|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
52-528 |
0e+00 |
|
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: 822.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 52 GVYNGEWVAGtAGKVQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKL 131
Cdd:cd07130 1 GVYDGEWGGG-GGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 132 VALEMGKILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTV 211
Cdd:cd07130 80 VSLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 212 GNTVLWKGAPSTSLVSVATTKIVTDVIKRNKLPP-IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFG 290
Cdd:cd07130 160 GNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGaIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 291 RCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLY 370
Cdd:cd07130 240 RSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQV--RIGDPLDDGTLV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 371 GPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISnLPHDAPVVKRETFAPIVYVFKASNLQEAISWNN 450
Cdd:cd07130 318 GPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNN 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158296454 451 EVDQGLSSSLFTNNIQSAFEWLGESGSDCGIVNINTSPSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTITVNHS 528
Cdd:cd07130 397 EVPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
52-528 |
0e+00 |
|
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: 786.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 52 GVYNGEWVAGTAGKVQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKL 131
Cdd:cd07086 1 GVIGGEWVGSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 132 VALEMGKILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTV 211
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 212 GNTVLWKGAPSTSLVSVATTKIVTDVIKRNKLPP-IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFG 290
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPgVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 291 RCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLY 370
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQV--RIGDPLDEGTLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 371 GPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDR--AGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISW 448
Cdd:cd07086 319 GPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 449 NNEVDQGLSSSLFTNNIQSAFEWLGESGSDCGIVNINTSPSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTITVNHS 528
Cdd:cd07086 399 NNDVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
34-539 |
0e+00 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 611.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 34 EEDNFAFLRDLGLQRVNNGVY-NGEWVAGtAGKVQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGD 112
Cdd:PLN02315 4 ARKEYEFLSEIGLSSRNLGCYvGGEWRAN-GPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 113 VIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVIS 192
Cdd:PLN02315 83 IVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 193 AFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSLVSVATTKIVTDVIKRNKLPP-IVTLCQGGEDVGKRMVSDERIRLMSF 271
Cdd:PLN02315 163 AFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGaIFTSFCGGAEIGEAIAKDTRIPLVSF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 272 TGSTAVGRTVGIEMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVK 351
Cdd:PLN02315 243 TGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 352 RYASLlkRVGHPLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISnLPHDAPVVKRETFA 431
Cdd:PLN02315 323 VYKQV--KIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 432 PIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEWLGESGSDCGIVNINTSPSGAEIGGAFGGEKHTGGGRESGS 511
Cdd:PLN02315 400 PVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGS 479
|
490 500
....*....|....*....|....*...
gi 158296454 512 DAWKQYARRSTITVNHSTDLPLAQGIVF 539
Cdd:PLN02315 480 DSWKQYMRRSTCTINYGNELPLAQGINF 507
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
55-527 |
1.74e-159 |
|
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: 462.67 E-value: 1.74e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGK-VQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVA 133
Cdd:COG1012 11 GGEWVAAASGEtFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 134 LEMGKILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGN 213
Cdd:COG1012 91 LETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 214 TVLWKGAPSTSLVSVATTKIVTDVikrnKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGR 291
Cdd:COG1012 171 TVVLKPAEQTPLSALLLAELLEEA----GLPAgVLNVVTGdGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 292 CLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYG 371
Cdd:COG1012 247 VTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKAL--KVGDPLDPGTDMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 372 PVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRA-GFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNN 450
Cdd:COG1012 325 PLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEgGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALAN 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158296454 451 EVDQGLSSSLFTNNIQSAFEWLgeSGSDCGIVNINTSPSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTITVNH 527
Cdd:COG1012 405 DTEYGLAASVFTRDLARARRVA--RRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
58-523 |
9.34e-159 |
|
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: 460.07 E-value: 9.34e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 58 WVAGTAGKVQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMG 137
Cdd:pfam00171 1 WVDSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 138 KILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSeRPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLW 217
Cdd:pfam00171 81 KPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 218 KGAPSTSLVSVATTKIVTDVIkrnkLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLE 295
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEAG----LPAgVLNVVTGsGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 296 LGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHN 375
Cdd:pfam00171 236 LGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKL--KVGDPLDPDTDMGPLIS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 376 QQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQG 455
Cdd:pfam00171 314 KAQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158296454 456 LSSSLFTNNIQSAFEWLGEsgSDCGIVNINTSPSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTI 523
Cdd:pfam00171 394 LAAGVFTSDLERALRVARR--LEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
89-525 |
1.18e-145 |
|
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: 425.85 E-value: 1.18e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 89 ERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQEFVDICDYAVGLSRMFGGAI 168
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 169 FPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSLVSVATTKIVTDVIkrnkLPP-IV 247
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAG----LPPgVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 248 TLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAG 326
Cdd:cd07078 157 NVVTGdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 327 QRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDR- 405
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKAL--KVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGg 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 406 AGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEWLGEsgSDCGIVNIN 485
Cdd:cd07078 315 KGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAER--LEAGTVWIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 158296454 486 TSPSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTITV 525
Cdd:cd07078 393 DYSVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
55-528 |
1.34e-129 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 386.32 E-value: 1.34e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKV-QSIDPASGR-VIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLV 132
Cdd:cd07131 4 GGEWVDSASGETfDSRNPADLEeVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 133 ALEMGKILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVG 212
Cdd:cd07131 84 TREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 213 NTVLWKGAPSTSLvsvATTKIVtDVIKRNKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFG 290
Cdd:cd07131 164 NTVVFKPAEDTPA---CALKLV-ELFAEAGLPPgVVNVVHGrGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 291 RCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLY 370
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRL--RVGDGLDEETDM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 371 GPVHNQQAVD---NYLQTVQEAvalGGKVECGGKVIDR----AGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQ 443
Cdd:cd07131 318 GPLINEAQLEkvlNYNEIGKEE---GATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 444 EAISWNNEVDQGLSSSLFTNNIQSAFEWLGEsgSDCGIVNINTSPSGAEIGGAFGGEKHTGGG-RESGSDAWKQYARRST 522
Cdd:cd07131 395 EAIEIANDTEYGLSSAIYTEDVNKAFRARRD--LEAGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKA 472
|
....*.
gi 158296454 523 ITVNHS 528
Cdd:cd07131 473 VYVDYS 478
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
52-513 |
3.21e-119 |
|
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: 359.64 E-value: 3.21e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 52 GVYNGEWVAGTAGKVqSIDPASGR-VIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGK 130
Cdd:cd07097 3 NYIDGEWVAGGDGEE-NRNPSDTSdVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 131 LVALEMGKILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALT 210
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 211 VGNTVLWKGAPSTSLVSVAttkiVTDVIKRNKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRR 288
Cdd:cd07097 162 YGNTVVFKPAELTPASAWA----LVEILEEAGLPAgVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 289 FGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSAT 368
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKAL--KVGDALDEGV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 369 LYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRA--GFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAI 446
Cdd:cd07097 316 DIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEAL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158296454 447 SWNNEVDQGLSSSLFTNNIQSAFEWlgESGSDCGIVNINTSPSGAEIGGAFGGEKHTG-GGRESGSDA 513
Cdd:cd07097 396 AIANDTEFGLSAGIVTTSLKHATHF--KRRVEAGVVMVNLPTAGVDYHVPFGGRKGSSyGPREQGEAA 461
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
93-525 |
3.28e-111 |
|
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: 335.35 E-value: 3.28e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 93 TAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSE 172
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 173 RPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSLVSVATTKIVTDVIkrnkLPPIV--TLC 250
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAG----LPPGVvnVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 251 QGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCT 330
