAT----TVGIVFEqflRLLIHCGLPATDAD 235
Cdd:cd07151 116 PSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASdtpiTGGLLLA---KIFEEAGLPKGVLN 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 236 MVHCRGSKMG---------KLISaasdkirmvqFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDPswsdyva 303
Cdd:cd07151 193 VVVGAGSEIGdafvehpvpRLIS----------FTGSTPVGRHIgelAGRHLKKVALELGGNNPFVVLEDADI------- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 304 wqcdEDAYNA--------SGQKCSAQSILFVHknwEQDLLLKLKQLAERRK--------LENLSIGPVLtwNNDQlfnhI 367
Cdd:cd07151 256 ----DAAVNAavfgkflhQGQICMAINRIIVH---EDVYDEFVEKFVERVKalpygdpsDPDTVVGPLI--NESQ----V 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 368 NSLLEI------PGTTCLFGGteleshnipKIYGSIKPTAVSIPVNQllgkDFELITSEVFGPVQVIVVYEDQDlptimE 441
Cdd:cd07151 323 DGLLDKieqaveEGATLLVGG---------EAEGNVLEPTVLSDVTN----DMEIAREEIFGPVAPIIKADDEE-----E 384
|
330 340
....*....|....*....|..
gi 167041430 442 ALE---KIPQNLTAAVVSNDVH 460
Cdd:cd07151 385 ALElanDTEYGLSGAVFTSDLE 406
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
172-435 |
6.40e-10 |
|
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: 61.32 E-value: 6.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 172 RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCgLPATDADMVHCRGSKMGKLISAA 251
Cdd:cd07117 134 REPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNH 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 252 SDkIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDpsWSDYVAWQCDEDAYNaSGQKCSAQSILFVHK 328
Cdd:cd07117 213 PG-LDKLAFTGSTEVGRDVaiaAAKKLIPATLELGGKSANIIFDDAN--WDKALEGAQLGILFN-QGQVCCAGSRIFVQE 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 329 NweqdlLLKLKQLAERRKLENLSIGpvLTWN---------NDQLFNHINSLLEI---PGTTCLFGGTELESHNIPKIYgS 396
Cdd:cd07117 289 G-----IYDEFVAKLKEKFENVKVG--NPLDpdtqmgaqvNKDQLDKILSYVDIakeEGAKILTGGHRLTENGLDKGF-F 360
|
250 260 270
....*....|....*....|....*....|....*....
gi 167041430 397 IKPTAVSIPVNqllgkDFELITSEVFGPVQVIVVYEDQD 435
Cdd:cd07117 361 IEPTLIVNVTN-----DMRVAQEEIFGPVATVIKFKTED 394
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
174-459 |
1.67e-09 |
|
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: 59.85 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 174 PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIK-SATTVGIVfeqfLRL--LIHCGLPA------TDADMVhcrgskm 244
Cdd:cd07106 114 PLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKpSPFTPLCT----LKLgeLAQEVLPPgvlnvvSGGDEL------- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 245 GKLISAASDkIRMVQFTGSCAVAERI---AADTNGKVRVE----DAGfnwkLIGPDYDPswsDYVAWQCDEDAYNASGQK 317
Cdd:cd07106 183 GPALTSHPD-IRKISFTGSTATGKKVmasAAKTLKRVTLElggnDAA----IVLPDVDI---DAVAPKLFWGAFINSGQV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 318 CSAQSILFVHKNWEQDLLLKLKQLAERRKL-----ENLSIGPVltwNNDQLFNHINSLLE---IPGTTCLFGGTELES-- 387
Cdd:cd07106 255 CAAIKRLYVHESIYDEFCEALVALAKAAVVgdgldPGTTLGPV---QNKMQYDKVKELVEdakAKGAKVLAGGEPLDGpg 331
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167041430 388 HNIPkiygsikPTAVSIPVNqllgkDFELITSEVFGPVQVIVVYEDQDlptimEALEKIPQN---LTAAVVSNDV 459
Cdd:cd07106 332 YFIP-------PTIVDDPPE-----GSRIVDEEQFGPVLPVLKYSDED-----EVIARANDSeygLGASVWSSDL 389
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
161-324 |
2.37e-09 |
|
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: 59.45 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 161 GDHLGQESSG-----YRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDAD 235
Cdd:cd07085 118 GEYLENVARGidtysYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLN 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 236 MVHCRGSKMGKLISAAsdKIRMVQFTGSCAVAERI--AADTNGKvRVEDAG--FNWKLIGPDYDPswsDYVAWQCDEDAY 311
Cdd:cd07085 198 VVHGGKEAVNALLDHP--DIKAVSFVGSTPVGEYIyeRAAANGK-RVQALGgaKNHAVVMPDADL---EQTANALVGAAF 271
|
170
....*....|...
gi 167041430 312 NASGQKCSAQSIL 324
Cdd:cd07085 272 GAAGQRCMALSVA 284
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
171-465 |
2.83e-09 |
|
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: 59.29 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 171 YRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISA 250
Cdd:cd07110 117 RREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 251 ASDkIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDPSWSdyVAWQCDEDAYNAsGQKCSAQSILFVH 327
Cdd:cd07110 197 HPG-IDKISFTGSTATGSQVmqaAAQDIKPVSLELGGKSPIIVFDDADLEKA--VEWAMFGCFWNN-GQICSATSRLLVH 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 328 KNWEQDLLLKLKQLAERRKL-----ENLSIGPVLTWNN-DQLFNHINSLLEiPGTTCLFGGTELEshNIPKIYgSIKPTA 401
Cdd:cd07110 273 ESIADAFLERLATAAEAIRVgdpleEGVRLGPLVSQAQyEKVLSFIARGKE-EGARLLCGGRRPA--HLEKGY-FIAPTV 348
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167041430 402 VSIPvnqllGKDFELITSEVFGPVQVIVVYEDQDlptimEALEKIPQN---LTAAVVSNDVHFQQKV 465
Cdd:cd07110 349 FADV-----PTDSRIWREEIFGPVLCVRSFATED-----EAIALANDSeygLAAAVISRDAERCDRV 405
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
174-459 |
2.87e-09 |
|
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: 59.43 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 174 PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISAASD 253
Cdd:cd07142 141 PIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMD 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 254 kIRMVQFTGSCAVAERI---AADTNGK-VRVEDAGFNWKLIGPDYDPSwsdyvawQCDEDAYNA----SGQKCSAQSILF 325
Cdd:cd07142 221 -VDKVAFTGSTEVGKIImqlAAKSNLKpVTLELGGKSPFIVCEDADVD-------KAVELAHFAlffnQGQCCCAGSRTF 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 326 VHKNWEQDLLLKLKQLAERRKL-----ENLSIGPVLtwNNDQlFNHINSLLEI---PGTTCLFGGTELEShnipKIYgSI 397
Cdd:cd07142 293 VHESIYDEFVEKAKARALKRVVgdpfrKGVEQGPQV--DKEQ-FEKILSYIEHgkeEGATLITGGDRIGS----KGY-YI 364
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167041430 398 KPTAVSIpvnqlLGKDFELITSEVFGPVQVIVVYEDQDlptimEALEKIPQN---LTAAVVSNDV 459
Cdd:cd07142 365 QPTIFSD-----VKDDMKIARDEIFGPVQSILKFKTVD-----EVIKRANNSkygLAAGVFSKNI 419
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
135-459 |
6.26e-09 |
|
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: 58.20 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 135 VTVTRKFlenfsgDGVRFLARSFSNPGDH-----LGQESSG-----YRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNR 204
Cdd:cd07148 81 VEVTRAI------DGVELAADELGQLGGReipmgLTPASAGriaftTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 205 PLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISaaSDKIRMVQFTGSCAVA----ERIAADTngKVRV 280
Cdd:cd07148 155 VIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVT--DPRVAFFSFIGSARVGwmlrSKLAPGT--RCAL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 281 EDAGFNWKLIGPDYDpswSDYVAWQCDEDAYNASGQKC-SAQSIlFVHKNWEQDLLLKLKQLAERRK-----LENLSIGP 354
Cdd:cd07148 231 EHGGAAPVIVDRSAD---LDAMIPPLVKGGFYHAGQVCvSVQRV-FVPAEIADDFAQRLAAAAEKLVvgdptDPDTEVGP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 355 ---------VLTWNNDQLfnhinslleIPGTTCLFGGTELEShnipkiyGSIKPTAVSIPvnqllGKDFELITSEVFGPv 425
Cdd:cd07148 307 lirprevdrVEEWVNEAV---------AAGARLLCGGKRLSD-------TTYAPTVLLDP-----PRDAKVSTQEIFGP- 364
|
330 340 350
....*....|....*....|....*....|....
gi 167041430 426 qVIVVYEDQDLPTIMEALEKIPQNLTAAVVSNDV 459
Cdd:cd07148 365 -VVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDL 397
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
160-459 |
1.21e-08 |
|
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: 57.20 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 160 PGDHLGQESSGYRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHC 239
Cdd:cd07105 84 PSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTH 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 240 RGSKMGKLISA--ASDKIRMVQFTGSCAVAeRIAADTNGK----VRVEDAGFNWKLIGPDYDpswSDYVAWQCDEDAYNA 313
Cdd:cd07105 164 SPEDAPEVVEAliAHPAVRKVNFTGSTRVG-RIIAETAAKhlkpVLLELGGKAPAIVLEDAD---LDAAANAALFGAFLN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 314 SGQKCSAQSILFVHKNWEQDLLLKLKQLAERRKLENLSIGPVLtwnNDQLFNHINSLLE---IPGTTCLFGGTELESHNI 390
Cdd:cd07105 240 SGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVLGSLV---SAAAADRVKELVDdalSKGAKLVVGGLADESPSG 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167041430 391 pkiyGSIKPTAVSiPVNqllgKDFELITSEVFGPVQVIVVYEDQDlptimEALEKIpqN-----LTAAVVSNDV 459
Cdd:cd07105 317 ----TSMPPTILD-NVT----PDMDIYSEESFGPVVSIIRVKDEE-----EAVRIA--NdseygLSAAVFTRDL 374
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
91-460 |
2.29e-08 |
|
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: 56.46 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 91 ERYVMLGNVcakAAALLSNKEVedfFVHLIQRVMPKSSNQCLGEVTVTRKFLENFSGDGVRFLARSFSNPGDHL-GQESS 169