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 331 TTRRLIIHAKLYDSFIAKLVkryasllkrvghpldsatlygpvhnqqavdnylqtvqeavalggkvecggkvidragffv 410
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV------------------------------------------------------------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 411 epTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEWLGEsgSDCGIVNINTSPSG 490
Cdd:cd06534 257 --TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAER--LRAGTVYINDSSIG 332
|
410 420 430
....*....|....*....|....*....|....*
gi 158296454 491 AEIGGAFGGEKHTGGGRESGSDAWKQYARRSTITV 525
Cdd:cd06534 333 VGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
69-513 |
1.85e-106 |
|
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: 325.93 E-value: 1.85e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 69 IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVq 148
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 149 efvdicDYAVGLSRMFG-------GAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAP 221
Cdd:cd07103 81 ------DYAASFLEWFAeearriyGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 222 STSLVSVATTKIVTDVikrnKLPP----IVTlcqG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVgieMQR---RFGRCL 293
Cdd:cd07103 155 ETPLSALALAELAEEA----GLPAgvlnVVT---GsPAEIGEALCASPRVRKISFTGSTAVGKLL---MAQaadTVKRVS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 294 LELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPV 373
Cdd:cd07103 225 LELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKL--KVGNGLDEGTDMGPL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 374 HNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVD 453
Cdd:cd07103 303 INERAVEKVEALVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTP 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158296454 454 QGLSSSLFTNNIQSAFEwLGEsGSDCGIVNINTS-PSGAEIggAFGGEKHTGGGRESGSDA 513
Cdd:cd07103 383 YGLAAYVFTRDLARAWR-VAE-ALEAGMVGINTGlISDAEA--PFGGVKESGLGREGGKEG 439
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
87-525 |
4.39e-99 |
|
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: 306.38 E-value: 4.39e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 87 DLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQEFVDICDYAVGLSRMFGG 166
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 167 AIFPSERPqhtilEKWN-----PLGLVGVISAFNFPcAVFGWNA-AIALTVGNTVLWKGAPSTSlvsVATTKIVTDVIKR 240
Cdd:cd07104 81 EILPSDVP-----GKESmvrrvPLGVVGVISPFNFP-LILAMRSvAPALALGNAVVLKPDSRTP---VTGGLLIAEIFEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 241 NKLPPIV--TLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALIINEDAPQEMALDAAF 318
Cdd:cd07104 152 AGLPKGVlnVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 319 FGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVEC 398
Cdd:cd07104 232 FGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKAL--PVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 399 GGKvidRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEwLGESgSD 478
Cdd:cd07104 310 GGT---YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMA-FAER-LE 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 158296454 479 CGIVNINTSPSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTITV 525
Cdd:cd07104 385 TGMVHINDQTVNDEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
55-470 |
2.48e-98 |
|
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: 305.73 E-value: 2.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKVQS-IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVA 133
Cdd:cd07088 3 NGEFVPSSSGETIDvLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 134 LEMGKILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGN 213
Cdd:cd07088 83 EEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 214 TVLWKGAPSTSLVSVATTKIVTDVikrnKLPPIV--TLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGR 291
Cdd:cd07088 163 TIVIKPSEETPLNALEFAELVDEA----GLPAGVlnIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 292 CLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYG 371
Cdd:cd07088 239 VSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAV--KVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 372 PVHNQQAVDNYLQTVQEAVALGGKVECGGKVID-RAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNN 450
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAN 396
|
410 420
....*....|....*....|
gi 158296454 451 EVDQGLSSSLFTNNIQSAFE 470
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMR 416
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
70-525 |
2.72e-96 |
|
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: 300.02 E-value: 2.72e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 70 DPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQE 149
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 150 FVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISAFNFPcAVFGWNA-AIALTVGNTVLWKGAPSTslvsV 228
Cdd:cd07150 85 TPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYP-LILATKKvAFALAAGNTVVLKPSEET----P 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 229 ATTKIVTDVIKRNKLPP----IVTlCQGGEdVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALII 304
Cdd:cd07150 160 VIGLKIAEIMEEAGLPKgvfnVVT-GGGAE-VGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 305 NEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYLQ 384
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKL--KVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 385 TVQEAVALGGKVECGGKvidRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNN 464
Cdd:cd07150 316 QVEDAVAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158296454 465 IQSAFEwLGESgSDCGIVNINTSPSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTITV 525
Cdd:cd07150 393 LQRAFK-LAER-LESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
53-526 |
1.57e-94 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 297.21 E-value: 1.57e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 53 VYNGEWVaGTAGKVQSIDPA-SGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKL 131
Cdd:cd07124 36 VIGGKEV-RTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 132 VALEMGKILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSERPQHTILeKWNPLGLVGVISAFNFPCAVFGWNAAIALTV 211
Cdd:cd07124 115 MVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRY-VYRPLGVGAVISPWNFPLAILAGMTTAALVT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 212 GNTVLWKGAPSTSLVSvattKIVTDVIKRNKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGR------TVGI 283
Cdd:cd07124 194 GNTVVLKPAEDTPVIA----AKLVEILEEAGLPPgVVNFLPGpGEEVGDYLVEHPDVRFIAFTGSREVGLriyeraAKVQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 284 EMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHP 363
Cdd:cd07124 270 PGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKAL--KVGDP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 364 LDSATLYGPVHNQQAVDNYLQTVQEAVAlGGKVECGGKVIDRA--GFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASN 441
Cdd:cd07124 348 EDPEVYMGPVIDKGARDRIRRYIEIGKS-EGRLLLGGEVLELAaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 442 LQEAISWNNEVDQGLSSSLFTNN---IQSAFEWLgesgsDCGIVNINTSPSGAEIG-GAFGGEKHTG-GGRESGSDAWKQ 516
Cdd:cd07124 427 FDEALEIANDTEYGLTGGVFSRSpehLERARREF-----EVGNLYANRKITGALVGrQPFGGFKMSGtGSKAGGPDYLLQ 501
|
490
....*....|
gi 158296454 517 YARRSTITVN 526
Cdd:cd07124 502 FMQPKTVTEN 511
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
69-525 |
2.55e-93 |
|
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: 292.12 E-value: 2.55e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 69 IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQ 148
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 149 EFVDICDYAVGLSrmfggaiFPSER----PQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTS 224
Cdd:cd07106 82 GAVAWLRYTASLD-------LPDEVieddDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 225 LVSVATTKIVTDVikrnkLPP----IVTlcqGGEDVGKRMVSDERIRLMSFTGSTAVGRTVgieMQRRFG---RCLLELG 297
Cdd:cd07106 155 LCTLKLGELAQEV-----LPPgvlnVVS---GGDELGPALTSHPDIRKISFTGSTATGKKV---MASAAKtlkRVTLELG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 298 GNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVkRYASLLKrVGHPLDSATLYGPVHNQQ 377
Cdd:cd07106 224 GNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALV-ALAKAAV-VGDGLDPGTTLGPVQNKM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 378 AVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLS 457
Cdd:cd07106 302 QYDKVKELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLG 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 458 SSLFTNNIQSAfEWLGESgSDCGIVNINTSpsgAEIGGA--FGGEKHTGGGRESGSDAWKQYARRSTITV 525
Cdd:cd07106 382 ASVWSSDLERA-EAVARR-LEAGTVWINTH---GALDPDapFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
68-525 |
3.14e-92 |
|
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: 289.45 E-value: 3.14e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 68 SIDPASGRVIAEVATGSEQDLERCLTAGVAAY--QEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVG 145
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 146 EVQEFVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSL 225
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 226 VSVATTKIVTDVikrnKLPPIV--TLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALI 303
Cdd:cd07114 161 STLELAKLAEEA----GFPPGVvnVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 304 INEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYL 383
Cdd:cd07114 237 VFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAI--RVGDPLDPETQMGPLATERQLEKVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 384 QTVQEAVALGGKVECGGKVID----RAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSS 459
Cdd:cd07114 315 RYVARAREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAG 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 460 LFTNNIQSAfeWLGESGSDCGIVNINT----SPSgaeigGAFGGEKHTGGGRESGSDAWKQYARRSTITV 525
Cdd:cd07114 395 IWTRDLARA--HRVARAIEAGTVWVNTyralSPS-----SPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
88-508 |
3.02e-91 |
|
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: 285.89 E-value: 3.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 88 LERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQEFVDICD-YAVGLSRMFGG 166
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRyYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 167 AIFPSERPQHTIleKWNPLGLVGVISAFNFP---CAVFgwnAAIALTVGNTVLWKGAPSTSLVSVATTKIVTDVikrnKL 243
Cdd:cd07100 81 EPIETDAGKAYV--RYEPLGVVLGIMPWNFPfwqVFRF---AAPNLMAGNTVLLKHASNVPGCALAIEELFREA----GF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 244 PP--IVTLCQGGEDVGKrMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGC 321
Cdd:cd07100 152 PEgvFQNLLIDSDQVEA-IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 322 IGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGK 401
Cdd:cd07100 231 LQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAAL--KVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 402 VIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAfEWLGeSGSDCGI 481
Cdd:cd07100 309 RPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERA-ERVA-RRLEAGM 386
|
410 420
....*....|....*....|....*...
gi 158296454 482 VNINT-SPSGAEIggAFGGEKHTGGGRE 508
Cdd:cd07100 387 VFINGmVKSDPRL--PFGGVKRSGYGRE 412
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
69-508 |
5.02e-90 |
|
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: 283.72 E-value: 5.02e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 69 IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQ 148
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 149 EFVDICDYAVGLSRMFGGAIFPSE-------RPQHTILEkwnPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAP 221
Cdd:cd07149 84 RAIETLRLSAEEAKRLAGETIPFDaspggegRIGFTIRE---PIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 222 STSLVSVATTKIVTDVikrnKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRtvgiEMQRRFG--RCLLELG 297
Cdd:cd07149 161 QTPLSALKLAELLLEA----GLPKgALNVVTGsGETVGDALVTDPRVRMISFTGSPAVGE----AIARKAGlkKVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 298 GNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQ 377
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKL--VVGDPLDEDTDVGPMISEA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 378 AVDNYLQTVQEAVALGGKVECGGKvidRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLS 457
Cdd:cd07149 311 EAERIEEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQ 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 158296454 458 SSLFTNNIQSAFEWLGEsgSDCGIVNINTSPSGAEIGGAFGGEKHTGGGRE 508
Cdd:cd07149 388 AGVFTNDLQKALKAARE--LEVGGVMINDSSTFRVDHMPYGGVKESGTGRE 436
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
69-509 |
1.39e-85 |
|
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: 272.30 E-value: 1.39e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 69 IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQ 148
Cdd:cd07145 4 RNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 149 EFVDICDYAVGLSRMFGGAIFPSERPQHT----ILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTS 224
Cdd:cd07145 84 RTIRLFKLAAEEAKVLRGETIPVDAYEYNerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 225 LVSVATTKIVTDVikrnKLPP--IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNAL 302
Cdd:cd07145 164 LTAIELAKILEEA----GLPPgvINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 303 IINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNY 382
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKL--KVGDPLDESTDLGPLISPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 383 LQTVQEAVALGGKVECGGKVIDraGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFT 462
Cdd:cd07145 318 ENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFT 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 158296454 463 NNIQSAFEWLGEsgSDCGIVNINTSPSGAEIGGAFGGEKHTGGGRES 509
Cdd:cd07145 396 NDINRALKVARE--LEAGGVVINDSTRFRWDNLPFGGFKKSGIGREG 440
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
69-508 |
2.88e-85 |
|
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: 271.43 E-value: 2.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 69 IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQ 148
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 149 EFVDICDYAVGLSRMFGGAIFP---SERPQ-HTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTS 224
Cdd:cd07147 84 RAIDTFRIAAEEATRIYGEVLPldiSARGEgRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 225 LVSVattkIVTDVIKRNKLPP----IVTLCQGGEDvgkRMVSDERIRLMSFTGSTAVGrtvgIEMQRRFGR--CLLELGG 298
Cdd:cd07147 164 LSAL----ILGEVLAETGLPKgafsVLPCSRDDAD---LLVTDERIKLLSFTGSPAVG----WDLKARAGKkkVVLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 299 NNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQA 378
Cdd:cd07147 233 NAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKAL--KTGDPKDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 379 VDNYLQTVQEAVALGGKVECGGKvidRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSS 458
Cdd:cd07147 311 AERVEGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 158296454 459 SLFTNNIQSAFEWLGEsgSDCGIVNINTSPSGAEIGGAFGGEKHTGGGRE 508
Cdd:cd07147 388 GVFTRDLEKALRAWDE--LEVGGVVINDVPTFRVDHMPYGGVKDSGIGRE 435
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
56-527 |
5.97e-85 |
|
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: 271.10 E-value: 5.97e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 56 GEWVAGTAGKVQS-IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVAL 134
Cdd:cd07151 1 GEWRDGTSERTIDvLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 135 EMGKILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSERP--QHTILEKwnPLGLVGVISAFNFPCAVFGWNAAIALTVG 212
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPgkENRVYRE--PLGVVGVISPWNFPLHLSMRSVAPALALG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 213 NTVLWKGAPSTSLVSvatTKIVTDVIKRNKLPPIV--TLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFG 290
Cdd:cd07151 159 NAVVLKPASDTPITG---GLLLAKIFEEAGLPKGVlnVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 291 RCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLY 370
Cdd:cd07151 236 KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKAL--PYGDPSDPDTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 371 GPVHNQQAVDNYLQTVQEAVALGGKVECGGKVidrAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNN 450
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAN 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158296454 451 EVDQGLSSSLFTNNIQSAFEWlgESGSDCGIVNINTSPSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTITVNH 527
Cdd:cd07151 391 DTEYGLSGAVFTSDLERGVQF--ARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQH 465
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
68-526 |
6.26e-83 |
|
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: 265.46 E-value: 6.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 68 SIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVG-E 146
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 147 VQEFVDICDYAVGLSRMFGGAIFPSERP--QHTILEkwnPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTS 224
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPflNYTVRE---PVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 225 LVSVATTKIVTDVikrnKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNAL 302
Cdd:cd07115 158 LSALRIAELMAEA----GFPAgVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 303 IINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNY 382
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSL--RPGDPLDPKTQMGPLVSQAQFDRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 383 LQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFT 462
Cdd:cd07115 312 LDYVDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158296454 463 NNIQSAFEWlgESGSDCGIVNINTSpSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTITVN 526
Cdd:cd07115 392 RDLGRAHRV--AAALKAGTVWINTY-NRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVN 452
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
41-517 |
1.38e-81 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 263.09 E-value: 1.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 41 LRDLGLQRvNNGVYNGEWVAGTAGK-VQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGD 119
Cdd:PLN02278 17 LRNAGLLR-TQGLIGGKWTDAYDGKtFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 120 ELRKYREPLGKLVALEMGKILPEGVGEVQ---EFVDIcdYAVGLSRMFGGAIfPSERPQHTILEKWNPLGLVGVISAFNF 196
Cdd:PLN02278 96 LIIANKEDLAQLMTLEQGKPLKEAIGEVAygaSFLEY--FAEEAKRVYGDII-PSPFPDRRLLVLKQPVGVVGAITPWNF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 197 PCAVFGWNAAIALTVGNTVLWKGAPSTSLVSVAttkiVTDVIKRNKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGS 274
Cdd:PLN02278 173 PLAMITRKVGPALAAGCTVVVKPSELTPLTALA----AAELALQAGIPPgVLNVVMGdAPEIGDALLASPKVRKITFTGS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 275 TAVGRTVGIEMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYA 354
Cdd:PLN02278 249 TAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 355 SLlkRVGHPLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIV 434
Cdd:PLN02278 329 KL--VVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 435 YVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAF---EWLgesgsDCGIVNINTSPSGAEIgGAFGGEKHTGGGRESGS 511
Cdd:PLN02278 407 PLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWrvsEAL-----EYGIVGVNEGLISTEV-APFGGVKQSGLGREGSK 480
|
....*.
gi 158296454 512 DAWKQY 517
Cdd:PLN02278 481 YGIDEY 486
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
70-525 |
4.76e-81 |
|
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: 260.37 E-value: 4.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 70 DPASGRVIAEVATGSEQDLERCLtAGVAAYQewKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQE 149
Cdd:cd07146 5 NPYTGEVVGTVPAGTEEALREAL-ALAASYR--STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 150 FVDICDYAVGLSRMFGGAIFPSERPQHT----ILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSL 225
Cdd:cd07146 82 AADVLRFAAAEALRDDGESFSCDLTANGkarkIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 226 VSVAttkiVTDVIKRNKLPP-IVTLCQGG-EDVGKRMVSDERIRLMSFTGSTAVGRTvgIEMQRRFGRCLLELGGNNALI 303
Cdd:cd07146 162 SAIY----LADLLYEAGLPPdMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKA--IAATAGYKRQLLELGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 304 INEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYL 383
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAAL--VVGDPMDPATDMGTVIDEEAAIQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 384 QTVQEAVALGGKVECGGKvidRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTN 463
Cdd:cd07146 314 NRVEEAIAQGARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTN 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158296454 464 NIQSAFEWLgeSGSDCGIVNINTSPSGAEIGGAFGGEKHTG-GGRESGSDAWKQYARRSTITV 525
Cdd:cd07146 391 DLDTIKRLV--ERLDVGTVNVNEVPGFRSELSPFGGVKDSGlGGKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
55-525 |
6.41e-81 |
|
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: 260.60 E-value: 6.41e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGK-VQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQE--WKKIPAPLRGDVIRQIGDELRKYREPLGKL 131
Cdd:cd07091 9 NNEFVDSVSGKtFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 132 VALEMGKILPEG-VGEVQEFVDICDYAVGLSRMFGGAIFPSERPQH--TILEkwnPLGLVGVISAFNFPCAVFGWNAAIA 208
Cdd:cd07091 89 ESLDNGKPLEESaKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLayTRRE---PIGVCGQIIPWNFPLLMLAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 209 LTVGNTVLWKGAPSTSLvsvaTTKIVTDVIKRNKLPPIV--TLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIE-M 285
Cdd:cd07091 166 LAAGNTVVLKPAEQTPL----SALYLAELIKEAGFPPGVvnIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAaA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 286 QRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLD 365
Cdd:cd07091 242 KSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKR--VVGDPFD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 366 SATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEA 445
Cdd:cd07091 320 PDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 446 ISWNNEVDQGLSSSLFTNNIQSAFEWLGESGSdcGIVNINT-------SPsgaeiggaFGGEKHTGGGRESGSDAWKQYA 518
Cdd:cd07091 400 IERANDTEYGLAAGVFTKDINKALRVSRALKA--GTVWVNTynvfdaaVP--------FGGFKQSGFGRELGEEGLEEYT 469
|
....*..