Cdd:cd07099 41 GRAQRLLRW---KRALADHADE---LAELLHAETGKPRADAGLEVLLALEAIDWAARNAPRVLAPRKVPTGLLMpNKKAT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 170 GYRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIK-SATTVGIVfeQFLRLLIHCGLPATDA-DMVHCRGSKMGKL 247
Cdd:cd07099 115 VEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKpSEVTPLVG--ELLAEAWAAAGPPQGVlQVVTGDGATGAAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 248 ISAASDKIrmvQFTGSCAVAERI---AADTNGKVRVEDAGfnwKligpdyDPSwsdYVAWQCD-EDAYNA--------SG 315
Cdd:cd07099 193 IDAGVDKV---AFTGSVATGRKVmaaAAERLIPVVLELGG---K------DPM---IVLADADlERAAAAavwgamvnAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 316 QKCSA-------QSIL--FVHKnweqdlllklkQLAERRKL-------ENLSIGPVLTWNN-DQLFNHINSLLEiPGTTC 378
Cdd:cd07099 258 QTCISvervyvhESVYdeFVAR-----------LVAKARALrpgaddiGDADIGPMTTARQlDIVRRHVDDAVA-KGAKA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 379 LFGGTELeshNIPKIYgsIKPTaVSIPVNQllgkDFELITSEVFGPVQVIVVYEDQDlptimEALEKI---PQNLTAAVV 455
Cdd:cd07099 326 LTGGARS---NGGGPF--YEPT-VLTDVPH----DMDVMREETFGPVLPVMPVADED-----EAIALAndsRYGLSASVF 390
|
....*
gi 167041430 456 SNDVH 460
Cdd:cd07099 391 SRDLA 395
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
172-435 |
2.65e-08 |
|
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: 56.10 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 172 RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIK-------SATTVGivfeqflRLLIHCGLPATDADMVHCRGSKM 244
Cdd:cd07089 121 REPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKpapdtplSALLLG-------EIIAETDLPAGVVNVVTGSDNAV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 245 GKLISaASDKIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDPS--WSDYVAWQCdedayNASGQKCS 319
Cdd:cd07089 194 GEALT-TDPRVDMVSFTGSTAVGRRImaqAAATLKRVLLELGGKSANIVLDDADLAaaAPAAVGVCM-----HNAGQGCA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 320 AQSILFVHKNWEQDLLLKLKQLAERRKL-----ENLSIGPVLtwNNDQLfNHINSLLEI---PGTTCLFGGTELESHniP 391
Cdd:cd07089 268 LTTRLLVPRSRYDEVVEALAAAFEALPVgdpadPGTVMGPLI--SAAQR-DRVEGYIARgrdEGARLVTGGGRPAGL--D 342
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 167041430 392 KIYgSIKPTAVSIPVNqllgkDFELITSEVFGPVQVIVVYEDQD 435
Cdd:cd07089 343 KGF-YVEPTLFADVDN-----DMRIAQEEIFGPVLVVIPYDDDD 380
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
17-427 |
2.89e-08 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 56.29 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 17 TVDPISGMNSKNPGKAQNLLSGEWLDT-SKYFDNIPDPVSGEYFIDIPDT--DDLSGFIQNLDICPKSGLHNPIKNVERy 93
Cdd:PLN02419 99 STSPEQSTQPQMPPRVPNLIGGSFVESqSSSFIDVINPATQEVVSKVPLTtnEEFKAAVSAAKQAFPLWRNTPITTRQR- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 94 VMLGnvcakaaallsnkevedfFVHLIQRVMPKSSnqcLGEVTVTRKFLENFSGDGVRFL-------ARSFSNPGDHLGQ 166
Cdd:PLN02419 178 VMLK------------------FQELIRKNMDKLA---MNITTEQGKTLKDSHGDIFRGLevvehacGMATLQMGEYLPN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 167 ESSGY-----RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRG 241
Cdd:PLN02419 237 VSNGVdtysiREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTN 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 242 SKMGKLISaaSDKIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPD--YDPSWSDYVAwqcdeDAYNASGQ 316
Cdd:PLN02419 317 DTVNAICD--DEDIRAVSFVGSNTAGMHIyarAAAKGKRIQSNMGAKNHGLVLPDanIDATLNALLA-----AGFGAAGQ 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 317 KCSAQS-ILFV--HKNWEqdlllklKQLAERRKLENLS--------IGPVLTWN-NDQLFNHINSLLEiPGTTCLFGGTE 384
Cdd:PLN02419 390 RCMALStVVFVgdAKSWE-------DKLVERAKALKVTcgsepdadLGPVISKQaKERICRLIQSGVD-DGAKLLLDGRD 461
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 167041430 385 L-----ESHNI--PKIYGSIKPtavsipvnqllgkDFELITSEVFGPVQV 427
Cdd:PLN02419 462 IvvpgyEKGNFigPTILSGVTP-------------DMECYKEEIFGPVLV 498
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
174-501 |
3.19e-08 |
|
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: 55.74 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 174 PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHcrGSK-MGKLIsAAS 252
Cdd:cd07095 97 PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQ--GGReTGEAL-AAH 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 253 DKIRMVQFTGSCAVAERIAADTNGKVRV----EDAGFNWKLIGPDYDPSWSDYVAWQcdeDAYNASGQKCSAQSILFVHK 328
Cdd:cd07095 174 EGIDGLLFTGSAATGLLLHRQFAGRPGKilalEMGGNNPLVVWDVADIDAAAYLIVQ---SAFLTAGQRCTCARRLIVPD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 329 NWEqdllLKLKQLAERRKLENLSIGPvltWNNDQLF------NHINSLLEIPGTTCLFGGTE--LESHNIPKIYGSIKPT 400
Cdd:cd07095 251 GAV----GDAFLERLVEAAKRLRIGA---PDAEPPFmgpliiAAAAARYLLAQQDLLALGGEplLAMERLVAGTAFLSPG 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 401 AVsipvnqLLGKDFELITSEVFGP-VQVIVVyedQDLPTIMEALEKIPQNLTAAVVSND-VHFQQkvlgytvngtTYAGM 478
Cdd:cd07095 324 II------DVTDAADVPDEEIFGPlLQVYRY---DDFDEAIALANATRFGLSAGLLSDDeALFER----------FLARI 384
|
330 340 350
....*....|....*....|....*....|...
gi 167041430 479 RA-------RTTGAPQNHWFG---PSGDPRSAG 501
Cdd:cd07095 385 RAgivnwnrPTTGASSTAPFGgvgLSGNHRPSA 417
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
171-508 |
5.01e-08 |
|
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: 55.24 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 171 YRWPFGSVVIVAPFNFPLeipALQFLG-----ALFMGNrPLI-KS-----ATTVgIVFEQFLRLLIHCGLPATDADMVHC 239
Cdd:cd07129 102 MLVPLGPVAVFGASNFPL---AFSVAGgdtasALAAGC-PVVvKAhpahpGTSE-LVARAIRAALRATGLPAGVFSLLQG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 240 RGSKMG-KLISAAsdKIRMVQFTGS----CAVAERIAADTNGK-VRVEDAGFNWKLIGPDydpswsdyvAWQCDEDA--- 310
Cdd:cd07129 177 GGREVGvALVKHP--AIKAVGFTGSrrggRALFDAAAARPEPIpFYAELGSVNPVFILPG---------ALAERGEAiaq 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 311 -YNAS-----GQKCSAQSILFVHKNWEQDLLLKlkqlAERRKLENLSIGPVLTWNNDQLFNH-INSLLEIPGTTCLFGGT 383
Cdd:cd07129 246 gFVGSltlgaGQFCTNPGLVLVPAGPAGDAFIA----ALAEALAAAPAQTMLTPGIAEAYRQgVEALAAAPGVRVLAGGA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 384 ELESHNIPKiygsikPTAVSIPVNQLLGKdfELITSEVFGPVQVIVVYEDQDlpTIMEALEKIPQNLTAAVVS--NDVHF 461
Cdd:cd07129 322 AAEGGNQAA------PTLFKVDAAAFLAD--PALQEEVFGPASLVVRYDDAA--ELLAVAEALEGQLTATIHGeeDDLAL 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 167041430 462 QQK---VLGYTVNGTTYAGMrarTTG----APQNHWfGP---SGDPRSAGIGTpEAI 508
Cdd:cd07129 392 AREllpVLERKAGRLLFNGW---PTGvevcPAMVHG-GPypaTTDPRFTSVGT-AAI 443
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
172-460 |
7.04e-08 |
|
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: 54.92 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 172 RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSAttvgivfEQ----FLR---LLIHCGLPATDADMVHCRGSKM 244
Cdd:cd07112 122 REPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA-------EQspltALRlaeLALEAGLPAGVLNVVPGFGHTA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 245 GKLISAASDkIRMVQFTGSCAVAERI---AADTNGK-VRVEDAGFNWKLIGPDY-DPswsDYVAWQCDEDAYNASGQKCS 319
Cdd:cd07112 195 GEALGLHMD-VDALAFTGSTEVGRRFleySGQSNLKrVWLECGGKSPNIVFADApDL---DAAAEAAAAGIFWNQGEVCS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 320 AQSILFVHKNWEQDLLLKLKQLAERRKLEN-----LSIGPVLtwnNDQLFNHINSLLEI---PGTTCLFGGTELEshniP 391
Cdd:cd07112 271 AGSRLLVHESIKDEFLEKVVAAAREWKPGDpldpaTRMGALV---SEAHFDKVLGYIESgkaEGARLVAGGKRVL----T 343
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167041430 392 KIYGS-IKPTavsipVNQLLGKDFELITSEVFGPVQVIVVYEDQDlptimEALE---KIPQNLTAAVVSNDVH 460
Cdd:cd07112 344 ETGGFfVEPT-----VFDGVTPDMRIAREEIFGPVLSVITFDSEE-----EAVAlanDSVYGLAASVWTSDLS 406
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
154-442 |
8.44e-08 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 55.26 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 154 ARSFSNPGDHLgqessgyrwPFGSVVIVAPFNFPLEIpalqFLG----ALFMGNRPLIKSATTVGIVFEQFLRLLIHCGL 229
Cdd:PRK11905 665 ARRLLNGPGHK---------PLGPVVCISPWNFPLAI----FTGqiaaALVAGNTVLAKPAEQTPLIAARAVRLLHEAGV 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 230 PatdADMVHC---RGSKMGKLISAASdKIRMVQFTGSCAVAERIA---ADTNGKVRV---EDAGFNWKLIgpDydpswSD 300
Cdd:PRK11905 732 P---KDALQLlpgDGRTVGAALVADP-RIAGVMFTGSTEVARLIQrtlAKRSGPPVPliaETGGQNAMIV--D-----SS 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 301 YVAWQCDED----AYNASGQKCSAQSILFVHKNweqdlllklkqLAER---------RKL-----ENLS--IGPVLTWN- 359
Cdd:PRK11905 801 ALPEQVVADviasAFDSAGQRCSALRVLCLQED-----------VADRvltmlkgamDELrigdpWRLStdVGPVIDAEa 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 360 NDQLFNHINSLLEIpgttclfgGTELESHNIPKIYGS---IKPTAVSIpvnqllgKDFELITSEVFGPVQVIVVYEDQDL 436
Cdd:PRK11905 870 QANIEAHIEAMRAA--------GRLVHQLPLPAETEKgtfVAPTLIEI-------DSISDLEREVFGPVLHVVRFKADEL 934
|
....*.
gi 167041430 437 PTIMEA 442
Cdd:PRK11905 935 DRVIDD 940
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
91-274 |
2.34e-07 |
|
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: 53.20 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 91 ERYVMLGnvcaKAAALLsnKEVEDFFVHLIQRVMPKSSNQCLGEVTVTRKFLENFSGDGVRFLARSFsnPGDHLGQESSG 170
Cdd:cd07103 42 ERAAILR----RWADLI--RERAEDLARLLTLEQGKPLAEARGEVDYAASFLEWFAEEARRIYGRTI--PSPAPGKRILV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 171 YRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSA-----TTVGIVfeqflRLLIHCGLPATDADMVHCRGSKMG 245
Cdd:cd07103 114 IKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAeetplSALALA-----ELAEEAGLPAGVLNVVTGSPAEIG 188
|
170 180 190
....*....|....*....|....*....|..