gi 158296454 519 RRSTITV 525
Cdd:cd07091 470 QVKAVTI 476
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
55-517 |
9.55e-81 |
|
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: 260.71 E-value: 9.55e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKVQSI-DPASGRVIAEVATGSEQDLERCLTAGVAAYQ--EWKKIPAPLRGDVIRQIGDELRKYREPLGKL 131
Cdd:cd07119 3 DGEWVEAASGKTRDIiNPANGEVIATVPEGTAEDAKRAIAAARRAFDsgEWPHLPAQERAALLFRIADKIREDAEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 132 VALEMGKILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSERPQHTILEKwNPLGLVGVISAFNFPCAVFGWNAAIALTV 211
Cdd:cd07119 83 ETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVR-EPVGVCGLITPWNYPLLQAAWKLAPALAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 212 GNTVLWKGAPSTSLVSVATTKIVTDVikrnKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRF 289
Cdd:cd07119 162 GNTVVIKPSEVTPLTTIALFELIEEA----GLPAgVVNLVTGsGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 290 GRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATL 369
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKI--KLGNGLDADTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 370 YGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRA----GFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEA 445
Cdd:cd07119 316 MGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158296454 446 ISWNNEVDQGLSSSLFTNNIQSAFEWLgeSGSDCGIVNINT-SPSGAEigGAFGGEKHTGGGRESGSDAWKQY 517
Cdd:cd07119 396 IRLANDTPYGLAGAVWTKDIARANRVA--RRLRAGTVWINDyHPYFAE--APWGGYKQSGIGRELGPTGLEEY 464
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
68-526 |
1.20e-80 |
|
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: 259.61 E-value: 1.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 68 SIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEV 147
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 148 QEFVDICDYAVGLSRMFGGAIFPSErPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSLVS 227
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVG-GRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 228 VATTKIVTDVikrnkLPPIV--TLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALIIN 305
Cdd:cd07107 160 LRLAELAREV-----LPPGVfnILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 306 EDAPQEMALDAAFFGC-IGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYLQ 384
Cdd:cd07107 235 PDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAI--KVGDPTDPATTMGPLVSRQQYDRVMH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 385 TVQEAVALGGKVECGGK----VIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSL 460
Cdd:cd07107 313 YIDSAKREGARLVTGGGrpegPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAI 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158296454 461 FTNNIQSAFewLGESGSDCGIVNINTSPSGAeIGGAFGGEKHTGGGRESGSDAWKQYARRSTITVN 526
Cdd:cd07107 393 WTNDISQAH--RTARRVEAGYVWINGSSRHF-LGAPFGGVKNSGIGREECLEELLSYTQEKNVNVR 455
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
74-525 |
1.49e-80 |
|
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: 258.76 E-value: 1.49e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 74 GRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQEFVDI 153
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 154 CDYAVGLSRMFGGAIFPSERPQHTILEKwNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSlvsVATTKI 233
Cdd:cd07152 81 LHEAAGLPTQPQGEILPSAPGRLSLARR-VPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTP---VSGGVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 234 VTDVIKRNKLPP-IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALIINEDAPQEM 312
Cdd:cd07152 157 IARLFEEAGLPAgVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 313 ALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYLQTVQEAVAL 392
Cdd:cd07152 237 AASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHL--PVGDPATGQVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 393 GGKVECGGKvidRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEwL 472
Cdd:cd07152 315 GARLEAGGT---YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMA-L 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 158296454 473 GESgSDCGIVNINTSPSGAEIGGAFGGEKHTG-GGRESGSDAWKQYARRSTITV 525
Cdd:cd07152 391 ADR-LRTGMLHINDQTVNDEPHNPFGGMGASGnGSRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
68-525 |
3.38e-79 |
|
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: 255.57 E-value: 3.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 68 SIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEV 147
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 148 -----QEFVDICDYAVGLsrmfGGAIFPSErPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPS 222
Cdd:cd07093 81 ipraaANFRFFADYILQL----DGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 223 TSLvsvaTTKIVTDVIKRNKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNN 300
Cdd:cd07093 156 TPL----TAWLLAELANEAGLPPgVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 301 ALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGP----VHnQ 376
Cdd:cd07093 232 PNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKAL--KVGDPLDPDTEVGPliskEH-L 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 377 QAVDNYlqtVQEAVALGGKVECGGKVID----RAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEV 452
Cdd:cd07093 309 EKVLGY---VELARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDT 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158296454 453 DQGLSSSLFTNNIQSAFEWlgESGSDCGIVNINTsPSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTITV 525
Cdd:cd07093 386 PYGLAAYVWTRDLGRAHRV--ARRLEAGTVWVNC-WLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
69-525 |
1.67e-78 |
|
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: 253.89 E-value: 1.67e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 69 IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQ 148
Cdd:cd07094 4 HNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 149 EFVDICDYAVGLSRMFGGAIFPSE----RPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTS 224
Cdd:cd07094 84 RAIDTLRLAAEEAERIRGEEIPLDatqgSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 225 LVSVATTKIVTDVikrNKLPPIVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTvgIEMQRRFGRCLLELGGNNALI 303
Cdd:cd07094 164 LSALELAKILVEA---GVPEGVLQVVTGeREVLGDAFAADERVAMLSFTGSAAVGEA--LRANAGGKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 304 INEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYL 383
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKL--KVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 384 QTVQEAVALGGKVECGGKvidRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTN 463
Cdd:cd07094 317 RWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158296454 464 NIQSAFEwlGESGSDCGIVNINTSPSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTITV 525
Cdd:cd07094 394 DLNVAFK--AAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
69-519 |
1.44e-76 |
|
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: 248.78 E-value: 1.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 69 IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGV-GEV 147
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 148 QEFVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSLVS 227
Cdd:cd07092 82 PGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 228 VATTKIVTDVikrnkLPPIV--TLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALIIN 305
Cdd:cd07092 162 LLLAELAAEV-----LPPGVvnVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 306 EDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYLQT 385
Cdd:cd07092 237 DDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAI--RVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 386 VQEAVAlGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNI 465
Cdd:cd07092 315 VERAPA-HARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDV 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 158296454 466 QSAFEWLGEsgSDCGIVNINTS-PSGAEIggAFGGEKHTGGGRESGSDAWKQYAR 519
Cdd:cd07092 394 GRAMRLSAR--LDFGTVWVNTHiPLAAEM--PHGGFKQSGYGKDLSIYALEDYTR 444
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
69-525 |
3.97e-76 |
|
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: 247.66 E-value: 3.97e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 69 IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKIL-PEGVGEV 147
Cdd:cd07108 2 INPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 148 QEFVDICDYAVGLSRMFGGAIFPSeRPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSLVS 227
Cdd:cd07108 82 AVLADLFRYFGGLAGELKGETLPF-GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 228 VATTKIVTDVikrnkLPPIV--TLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALIIN 305
Cdd:cd07108 161 LLLAEILAQV-----LPAGVlnVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 306 EDAPQEMALDAAFFGCIGT-AGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYLQ 384
Cdd:cd07108 236 PDADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKL--KIGDPLDEATDIGAIISEKQFAKVCG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 385 TVQEAVAL-GGKVECGGK----VIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSS 459
Cdd:cd07108 314 YIDLGLSTsGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAY 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158296454 460 LFTNNIQSAFEwlGESGSDCGIVNINTSpSGAEIGGAFGGEKHTGGGRESGSDAW-KQYARRSTITV 525
Cdd:cd07108 394 VWTRDLGRALR--AAHALEAGWVQVNQG-GGQQPGQSYGGFKQSGLGREASLEGMlEHFTQKKTVNI 457
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
69-525 |
9.56e-76 |
|
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: 246.75 E-value: 9.56e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 69 IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQ 148
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 149 EFVDICDYAVGL-------SRMFGGAIFPSERPQHTILekwnPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAP 221
Cdd:cd07099 81 LALEAIDWAARNaprvlapRKVPTGLLMPNKKATVEYR----PYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 222 STSLVSVATTKIVTDVikrNKLPPIVTLCQGGEDVGKRMVsDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNA 301
Cdd:cd07099 157 VTPLVGELLAEAWAAA---GPPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 302 LIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDN 381
Cdd:cd07099 233 MIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARAL--RPGADDIGDADIGPMTTARQLDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 382 YLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLF 461
Cdd:cd07099 311 VRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158296454 462 TNNIQSAfEWLGESgSDCGIVNINTSPSGAEIGGA-FGGEKHTGGGRESGSDAWKQYARRSTITV 525
Cdd:cd07099 391 SRDLARA-EAIARR-LEAGAVSINDVLLTAGIPALpFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
55-517 |
1.13e-74 |
|
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: 244.33 E-value: 1.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKV-QSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQE--WKKIPAPLRGDVIRQIGDELRKYREPLGKL 131
Cdd:cd07142 9 NGQFVDAASGKTfPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 132 VALEMGKILPEG-VGEVQEFVDICDYAVGLSRMFGGAIFPSERPQH--TILEkwnPLGLVGVISAFNFPCAVFGWNAAIA 208
Cdd:cd07142 89 ETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHvyTLHE---PIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 209 LTVGNTVLWKGAPSTSLVSVATTKIVTDVikrnKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTV-GIEM 285
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSALLAAKLAAEA----GLPDgVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIImQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 286 QRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRyasLLKR-VGHPL 364
Cdd:cd07142 242 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKAR---ALKRvVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 365 DSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQE 444
Cdd:cd07142 319 RKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158296454 445 AISWNNEVDQGLSSSLFTNNIQSAFEWLgeSGSDCGIVNINTSpSGAEIGGAFGGEKHTGGGRESGSDAWKQY 517
Cdd:cd07142 399 VIKRANNSKYGLAAGVFSKNIDTANTLS--RALKAGTVWVNCY-DVFDASIPFGGYKMSGIGREKGIYALNNY 468
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
71-525 |
2.04e-74 |
|
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: 243.01 E-value: 2.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 71 PASGRVIAEVATGSEQDLERCLTAGVAAYQE--WKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQ 148
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 149 EFVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSlvsv 228
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 229 ATTKIVTDVIKRNKLPP----IVTlcQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALII 304
Cdd:cd07118 160 GTTLMLAELLIEAGLPAgvvnIVT--GYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 305 NEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYLQ 384
Cdd:cd07118 238 FADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKV--RVGDPLDPETKVGAIINEAQLAKITD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 385 TVQEAVALGGKVECGGKVID-RAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTN 463
Cdd:cd07118 316 YVDAGRAEGATLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSK 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158296454 464 NIQSAFEWLGESGSdcGIVNINTSPSG-AEIggAFGGEKHTGGGRESGSDAWKQYARRSTITV 525
Cdd:cd07118 396 DIDTALTVARRIRA--GTVWVNTFLDGsPEL--PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
69-526 |
2.19e-74 |
|
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: 242.98 E-value: 2.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 69 IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQ 148
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 149 EFVDICDYAVGL-SRMFGGAI-FPSERPQHTILEkwnPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSLV 226
Cdd:cd07090 82 SSADCLEYYAGLaPTLSGEHVpLPGGSFAYTRRE---PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 227 SVATTKIVTDVikrnKLPP-IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALIIN 305
Cdd:cd07090 159 ALLLAEILTEA----GLPDgVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 306 EDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYLQT 385
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKI--RIGDPLDEDTQMGALISEEHLEKVLGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 386 VQEAVALGGKVECGGKVID-----RAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSL 460
Cdd:cd07090 313 IESAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158296454 461 FTNNIQSAFEWLGE--SGSdCGIVNINTSPsgAEIggAFGGEKHTGGGRESGSDAWKQYARRSTITVN 526
Cdd:cd07090 393 FTRDLQRAHRVIAQlqAGT-CWINTYNISP--VEV--PFGGYKQSGFGRENGTAALEHYTQLKTVYVE 455
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
55-526 |
3.32e-74 |
|
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: 243.47 E-value: 3.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAG-KVQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWK-KIPAPLRGDVIRQIGDELRKYREPLGKLV 132
Cdd:cd07144 13 NNEFVKSSDGeTIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWsKVTGEERGELLDKLADLVEKNRDLLAAIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 133 ALEMGKIL-PEGVGEVQEFVDICDYAVGLSRMFGGAIFPSERPQH--TILEkwnPLGLVGVISAFNFPCAVFGWNAAIAL 209
Cdd:cd07144 93 ALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLayTLHE---PYGVCGQIIPWNYPLAMAAWKLAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 210 TVGNTVLWKGAPST--SLVSVATtkivtdVIKRNKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEM 285
Cdd:cd07144 170 AAGNTVVIKPAENTplSLLYFAN------LVKEAGFPPgVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 286 QRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLLKrVGHPLD 365
Cdd:cd07144 244 AQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYK-VGSPFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 366 SATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGG---KVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNL 442
Cdd:cd07144 323 DDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 443 QEAISWNNEVDQGLSSSLFTNNIQSAFEWLGESGSdcGIVNINTSPSGaEIGGAFGGEKHTGGGRESGSDAWKQYARRST 522
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEA--GMVWINSSNDS-DVGVPFGGFKMSGIGRELGEYGLETYTQTKA 479
|
....