gi 167041430 246 KLISaASDKIRMVQFTGSCAVAE---RIAADT 274
Cdd:cd07103 189 EALC-ASPRVRKISFTGSTAVGKllmAQAADT 219
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
174-496 |
6.62e-07 |
|
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: 51.84 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 174 PFGSVVIVAPFNFPLeIPALQ-FLGALFMGNRPLIK---SATTVGIVFEQFLRllihcglPATDADMVHC-RGS--KMGK 246
Cdd:cd07135 108 PLGVVLIIGPWNYPV-LLALSpLVGAIAAGCTVVLKpseLTPHTAALLAELVP-------KYLDPDAFQVvQGGvpETTA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 247 LISAASDKIrmvQFTGSCAVAeRI----AADTNGKVRVEDAGFNWKLIGPDYDPS-------WSDYVawqcdedayNAsG 315
Cdd:cd07135 180 LLEQKFDKI---FYTGSGRVG-RIiaeaAAKHLTPVTLELGGKSPVIVTKNADLElaakrilWGKFG---------NA-G 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 316 QKCSAQSILFVHKNWEQDLLLKLKQLAERRKLENLSIGPVLT-WNNDQLFNHINSLLE-IPGTTCLFGGTELESHNIPki 393
Cdd:cd07135 246 QICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTrIVNPRHFNRLKSLLDtTKGKVVIGGEMDEATRFIP-- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 394 ygsikPTAVSIpvnqlLGKDFELITSEVFGPVQVIVVYEdqDLPTIMEALEKIPQNLTAAVVSNDVHFQQKVL------G 467
Cdd:cd07135 324 -----PTIVSD-----VSWDDSLMSEELFGPVLPIIKVD--DLDEAIKVINSRDTPLALYIFTDDKSEIDHILtrtrsgG 391
|
330 340
....*....|....*....|....*....
gi 167041430 468 YTVNGTTYAGMrarTTGAPqnhwFGPSGD 496
Cdd:cd07135 392 VVINDTLIHVG---VDNAP----FGGVGD 413
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
172-458 |
6.89e-07 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 52.04 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 172 RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISAA 251
Cdd:PLN02467 149 KEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASH 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 252 S--DKIrmvQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYD----PSWSDYvawqcdeDAYNASGQKCSAQS 322
Cdd:PLN02467 229 PgvDKI---AFTGSTATGRKImtaAAQMVKPVSLELGGKSPIIVFDDVDldkaVEWAMF-------GCFWTNGQICSATS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 323 ILFVHKNWEQDLLLKLKQLAERRKL-----ENLSIGPVLtwnNDQLFNHINSLLEIP---GTTCLFGGTELESHNipKIY 394
Cdd:PLN02467 299 RLLVHERIASEFLEKLVKWAKNIKIsdpleEGCRLGPVV---SEGQYEKVLKFISTAkseGATILCGGKRPEHLK--KGF 373
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167041430 395 gSIKPTavsIPVNqlLGKDFELITSEVFGPVQVIVVYEDQDlptimEALEKIPQN---LTAAVVSND 458
Cdd:PLN02467 374 -FIEPT---IITD--VTTSMQIWREEVFGPVLCVKTFSTED-----EAIELANDShygLAGAVISND 429
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
174-454 |
8.32e-07 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 51.76 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 174 PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRL----LIHCGLPATDADMVhCRGSKMGKLIS 249
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLvaevLEKNNLPGAIFTSF-CGGAEIGEAIA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 250 AASdKIRMVQFTGSCAVAERIAADTN---GKVRVEDAGFNWKLIGPDYDPSWSdyvAWQCDEDAYNASGQKCSAQSILFV 326
Cdd:PLN02315 233 KDT-RIPLVSFTGSSKVGLMVQQTVNarfGKCLLELSGNNAIIVMDDADIQLA---VRSVLFAAVGTAGQRCTTCRRLLL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 327 HKNWEQDLLLKLKQLAERRK----LENLS-IGPVLTWNNDQLFNHINSLLEIPGTTCLFGGTELESHNipkiyGSIKPTA 401
Cdd:PLN02315 309 HESIYDDVLEQLLTVYKQVKigdpLEKGTlLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEG-----NFVQPTI 383
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 167041430 402 VSIpvnqllGKDFELITSEVFGPvqVIVVYEDQDLPTIMEALEKIPQNLTAAV 454
Cdd:PLN02315 384 VEI------SPDADVVKEELFGP--VLYVMKFKTLEEAIEINNSVPQGLSSSI 428
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
176-443 |
1.20e-06 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 51.35 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 176 GSVVIVAPFNFPLEIpalqFLG----ALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISAA 251
Cdd:PRK11904 686 GVFVCISPWNFPLAI----FLGqvaaALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTAD 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 252 sDKIRMVQFTGSCAVAERI----AADTNGKVRV--EDAGFNwKLIgpdydpswSDYVAW--QCDED----AYNASGQKCS 319
Cdd:PRK11904 762 -PRIAGVAFTGSTETARIInrtlAARDGPIVPLiaETGGQN-AMI--------VDSTALpeQVVDDvvtsAFRSAGQRCS 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 320 AQSILFVHKNweqdlllklkqLAER---------RKL-----ENLS--IGPVLTWNN-DQLFNHINSL---------LEI 373
Cdd:PRK11904 832 ALRVLFVQED-----------IADRviemlkgamAELkvgdpRLLStdVGPVIDAEAkANLDAHIERMkrearllaqLPL 900
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167041430 374 PGTTclfggteLESHNIPkiygsikPTAVSIP-VNQLlgkdfeliTSEVFGPVQVIVVYEDQDLPTIMEAL 443
Cdd:PRK11904 901 PAGT-------ENGHFVA-------PTAFEIDsISQL--------EREVFGPILHVIRYKASDLDKVIDAI 949
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
174-435 |
1.32e-06 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 50.96 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 174 PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSA--TTVGIVFEQflRLLIHCGLPATDADMVHCRGSKMGKLISAA 251
Cdd:PLN02466 195 PIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAeqTPLSALYAA--KLLHEAGLPPGVLNVVSGFGPTAGAALASH 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 252 SDkIRMVQFTGSCAVAERI---AADTNGK-VRVEDAGFNWKLIGPDYDPSwsdyvawQCDEDAYNA----SGQKCSAQSI 323
Cdd:PLN02466 273 MD-VDKLAFTGSTDTGKIVlelAAKSNLKpVTLELGGKSPFIVCEDADVD-------KAVELAHFAlffnQGQCCCAGSR 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 324 LFVHKNWEQDLLLKLKQLAERRKL-----ENLSIGPVLtwNNDQ---LFNHINSLLEiPGTTCLFGGTELEShnipKIYg 395
Cdd:PLN02466 345 TFVHERVYDEFVEKAKARALKRVVgdpfkKGVEQGPQI--DSEQfekILRYIKSGVE-SGATLECGGDRFGS----KGY- 416
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 167041430 396 SIKPTAVS-IPVNQLLGKDfelitsEVFGPVQVIVVYEDQD 435
Cdd:PLN02466 417 YIQPTVFSnVQDDMLIAQD------EIFGPVQSILKFKDLD 451
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
148-328 |
4.04e-06 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 49.52 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 148 DGVRFLA---RSFSNP--GDHL-GQESSGYRWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFL 221
Cdd:PRK13473 106 DVFRFFAgaaRCLEGKaaGEYLeGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 222 RLLIHCgLPATDADMVHCRGSKMGKLIsAASDKIRMVQFTGSCAVAERI---AADTNGKVRVEDAG------FNwkligp 292
Cdd:PRK13473 186 ELAADI-LPPGVLNVVTGRGATVGDAL-VGHPKVRMVSLTGSIATGKHVlsaAADSVKRTHLELGGkapvivFD------ 257
|
170 180 190
....*....|....*....|....*....|....*.