gi 158296454 523 ITVN 526
Cdd:cd07144 480 VHIN 483
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
68-513 |
1.02e-73 |
|
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: 241.48 E-value: 1.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 68 SIDPASGRVIAEVATGSEQDLERCLTAGVAAYQE--WKKIPApLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVG 145
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 146 EVQEFVDICDYAVGLSR-MFGGAIFPSERPQHTILEKwnPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTS 224
Cdd:cd07120 80 EISGAISELRYYAGLARtEAGRMIEPEPGSFSLVLRE--PMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 225 LVSVATTKIVTDVikrNKLPP-IVTL-CQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNAL 302
Cdd:cd07120 158 QINAAIIRILAEI---PSLPAgVVNLfTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 303 IINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNY 382
Cdd:cd07120 235 IVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAV--KVGPGLDPASDMGPLIDRANVDRV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 383 LQTVQEAVALGGKVEC-GGKVIDR--AGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSS 459
Cdd:cd07120 313 DRMVERAIAAGAEVVLrGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAAS 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 158296454 460 LFTNNIQSAFEWlgESGSDCGIVNINTSP---SGAEiggaFGGEKHTGGGRESGSDA 513
Cdd:cd07120 393 VWTRDLARAMRV--ARAIRAGTVWINDWNklfAEAE----EGGYRQSGLGRLHGVAA 443
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
55-526 |
4.66e-73 |
|
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: 240.05 E-value: 4.66e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGK-VQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVA 133
Cdd:cd07117 6 NGEWVKGSSGEtIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 134 LEMGKILPEGVGevqefVDIcDYAVGLSRMFGGAIFPSERPQHTILEKW------NPLGLVGVISAFNFPCAVFGWNAAI 207
Cdd:cd07117 86 LDNGKPIRETRA-----VDI-PLAADHFRYFAGVIRAEEGSANMIDEDTlsivlrEPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 208 ALTVGNTVLWKGAPSTSLVSVATTKIVTDVIKRNklppIVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQ 286
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKG----VVNIVTGkGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 287 RRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDS 366
Cdd:cd07117 236 KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENV--KVGNPLDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 367 ATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDR----AGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNL 442
Cdd:cd07117 314 DTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTEngldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 443 QEAISWNNEVDQGLSSSLFTNNIQSAFEWlgESGSDCGIVNINTS---PSGAeiggAFGGEKHTGGGRESGSDAWKQYAR 519
Cdd:cd07117 394 DEVIDMANDSEYGLGGGVFTKDINRALRV--ARAVETGRVWVNTYnqiPAGA----PFGGYKKSGIGRETHKSMLDAYTQ 467
|
....*..
gi 158296454 520 RSTITVN 526
Cdd:cd07117 468 MKNIYID 474
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
69-510 |
5.76e-73 |
|
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: 239.56 E-value: 5.76e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 69 IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQ 148
Cdd:cd07110 2 INPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 149 EFVDICDYAVGLS---RMFGGAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSL 225
Cdd:cd07110 82 DVAGCFEYYADLAeqlDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 226 VSVATTKIVTDVikrnKLPPIV--TLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALI 303
Cdd:cd07110 162 TELELAEIAAEA----GLPPGVlnVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 304 INEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYL 383
Cdd:cd07110 238 VFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAI--RVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 384 QTVQEAVALGGKVECGGKVID--RAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLF 461
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 158296454 462 TNN------IQSAFEwlgesgsdCGIVNINTS-PSGAEIggAFGGEKHTGGGRESG 510
Cdd:cd07110 396 SRDaercdrVAEALE--------AGIVWINCSqPCFPQA--PWGGYKRSGIGRELG 441
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
68-525 |
6.95e-73 |
|
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: 239.06 E-value: 6.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 68 SIDPASGRVIAEVATGSEQDLERCLTAGVAAYQE-WKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGE 146
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 147 VQEFVDICDYAVGLSRMFGGAIFPSErPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSLV 226
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLG-PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 227 SVAttkiVTDVIKRNKLPP----IVTlcqG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNA 301
Cdd:cd07109 160 ALR----LAELAEEAGLPAgalnVVT---GlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 302 LIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLyGPVHNQQAVDN 381
Cdd:cd07109 233 QIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRAL--RVGPGLEDPDL-GPLISAKQLDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 382 YLQTVQEAVALGGKVECGGKVIDRA---GFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSS 458
Cdd:cd07109 310 VEGFVARARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVA 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158296454 459 SLFTNNIQSAFeWLGEsGSDCGIVNINTSPSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTITV 525
Cdd:cd07109 390 GVWTRDGDRAL-RVAR-RLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
55-508 |
3.70e-72 |
|
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: 238.01 E-value: 3.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGK-VQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVA 133
Cdd:cd07559 6 NGEWVAPSKGEyFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 134 LEMGKILPEGVGevqefVDIcDYAVGLSRMFGGAIFPSERPQHTILEK------WNPLGLVGVISAFNFPCAVFGWNAAI 207
Cdd:cd07559 86 LDNGKPIRETLA-----ADI-PLAIDHFRYFAGVIRAQEGSLSEIDEDtlsyhfHEPLGVVGQIIPWNFPLLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 208 ALTVGNTVLWKGAPSTSLVSVATTKIVTDVikrnkLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEM 285
Cdd:cd07559 160 ALAAGNTVVLKPASQTPLSILVLMELIGDL-----LPKgVVNVVTGfGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 286 QRRFGRCLLELGGNNALIINEDAPQEM-----ALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRV 360
Cdd:cd07559 235 AENLIPVTLELGGKSPNIFFDDAMDADddfddKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAI--KV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 361 GHPLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVI----DRAGFFVEPTIISNLPHDAPVVKRETFAPIVYV 436
Cdd:cd07559 313 GNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAV 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158296454 437 FKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEwLGEsGSDCGIVNINTS---PSGAeiggAFGGEKHTGGGRE 508
Cdd:cd07559 393 ITFKDEEEAIAIANDTEYGLGGGVWTRDINRALR-VAR-GIQTGRVWVNCYhqyPAHA----PFGGYKKSGIGRE 461
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
55-485 |
7.91e-72 |
|
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: 237.03 E-value: 7.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKVQSI-DPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVI---RQIgdeLRKYREPLGK 130
Cdd:cd07085 6 NGEWVESKTTEWLDVyNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMfkfRQL---LEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 131 LVALEMGKILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALT 210
Cdd:cd07085 83 LITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 211 VGNTVLWKgaPStSLVSVATTKIVtDVIKRNKLPP-IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRF 289
Cdd:cd07085 163 CGNTFVLK--PS-ERVPGAAMRLA-ELLQEAGLPDgVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 290 GRCLLELGGNNALIINEDAPQEMALDA---AFFGCigtAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDS 366
Cdd:cd07085 239 KRVQALGGAKNHAVVMPDADLEQTANAlvgAAFGA---AGQRCMALSVAVAVGDEADEWIPKLVERAKKL--KVGAGDDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 367 ATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRA----GFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNL 442
Cdd:cd07085 314 GADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTL 393
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 158296454 443 QEAISWNNEVDQGLSSSLFTNNIQSAFEWLGEsgSDCGIVNIN 485
Cdd:cd07085 394 DEAIAIINANPYGNGAAIFTRSGAAARKFQRE--VDAGMVGIN 434
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
55-525 |
2.13e-71 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 236.09 E-value: 2.13e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKV-QSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQ---EWKKIPAPLRGDVIRQIGDELRKYREPLGK 130
Cdd:cd07141 12 NNEWHDSVSGKTfPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLAS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 131 LVALEMGK-ILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSERPQHTiLEKWNPLGLVGVISAFNFPCAVFGWNAAIAL 209
Cdd:cd07141 92 LETLDNGKpFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFT-YTRHEPVGVCGQIIPWNFPLLMAAWKLAPAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 210 TVGNTVLWKGAPSTSLvsvaTTKIVTDVIKRNKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVgieMQ- 286
Cdd:cd07141 171 ACGNTVVLKPAEQTPL----TALYLASLIKEAGFPPgVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLI---QQa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 287 ---RRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASllKRVGHP 363
Cdd:cd07141 244 agkSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKK--RVVGNP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 364 LDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQ 443
Cdd:cd07141 322 FDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTID 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 444 EAISWNNEVDQGLSSSLFTNNIQSAFEWlgESGSDCGIVNINT-SPSGAEigGAFGGEKHTGGGRESGSDAWKQYARRST 522
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITF--SNALRAGTVWVNCyNVVSPQ--APFGGYKMSGNGRELGEYGLQEYTEVKT 477
|
...