gi 167041430 293 DYDPswsDYVAWQCDEDAYNASGQKCSAQSILFVHK 328
Cdd:PRK13473 258 DADL---DAVVEGIRTFGYYNAGQDCTAACRIYAQR 290
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
174-472 |
4.05e-06 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 49.26 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 174 PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIK----SATTVGIVFEQFLRLLihcglpatDADMVHC--RGSKMGK- 246
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKpselSPHTSKLMAKLLTKYL--------DPSYVRVieGGVEVTTe 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 247 LISAASDKIRmvqFTGSCAVAERI--AADTN---------GK--VRVeDAGFNWKLIGpdydpswsDYVAWQcdeDAYNA 313
Cdd:PTZ00381 181 LLKEPFDHIF---FTGSPRVGKLVmqAAAENltpctlelgGKspVIV-DKSCNLKVAA--------RRIAWG---KFLNA 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 314 sGQKCSAQSILFVHKNWEQDLLLKLkqlAERRK-------LENLSIGPVLtwnNDQLFNHINSLLEIPGTTCLFGGtele 386
Cdd:PTZ00381 246 -GQTCVAPDYVLVHRSIKDKFIEAL---KEAIKeffgedpKKSEDYSRIV---NEFHTKRLAELIKDHGGKVVYGG---- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 387 SHNIPKIYgsIKPTavsIPVNQLLgkDFELITSEVFGPVQVIVVYEDQDlptimEALEKI---PQNLTAAVVSNDVHFQQ 463
Cdd:PTZ00381 315 EVDIENKY--VAPT---IIVNPDL--DSPLMQEEIFGPILPILTYENID-----EVLEFInsrPKPLALYYFGEDKRHKE 382
|
....*....
gi 167041430 464 KVLGYTVNG 472
Cdd:PTZ00381 383 LVLENTSSG 391
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
167-459 |
4.59e-06 |
|
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: 49.13 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 167 ESSGYR----W-PFGSVVIVAPFNFPLEIPALQFLGALFMGN---------RPLIKSATT--VGIVFEQFlrllihcGLP 230
Cdd:cd07130 120 ERPGHRmmeqWnPLGVVGVITAFNFPVAVWGWNAAIALVCGNvvvwkpsptTPLTAIAVTkiVARVLEKN-------GLP 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 231 ATDADMVhCRGSKMGKLIsAASDKIRMVQFTGSCAVAERIA---ADTNGKVRVEDAGFNWKLIGPDYDpswSDYVAWQCD 307
Cdd:cd07130 193 GAIASLV-CGGADVGEAL-VKDPRVPLVSFTGSTAVGRQVGqavAARFGRSLLELGGNNAIIVMEDAD---LDLAVRAVL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 308 EDAYNASGQKCSAQSILFVHKNweqdlllKLKQLAERRK-----------LENLSI-GPVLTWNNDQLFNHINSLLEIPG 375
Cdd:cd07130 268 FAAVGTAGQRCTTTRRLIVHES-------IYDEVLERLKkaykqvrigdpLDDGTLvGPLHTKAAVDNYLAAIEEAKSQG 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 376 TTCLFGGTELEshnIPKIYgsIKPTAVSIPvnqllgKDFELITSEVFGPVQVIVVYEDQDlptimEALE---KIPQNLTA 452
Cdd:cd07130 341 GTVLFGGKVID---GPGNY--VEPTIVEGL------SDAPIVKEETFAPILYVLKFDTLE-----EAIAwnnEVPQGLSS 404
|
....*..