gi 158296454 523 ITV 525
Cdd:cd07141 478 VTI 480
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
55-528 |
2.40e-71 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 235.57 E-value: 2.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKVQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVAL 134
Cdd:PRK13473 8 NGELVAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 135 EMGKILPEGVG-EVQEFVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGN 213
Cdd:PRK13473 88 NCGKPLHLALNdEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 214 TVLWKGAPSTSLVSVATTKIVTDVikrnkLPPIV--TLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGR 291
Cdd:PRK13473 168 TVVLKPSEITPLTALKLAELAADI-----LPPGVlnVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 292 CLLELGGNNALIINEDAPQEMALD-AAFFGCIgTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLY 370
Cdd:PRK13473 243 THLELGGKAPVIVFDDADLDAVVEgIRTFGYY-NAGQDCTAACRIYAQRGIYDDLVAKLAAAVATL--KVGDPDDEDTEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 371 GPVHNQQAVDNYLQTVQEAVALG-GKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWN 449
Cdd:PRK13473 320 GPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 450 NEVDQGLSSSLFTNNIQSAFEWLGEsgSDCGIVNINTS-PSGAEIggAFGGEKHTGGGRESGSDAWKQYARRSTITVNHS 528
Cdd:PRK13473 400 NDSDYGLASSVWTRDVGRAHRVSAR--LQYGCTWVNTHfMLVSEM--PHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKHT 475
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
69-523 |
6.99e-71 |
|
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: 234.06 E-value: 6.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 69 IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWK-KIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILP-EGVGE 146
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMtARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 147 VQEFVDICDYAVGLSRMF-----GGAIFPSERPQHTILEKwNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAP 221
Cdd:cd07089 82 VDGPIGHLRYFADLADSFpwefdLPVPALRGGPGRRVVRR-EPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 222 STSLVSVATTKIV--TDvikrnkLPP----IVTlcQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLE 295
Cdd:cd07089 161 DTPLSALLLGEIIaeTD------LPAgvvnVVT--GSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 296 LGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHN 375
Cdd:cd07089 233 LGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEAL--PVGDPADPGTVMGPLIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 376 QQAVDNYLQTVQEAVALGGKVECGGKVIDR--AGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVD 453
Cdd:cd07089 311 AAQRDRVEGYIARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158296454 454 QGLSSSLFTNNIQSAFEWLGE--SGSdcgiVNINTSpSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTI 523
Cdd:cd07089 391 YGLSGGVWSADVDRAYRVARRirTGS----VGINGG-GGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
69-506 |
2.98e-70 |
|
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: 232.14 E-value: 2.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 69 IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQ 148
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 149 EFVDICDYAVGLSRmfgGAIFPSERPQHTILEKW---NPLGLVGVISAFNFP--CAVfgwNAAI-ALTVGNTVLWKGAPS 222
Cdd:cd07102 81 GMLERARYMISIAE---EALADIRVPEKDGFERYirrEPLGVVLIIAPWNYPylTAV---NAVIpALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 223 TSLVSVAttkiVTDVIKRNKLPP-IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNA 301
Cdd:cd07102 155 TPLCGER----FAAAFAEAGLPEgVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 302 LIINEDAPQEMA----LDAAFFGCigtaGQRCTTTRRLIIHAKLYDSFIAKLV---KRYasllkRVGHPLDSATLYGPVH 374
Cdd:cd07102 231 AYVRPDADLDAAaeslVDGAFFNS----GQSCCSIERIYVHESIYDAFVEAFVavvKGY-----KLGDPLDPSTTLGPVV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 375 NQQAVDNYLQTVQEAVALGGKVECGGKVIDRA---GFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNE 451
Cdd:cd07102 302 SARAADFVRAQIADAIAKGARALIDGALFPEDkagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMND 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 158296454 452 VDQGLSSSLFTNNIQsAFEWLGESgSDCGIVNIN----TSPsgaeiGGAFGGEKHTGGG 506
Cdd:cd07102 382 SEYGLTASVWTKDIA-RAEALGEQ-LETGTVFMNrcdyLDP-----ALAWTGVKDSGRG 433
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
49-526 |
1.21e-69 |
|
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: 231.26 E-value: 1.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 49 VNNGVY-NGEWVAGTAGK-VQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQ-EW-KKIPAPLRGDVIRQIGDELRKY 124
Cdd:cd07143 5 QPTGLFiNGEFVDSVHGGtVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWgLKVSGSKRGRCLSKLADLMERN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 125 REPLGKLVALEMGK-ILPEGVGEVQEFVDICDYAVGLS-RMFGGAI-FPSERPQHTILEkwnPLGLVGVISAFNFPCAVF 201
Cdd:cd07143 85 LDYLASIEALDNGKtFGTAKRVDVQASADTFRYYGGWAdKIHGQVIeTDIKKLTYTRHE---PIGVCGQIIPWNFPLLMC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 202 GWNAAIALTVGNTVLWKGAPSTSLVSVATTKIvtdvIKRNKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGR 279
Cdd:cd07143 162 AWKIAPALAAGNTIVLKPSELTPLSALYMTKL----IPEAGFPPgVINVVSGyGRTCGNAISSHMDIDKVAFTGSTLVGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 280 TVGIEMQR-RFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlk 358
Cdd:cd07143 238 KVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKL-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 359 RVGHPLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFK 438
Cdd:cd07143 316 KVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 439 ASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEwlGESGSDCGIVNINTSpSGAEIGGAFGGEKHTGGGRESGSDAWKQYA 518
Cdd:cd07143 396 FKTEEEAIKRANDSTYGLAAAVFTNNINNAIR--VANALKAGTVWVNCY-NLLHHQVPFGGYKQSGIGRELGEYALENYT 472
|
....*...
gi 158296454 519 RRSTITVN 526
Cdd:cd07143 473 QIKAVHIN 480
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
53-464 |
1.91e-69 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 231.75 E-value: 1.91e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 53 VYNGEWVAgTAGKVQSIDPAS-GRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKL 131
Cdd:PRK03137 40 IIGGERIT-TEDKIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAW 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 132 VALEMGKILPEGVGEVQEFVDICDY----AVGLSrmFGGAIFPseRPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAI 207
Cdd:PRK03137 119 LVKEAGKPWAEADADTAEAIDFLEYyarqMLKLA--DGKPVES--RPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 208 ALTVGNTVLWKGAPSTSLVSVattKIVtDVIKRNKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVG-----RT 280
Cdd:PRK03137 195 AIVAGNTVLLKPASDTPVIAA---KFV-EVLEEAGLPAgVVNFVPGsGSEVGDYLVDHPKTRFITFTGSREVGlriyeRA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 281 VGI-EMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkR 359
Cdd:PRK03137 271 AKVqPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKEL--T 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 360 VGHPLDSATLyGPVHNQQAVD---NYLQTVQEAvalgGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYV 436
Cdd:PRK03137 349 VGNPEDNAYM-GPVINQASFDkimSYIEIGKEE----GRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAF 423
|
410 420
....*....|....*....|....*...
gi 158296454 437 FKASNLQEAISWNNEVDQGLSSSLFTNN 464
Cdd:PRK03137 424 IKAKDFDHALEIANNTEYGLTGAVISNN 451
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
55-525 |
1.03e-68 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 228.61 E-value: 1.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGK-VQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQE--WKKIPAPLRGDVIRQIGDELRKYREPLGKL 131
Cdd:cd07139 4 GGRWVAPSGSEtIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 132 VALEMGK-ILPEGVGEVQEFVDICDYAVGLSRMFGgaiFPSERP----QHTILEKwNPLGLVGVISAFNFPCAVFGWNAA 206
Cdd:cd07139 84 WTAENGMpISWSRRAQGPGPAALLRYYAALARDFP---FEERRPgsggGHVLVRR-EPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 207 IALTVGNTVLWKGAPSTSLVSVattkIVTDVIKRNKLPP-IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEM 285
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAY----LLAEAAEEAGLPPgVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 286 QRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLD 365
Cdd:cd07139 236 GERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAAL--KVGDPLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 366 SATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKV---IDRaGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNL 442
Cdd:cd07139 314 PATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRpagLDR-GWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 443 QEAISWNNEVDQGLSSSLFTNNIQSAFEwLGE---SGSdcgiVNINTspSGAEIGGAFGGEKHTGGGRESGSDAWKQYAR 519
Cdd:cd07139 393 DDAVRIANDSDYGLSGSVWTADVERGLA-VARrirTGT----VGVNG--FRLDFGAPFGGFKQSGIGREGGPEGLDAYLE 465
|
....*.
gi 158296454 520 RSTITV 525
Cdd:cd07139 466 TKSIYL 471
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
55-525 |
1.81e-68 |
|
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: 228.09 E-value: 1.81e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKVQSI-DPASGRVIAEVATGSEQDLERCLTAGVAAYQ-EWKKIPAPLRGDVIRQIGDELRKYREPLGKLV 132
Cdd:cd07113 5 DGRPVAGQSEKRLDItNPATEQVIASVASATEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIEQHGEELAQLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 133 ALEMGK-ILPEGVGEVQEFVDICDYAVGLSRMFGGAI----FPS---ERpqHTILEKWNPLGLVGVISAFNFPCAVFGWN 204
Cdd:cd07113 85 TLCSGKsIHLSRAFEVGQSANFLRYFAGWATKINGETlapsIPSmqgER--YTAFTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 205 AAIALTVGNTVLWKGAPSTSLvsvaTTKIVTDVIKRNKLPP-IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGI 283
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPL----TLLRVAELAKEAGIPDgVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 284 EMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHP 363
Cdd:cd07113 239 QAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSF--QVGSP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 364 LDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQ 443
Cdd:cd07113 317 MDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 444 EAISWNNEVDQGLSSSLFTNNIQSAFEWLGESGSDCGIVNINT--SPSgaeigGAFGGEKHTGGGRESGSDAWKQYARRS 521
Cdd:cd07113 397 ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTflDPA-----VPFGGMKQSGIGREFGSAFIDDYTELK 471
|
....
gi 158296454 522 TITV 525
Cdd:cd07113 472 SVMI 475
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
55-527 |
2.86e-68 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 227.76 E-value: 2.86e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKV-QSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQ--EWKKIPAPLRGDVIRQIGDELRKYREPLGKL 131
Cdd:cd07140 11 NGEFVDAEGGKTyNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFEngEWGKMNARDRGRLMYRLADLMEEHQEELATI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 132 VALEMGKI----LPEGVG-EVQEFvdicDYAVGLSRMFGGAIFP--SERPQHTI-LEKWNPLGLVGVISAFNFPCAVFGW 203
Cdd:cd07140 91 ESLDSGAVytlaLKTHVGmSIQTF----RYFAGWCDKIQGKTIPinQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 204 NAAIALTVGNTVLWKGAPSTSLVSVATTKIVTdvikRNKLPP--IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTV 281
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTV----KAGFPKgvINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 282 gieMQ----RRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLl 357
Cdd:cd07140 243 ---MKscavSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKM- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 358 kRVGHPLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYV- 436
Cdd:cd07140 319 -KIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIIs 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 437 -FKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFeWLGESgSDCGIVNINTSpSGAEIGGAFGGEKHTGGGRESGSDAWK 515
Cdd:cd07140 398 kFDDGDVDGVLQRANDTEYGLASGVFTKDINKAL-YVSDK-LEAGTVFVNTY-NKTDVAAPFGGFKQSGFGKDLGEEALN 474
|
490
....*....|..
gi 158296454 516 QYARRSTITVNH 527
Cdd:cd07140 475 EYLKTKTVTIEY 486
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
69-525 |
3.03e-68 |
|
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: 226.81 E-value: 3.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 69 IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKilpegvGEVQ 148
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGK------ARRH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 149 EFVDICDYAVGlSRMFG---GAIFPSERPQHTI------LEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKG 219
Cdd:cd07101 75 AFEEVLDVAIV-ARYYArraERLLKPRRRRGAIpvltrtTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 220 APSTSLvsvaTTKIVTDVIKRNKLP----PIVtlCQGGEDVGKRMVsdERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLE 295
Cdd:cd07101 154 DSQTAL----TALWAVELLIEAGLPrdlwQVV--TGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRLIGCSLE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 296 LGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHN 375
Cdd:cd07101 226 LGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRAL--RLGAALDYGPDMGSLIS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 376 QQAVDNYLQTVQEAVALGGKVECGGK-VIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQ 454
Cdd:cd07101 304 QAQLDRVTAHVDDAVAKGATVLAGGRaRPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDY 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158296454 455 GLSSSLFTNNIQSAfeWLGESGSDCGIVNINTS--PSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTITV 525
Cdd:cd07101 384 GLNASVWTRDGARG--RRIAARLRAGTVNVNEGyaAAWASIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
67-523 |
9.40e-66 |
|
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: 220.55 E-value: 9.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 67 QSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQE--WKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGV 144
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 145 GevqefVDICD-------YAVGLSRMFGgAIFPSERPQHTILEKwNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLW 217
Cdd:cd07112 85 A-----VDVPSaantfrwYAEAIDKVYG-EVAPTGPDALALITR-EPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 218 KGAPSTSLvsvaTTKIVTDVIKRNKLPPIV--TLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTvgieMQRRFG----- 290
Cdd:cd07112 158 KPAEQSPL----TALRLAELALEAGLPAGVlnVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRR----FLEYSGqsnlk 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 291 RCLLELGGNNALIINEDAPQ-EMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATL 369
Cdd:cd07112 230 RVWLECGGKSPNIVFADAPDlDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREW--KPGDPLDPATR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 370 YGPVHNQQAVDNYLQTVQEAVALGGKVECGGKV--IDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAIS 447
Cdd:cd07112 308 MGALVSEAHFDKVLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVA 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158296454 448 WNNEVDQGLSSSLFTNNIQSAFEWLGEsgSDCGIVNINTSpSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTI 523
Cdd:cd07112 388 LANDSVYGLAASVWTSDLSRAHRVARR--LRAGTVWVNCF-DEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
41-508 |
1.76e-65 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 220.55 E-value: 1.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 41 LRDLGLQRvNNGVYNGEWVAGTAGKVQSI-DPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGD 119
Cdd:PRK11241 3 LNDSTLFR-QQALINGEWLDANNGEVIDVtNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 120 ELRKYREPLGKLVALEMGKILPEGVGEVQEFVDICD-YAVGLSRMFGGAIfPSERPQHTILEKWNPLGLVGVISAFNFPC 198
Cdd:PRK11241 82 LMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEwFAEEGKRIYGDTI-PGHQADKRLIVIKQPIGVTAAITPWNFPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 199 AVFGWNAAIALTVGNTVLWKGAPSTSLVSVAttkiVTDVIKRNKLPP----IVTLCQGgeDVGKRMVSDERIRLMSFTGS 274
Cdd:PRK11241 161 AMITRKAGPALAAGCTMVLKPASQTPFSALA----LAELAIRAGIPAgvfnVVTGSAG--AVGGELTSNPLVRKLSFTGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 275 TAVGRTVGIEMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYA 354
Cdd:PRK11241 235 TEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 355 SLlkRVGHPLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIV 434
Cdd:PRK11241 315 KL--HIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158296454 435 YVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEwLGESgSDCGIVNINTSPSGAEIgGAFGGEKHTGGGRE 508
Cdd:PRK11241 393 PLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFR-VGEA-LEYGIVGINTGIISNEV-APFGGIKASGLGRE 463
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
55-525 |
2.62e-65 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 220.14 E-value: 2.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKV-QSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVA 133
Cdd:PRK13252 12 DGAYVEATSGETfEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALET 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 134 LEMGKILPEG-VGEVQEFVDICDYAVGLSRMFGGAIFPSERPQ--HTILEkwnPLGLVGVISAFNFPCAVFGWNAAIALT 210
Cdd:PRK13252 92 LDTGKPIQETsVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSfvYTRRE---PLGVCAGIGAWNYPIQIACWKSAPALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 211 VGNTVLWKGAPSTSLVSVATTKIVTDVikrnKLPPIV-TLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRF 289
Cdd:PRK13252 169 AGNAMIFKPSEVTPLTALKLAEIYTEA----GLPDGVfNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 290 GRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATL 369
Cdd:PRK13252 245 KEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERI--RIGDPMDPATN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 370 YGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRA----GFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEA 445
Cdd:PRK13252 323 FGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGgfanGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 446 ISWNNEVDQGLSSSLFTNNIQSAFEWLGEsgSDCGIVNINT---SPsgAEIggAFGGEKHTGGGRESGSDAWKQYARRST 522
Cdd:PRK13252 403 IARANDTEYGLAAGVFTADLSRAHRVIHQ--LEAGICWINTwgeSP--AEM--PVGGYKQSGIGRENGIATLEHYTQIKS 476
|
...
gi 158296454 523 ITV 525
Cdd:PRK13252 477 VQV 479
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
55-517 |
3.19e-65 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 220.37 E-value: 3.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGK-VQSIDPASGRVIAEVATGSEQDLERCLTAGVAAY-----QEWKKIPAPLRGDVIRQIGDELRKYREPL 128
Cdd:PLN02467 13 GGEWREPVLGKrIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERKSEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 129 GKLVALEMGKILPEGVGEVQEFVDICDYAVGL-----SRMFGGAIFPSERPQHTILekWNPLGLVGVISAFNFPCAVFGW 203
Cdd:PLN02467 93 AKLETLDCGKPLDEAAWDMDDVAGCFEYYADLaealdAKQKAPVSLPMETFKGYVL--KEPLGVVGLITPWNYPLLMATW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 204 NAAIALTVGNTVLWKgaPStSLVSVaTTKIVTDVIKRNKLPP----IVTlcqG-GEDVGKRMVSDERIRLMSFTGSTAVG 278
Cdd:PLN02467 171 KVAPALAAGCTAVLK--PS-ELASV-TCLELADICREVGLPPgvlnVVT---GlGTEAGAPLASHPGVDKIAFTGSTATG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 279 RTVGIEMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlk 358
Cdd:PLN02467 244 RKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNI-- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 359 RVGHPLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVID--RAGFFVEPTIISNLPHDAPVVKRETFAPIVYV 436
Cdd:PLN02467 322 KISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 437 FKASNLQEAISWNNEVDQGLSSSLFTNN------IQSAFEwlgesgsdCGIVNINTS-PSGAEigGAFGGEKHTGGGRES 509
Cdd:PLN02467 402 KTFSTEDEAIELANDSHYGLAGAVISNDlercerVSEAFQ--------AGIVWINCSqPCFCQ--APWGGIKRSGFGREL 471
|
....*...