gi 167041430 453 AVVSNDV 459
Cdd:cd07130 405 SIFTTDL 411
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
142-475 |
3.76e-05 |
|
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: 46.14 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 142 LENFSGdgvrfLARSFSnpGDH--LGQESSGY--RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIK-------SA 210
Cdd:cd07090 87 LEYYAG-----LAPTLS--GEHvpLPGGSFAYtrREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKpspftplTA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 211 TTVGIVFEQflrllihCGLPATDADMVHcRGSKMGKLISAASDkIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNW 287
Cdd:cd07090 160 LLLAEILTE-------AGLPDGVFNVVQ-GGGETGQLLCEHPD-VAKVSFTGSVPTGKKVmsaAAKGIKHVTLELGGKSP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 288 KLIGPDydpswsdyvawqCD-EDAYN--------ASGQKCSAQSILFVHKNWEQDLLLKLKQLAERRK-----LENLSIG 353
Cdd:cd07090 231 LIIFDD------------ADlENAVNgammanflSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRigdplDEDTQMG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 354 PVLtwNNDQLfNHINSLLEIP---GTTCLFGGTELESHNIPKIYGSIKPTaVSIPVNQllgkDFELITSEVFGPVQVIVV 430
Cdd:cd07090 299 ALI--SEEHL-EKVLGYIESAkqeGAKVLCGGERVVPEDGLENGFYVSPC-VLTDCTD----DMTIVREEIFGPVMSILP 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 167041430 431 YEDQDlptimEALEK---IPQNLTAAVVSNDVHFQQKVLGYTVNGTTY 475
Cdd:cd07090 371 FDTEE-----EVIRRandTTYGLAAGVFTRDLQRAHRVIAQLQAGTCW 413
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
174-474 |
4.73e-05 |
|
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: 45.68 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 174 PFGSVVIVAPFNFPLEIpALQFL-GALFMGNRPLIK-----SATTvgivfeQFLRLLIHCGLPATDADMVHCRGSKMGKL 247
Cdd:cd07134 100 PKGVCLIISPWNYPFNL-AFGPLvSAIAAGNTAILKpseltPHTS------AVIAKIIREAFDEDEVAVFEGDAEVAQAL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 248 ISAASDKIRmvqFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYD-------PSWSDYVawqcdedayNAsGQK 317
Cdd:cd07134 173 LELPFDHIF---FTGSPAVGKIVmaaAAKHLASVTLELGGKSPTIVDETADlkkaakkIAWGKFL---------NA-GQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 318 CSAQSILFVHKNWEQDLLLKLKQLAERR------KLENLSIGPVLtwnNDQLFNHINSLLEIP---GTTCLFGGTELESH 388
Cdd:cd07134 240 CIAPDYVFVHESVKDAFVEHLKAEIEKFygkdaaRKASPDLARIV---NDRHFDRLKGLLDDAvakGAKVEFGGQFDAAQ 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 389 NIpkiygsIKPTAVSipvNqlLGKDFELITSEVFGPVQVIVVYEDQDlptimEALEKI---PQNLTAAVVSNDVHFQQKV 465
Cdd:cd07134 317 RY------IAPTVLT---N--VTPDMKIMQEEIFGPVLPIITYEDLD-----EVIEYInakPKPLALYVFSKDKANVNKV 380
|
....*....
gi 167041430 466 LGYTVNGTT 474
Cdd:cd07134 381 LARTSSGGV 389
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
174-460 |
7.11e-05 |
|
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: 45.52 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 174 PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSA--TTVGIVfeqFLRLLIHCGLPATDADMVHCRGSKMGKLIsAA 251
Cdd:cd07116 136 PLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAeqTPASIL---VLMELIGDLLPPGVVNVVNGFGLEAGKPL-AS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 252 SDKIRMVQFTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPD--------YDPSWSDYVAWqcdedAYNaSGQKCSA 320
Cdd:cd07116 212 SKRIAKVAFTGETTTGRLImqyASENIIPVTLELGGKSPNIFFADvmdaddafFDKALEGFVMF-----ALN-QGEVCTC 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 321 QSILFVHKNWEQDLLLKLKQLAERRKLEN-LSIGPVL--TWNNDQLfNHINSLLEI---PGTTCLFGGTELESHNIPKIY 394
Cdd:cd07116 286 PSRALIQESIYDRFMERALERVKAIKQGNpLDTETMIgaQASLEQL-EKILSYIDIgkeEGAEVLTGGERNELGGLLGGG 364
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167041430 395 GSIKPTAVSipvnqllGKDFELITSEVFGPVQVIVVYEDQDlptimEALE---KIPQNLTAAVVSNDVH 460
Cdd:cd07116 365 YYVPTTFKG-------GNKMRIFQEEIFGPVLAVTTFKDEE-----EALEianDTLYGLGAGVWTRDGN 421
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
171-271 |
1.34e-04 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 44.48 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 171 YRWPFGSVVIVAPFNFPLEIPALQFLGALFMGN----RPLIKSATTVGIVFEqflrLLIHCGLPATDADMVHCRGSKMGK 246
Cdd:PRK09407 151 LRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNavvlKPDSQTPLTALAAVE----LLYEAGLPRDLWQVVTGPGPVVGT 226
|
90 100
....*....|....*....|....*....
gi 167041430 247 LISAASDkirMVQFTGSCA----VAERIA 271
Cdd:PRK09407 227 ALVDNAD---YLMFTGSTAtgrvLAEQAG 252
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
174-473 |
2.99e-04 |
|
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: 43.28 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 174 PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIK-SATTvgivfeqflrllihcglPATdadmvhcrgSK-MGKLISAA 251
Cdd:cd07087 100 PLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKpSELA-----------------PAT---------SAlLAKLIPKY 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 252 SDK--IRMVQ------------------FTGSCAVAERI---AADTNGKVRVEDAGFNWKLIGPDYDpswSDYVAWQCde 308
Cdd:cd07087 154 FDPeaVAVVEggvevatallaepfdhifFTGSPAVGKIVmeaAAKHLTPVTLELGGKSPCIVDKDAN---LEVAARRI-- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 309 dAY----NAsGQKCSAQSILFVHKNWEqdlllkLKQLAERRK----------LENLSIGPVLtwnNDQLFNHINSLLEip 374
Cdd:cd07087 229 -AWgkflNA-GQTCIAPDYVLVHESIK------DELIEELKKaikefygedpKESPDYGRII---NERHFDRLASLLD-- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 375 GTTCLFGGteleSHNIPKIYgsIKPTAVSIPvnqllGKDFELITSEVFGPVQVIVVYEDQDlptimEALEKI---PQNLT 451
Cdd:cd07087 296 DGKVVIGG----QVDKEERY--IAPTILDDV-----SPDSPLMQEEIFGPILPILTYDDLD-----EAIEFInsrPKPLA 359
|
330 340
....*....|....*....|..
gi 167041430 452 AAVVSNDVHFQQKVLGYTVNGT 473
Cdd:cd07087 360 LYLFSEDKAVQERVLAETSSGG 381
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
132-466 |
3.82e-04 |
|
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: 42.88 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 132 LGEVTVTRKFLENFSGDgvrflaRSFSNPGDHLGQESSGYRWPFGSVVIVAPFNFPLEIpALQFL-GALFMGNRPLIK-S 209
Cdd:cd07136 64 LSEINYAIKHLKKWMKP------KRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQL-ALAPLiGAIAAGNTAVLKpS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 210 ATTvgivfeqflrllihcglPATdadmvhcrgSK-MGKLISAASDK--IRMVQ------------------FTGSCAVAe 268
Cdd:cd07136 137 ELT-----------------PNT---------SKvIAKIIEETFDEeyVAVVEggveenqelldqkfdyifFTGSVRVG- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 269 RI---AADTN---------GKVRV---EDAgfNWKL----IgpdydpSWSDYVawqcdedayNAsGQKCSAQSILFVHKN 329
Cdd:cd07136 190 KIvmeAAAKHltpvtlelgGKSPCivdEDA--NLKLaakrI------VWGKFL---------NA-GQTCVAPDYVLVHES 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 330 WEQDLLLKLKQLAERRKLENLSIGPVLTWN-NDQLFNHINSLLEiPGTTCLFGGTELESHNI-PKIYGSIKPTAvsiPVN 407
Cdd:cd07136 252 VKEKFIKELKEEIKKFYGEDPLESPDYGRIiNEKHFDRLAGLLD-NGKIVFGGNTDRETLYIePTILDNVTWDD---PVM 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167041430 408 QllgkdfelitSEVFGPVQVIVVYEDQDlptimEALEKI---PQNLTAAVVSNDVHFQQKVL 466
Cdd:cd07136 328 Q----------EEIFGPILPVLTYDTLD-----EAIEIIksrPKPLALYLFSEDKKVEKKVL 374
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
102-326 |
1.10e-03 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 41.67 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 102 KAAALLsnKEVEDFFVHLIQRVMPKSSNQCLGEVTVTRKFLENFSGDGVRFLAR-----SFSNPGDHLGQESSGYRWPFG 176
Cdd:PLN00412 83 KAAAIL--KEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEgkflvSDSFPGNERNKYCLTSKIPLG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 177 SVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVfeqfLRLLIHC----GLPATDADMVHCRGSKMGKLISAAS 252
Cdd:PLN00412 161 VVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVA----ALHMVHCfhlaGFPKGLISCVTGKGSEIGDFLTMHP 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167041430 253 DkIRMVQFTG---SCAVAERIaadtnGKV--RVEDAGFNWKLIGPDYDpswSDYVAWQCDEDAYNASGQKCSAQSILFV 326
Cdd:PLN00412 237 G-VNCISFTGgdtGIAISKKA-----GMVplQMELGGKDACIVLEDAD---LDLAAANIIKGGFSYSGQRCTAVKVVLV 306
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
172-326 |
1.54e-03 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 41.03 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 172 RWPFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKMGKLISAA 251
Cdd:PRK09847 155 REPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRH 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 252 SDkIRMVQFTGSCAVAERI---AADTNGK-VRVEDAGFNWKLI---GPDYDPSWSDYVAwqcdEDAYNaSGQKCSAQSIL 324
Cdd:PRK09847 235 ND-IDAIAFTGSTRTGKQLlkdAGDSNMKrVWLEAGGKSANIVfadCPDLQQAASATAA----GIFYN-QGQVCIAGTRL 308
|
..
gi 167041430 325 FV 326
Cdd:PRK09847 309 LL 310
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
166-276 |
1.57e-03 |
|
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: 41.23 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 166 QESSGYRW-PFGSVVIVAPFNFPLEIPALQFLGALFMGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVHCRGSKM 244
Cdd:cd07111 138 LDTELAGWkPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFG 217
|
90 100 110
....*....|....*....|....*....|..
gi 167041430 245 GKLisAASDKIRMVQFTGSCAVAERIAADTNG 276
Cdd:cd07111 218 SAL--ANHPGVDKVAFTGSTEVGRALRRATAG 247
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
102-268 |
1.90e-03 |
|
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: 40.91 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 102 KAAALL-SNKeveDFFVHLIQRVMPKSSNQCLGEV----TVTRKFLENfsgdGVRFLARsfsNPGDHLGQESSGYRWPFG 176
Cdd:cd07100 29 KLADLLrERK---DELARLITLEMGKPIAEARAEVekcaWICRYYAEN----AEAFLAD---EPIETDAGKAYVRYEPLG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 177 SVVIVAPFNFPLeIPALQFLGALFM-GNRPLIKSATTV---GIVFEQflrLLIHCGLPA-------TDADMVhcrgskmG 245
Cdd:cd07100 99 VVLGIMPWNFPF-WQVFRFAAPNLMaGNTVLLKHASNVpgcALAIEE---LFREAGFPEgvfqnllIDSDQV-------E 167
|
170 180
....*....|....*....|....*..
gi 167041430 246 KLIsaASDKIRMVQFTGS----CAVAE 268
Cdd:cd07100 168 AII--ADPRVRGVTLTGSeragRAVAA 192
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
126-328 |
2.59e-03 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 40.44 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 126 KSSNQCLGEVTVTRKFLENFSGDGVRFLarsfsnpGDHLGQESSGYRW-----PFGSVVIVAPFNFPLEIPALQFLGALF 200
Cdd:PLN02278 114 KPLKEAIGEVAYGASFLEYFAEEAKRVY-------GDIIPSPFPDRRLlvlkqPVGVVGAITPWNFPLAMITRKVGPALA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041430 201 MGNRPLIKSATTVGIVFEQFLRLLIHCGLPATDADMVhcrgskMGKL--ISAA---SDKIRMVQFTGSCAVAERI---AA 272
Cdd:PLN02278 187 AGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVV------MGDApeIGDAllaSPKVRKITFTGSTAVGKKLmagAA 260
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 167041430 273 DTNGKVRVEDAGFNWKLIGPDYDpswSDYVAWQCDEDAYNASGQKC-SAQSILfVHK 328
Cdd:PLN02278 261 ATVKRVSLELGGNAPFIVFDDAD---LDVAVKGALASKFRNSGQTCvCANRIL-VQE 313
|
|
| |