gi 158296454 510 GSDAWKQY 517
Cdd:PLN02467 472 GEWGLENY 479
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
38-510 |
4.34e-64 |
|
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: 217.45 E-value: 4.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 38 FAFLRDLGLQRVNNG--VYNGEWVAGTAGKVQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIR 115
Cdd:cd07083 5 REALRRVKEEFGRAYplVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 116 QIGDELRKYREPLGKLVALEMGKILPEGVGEVQEFVDICDY-AVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISAF 194
Cdd:cd07083 85 KAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYyARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 195 NFPCAVFGWNAAIALTVGNTVLWKGAPSTSLVSVAttkiVTDVIKRNKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFT 272
Cdd:cd07083 165 NFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYK----VFEIFHEAGFPPgVVQFLPGvGEEVGAYLTEHERIRGINFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 273 GSTAVGRTVGIEMQRR------FGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFI 346
Cdd:cd07083 241 GSLETGKKIYEAAARLapgqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 347 AKLVKRYASLlkRVGHPLDSATLYGPVHNQQA---VDNYLQTVQEAvalgGKVECGGKVIDRAGFFVEPTIISNLPHDAP 423
Cdd:cd07083 321 ERLLKRAERL--SVGPPEENGTDLGPVIDAEQeakVLSYIEHGKNE----GQLVLGGKRLEGEGYFVAPTVVEEVPPKAR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 424 VVKRETFAPI--VYVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEWLGEsgSDCGIVNINTSPSGAEIG-GAFGGE 500
Cdd:cd07083 395 IAQEEIFGPVlsVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARRE--FHVGNLYINRKITGALVGvQPFGGF 472
|
490
....*....|
gi 158296454 501 KHTGGGRESG 510
Cdd:cd07083 473 KLSGTNAKTG 482
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
55-521 |
8.35e-64 |
|
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: 216.11 E-value: 8.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGK-VQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVA 133
Cdd:cd07111 27 NGKWVKPENRKsFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLES 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 134 LEMGKilpegvgEVQEFVDiCDYAVGLSRMFGGAIFPSErpQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGN 213
Cdd:cd07111 107 LDNGK-------PIRESRD-CDIPLVARHFYHHAGWAQL--LDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 214 TVLWKGAPSTSLVSVATTKIVTDVikrnKLPP-IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRC 292
Cdd:cd07111 177 TVVLKPAEYTPLTALLFAEICAEA----GLPPgVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 293 LLELGGNNALIINEDAPQEMAL----DAAFFgcigTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSAT 368
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVegivDAIWF----NQGQVCCAGSRLLVQESVAEELIRKLKERMSHL--RVGDPLDKAI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 369 LYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISW 448
Cdd:cd07111 327 DMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVAL 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158296454 449 NNEVDQGLSSSLFTNNIQSAFEWlgESGSDCGIVNINT----SPSgaeigGAFGGEKHTGGGRESGSDAWKQYARRS 521
Cdd:cd07111 407 ANNTPYGLAASVWSENLSLALEV--ALSLKAGVVWINGhnlfDAA-----AGFGGYRESGFGREGGKEGLYEYLRPS 476
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
55-526 |
1.89e-63 |
|
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: 214.74 E-value: 1.89e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKVQSIDPASGRVIAEVATGSEQDLercLTAGVAAY--QEWKKIPAPL--RGDVIRQIGDELRKYREPLGK 130
Cdd:cd07082 7 NGEWKESSGKTIEVYSPIDGEVIGSVPALSALEI---LEAAETAYdaGRGWWPTMPLeeRIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 131 LVALEMGKILPEGVGEVQEFVDICDYAV-GLSRMFG----GAIFPSERPQHTILEKwNPLGLVGVISAFNFPCavfgwNA 205
Cdd:cd07082 84 LLMWEIGKTLKDALKEVDRTIDYIRDTIeELKRLDGdslpGDWFPGTKGKIAQVRR-EPLGVVLAIGPFNYPL-----NL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 206 AI-----ALTVGNTVLWKGAPSTSLVSVATTKIVTDVIkrnkLPP----IVTLcqGGEDVGKRMVSDERIRLMSFTGSTA 276
Cdd:cd07082 158 TVsklipALIMGNTVVFKPATQGVLLGIPLAEAFHDAG----FPKgvvnVVTG--RGREIGDPLVTHGRIDVISFTGSTE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 277 VGRTVgIEMQRRfGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASL 356
Cdd:cd07082 232 VGNRL-KKQHPM-KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 357 lkRVGHPLDSATLYGPVHNQQAVDnYLQT-VQEAVALGGKVECGGKviDRAGFFVEPTIISNLPHDAPVVKRETFAPIVY 435
Cdd:cd07082 310 --KVGMPWDNGVDITPLIDPKSAD-FVEGlIDDAVAKGATVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 436 VFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEwLG---ESGSdcgiVNINTSPS-GAEIgGAFGGEKHTGGGRESGS 511
Cdd:cd07082 385 IIRVNDIEEAIELANKSNYGLQASIFTKDINKARK-LAdalEVGT----VNINSKCQrGPDH-FPFLGRKDSGIGTQGIG 458
|
490
....*....|....*
gi 158296454 512 DAWKQYARRSTITVN 526
Cdd:cd07082 459 DALRSMTRRKGIVIN 473
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
59-534 |
3.25e-61 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 210.12 E-value: 3.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 59 VAGTAGKVQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGK 138
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 139 ILPEGVGEVQEFVDICDY----AVGL--SRMFGGAIfpserPQHT-ILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTV 211
Cdd:PRK09407 107 ARRHAFEEVLDVALTARYyarrAPKLlaPRRRAGAL-----PVLTkTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 212 GNTVLWKGAPSTSLvsvaTTKIVTDVIKRNKLPP----IVTlcqG-GEDVGKRMVsdERIRLMSFTGSTAVGRTVGIEMQ 286
Cdd:PRK09407 182 GNAVVLKPDSQTPL----TALAAVELLYEAGLPRdlwqVVT---GpGPVVGTALV--DNADYLMFTGSTATGRVLAEQAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 287 RRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDS 366
Cdd:PRK09407 253 RRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAM--RLGAGYDY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 367 ATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKV-IDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEA 445
Cdd:PRK09407 331 SADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKArPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 446 ISWNNEVDQGLSSSLFTNNIQSAfeWLGESGSDCGIVNINTS--PSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTI 523
Cdd:PRK09407 411 VERANDTPYGLNASVWTGDTARG--RAIAARIRAGTVNVNEGyaAAWGSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
490
....*....|.
gi 158296454 524 TVNHStdLPLA 534
Cdd:PRK09407 489 ATQRV--LPLA 497
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
114-474 |
3.89e-61 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 206.90 E-value: 3.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 114 IRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISA 193
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 194 FNFPCAVFGWNAAIALTVGNTVLWKGAPSTSLVSVATTKIVTDVikrnKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSF 271
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEI----GLPKgVFNLVLGrGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 272 TGSTAVGRTVGIEMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVK 351
Cdd:PRK10090 157 TGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 352 RYASLlkRVGHPLDSATL-YGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETF 430
Cdd:PRK10090 237 AMQAV--QFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETF 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 158296454 431 APIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEWLGE 474
Cdd:PRK10090 315 GPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKG 358
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
55-517 |
1.39e-60 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 208.89 E-value: 1.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKV-QSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQE--WKKIPAPLRGDVIRQIGDELRKYREPLGKL 131
Cdd:PLN02466 63 NGQFVDAASGKTfPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAAL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 132 VALEMGKILPEGVG-EVQEFVDICDYAVGLSRMFGGAIFPSERPQH--TILEkwnPLGLVGVISAFNFPCAVFGWNAAIA 208
Cdd:PLN02466 143 ETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPADGPHHvqTLHE---PIGVAGQIIPWNFPLLMFAWKVGPA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 209 LTVGNTVLWKGAPSTSLVSVATTKIVTDVikrnKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTV-GIEM 285
Cdd:PLN02466 220 LACGNTIVLKTAEQTPLSALYAAKLLHEA----GLPPgVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVlELAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 286 QRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRyaSLLKRVGHPLD 365
Cdd:PLN02466 296 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKAR--ALKRVVGDPFK 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 366 SATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEA 445
Cdd:PLN02466 374 KGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEV 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158296454 446 ISWNNEVDQGLSSSLFTNNIQSAFEWlgESGSDCGIVNINT-SPSGAEIggAFGGEKHTGGGRESGSDAWKQY 517
Cdd:PLN02466 454 IRRANNTRYGLAAGVFTQNLDTANTL--SRALRVGTVWVNCfDVFDAAI--PFGGYKMSGIGREKGIYSLNNY 522
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
94-513 |
4.94e-60 |
|
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: 204.43 E-value: 4.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 94 AGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQEFVDICDYAVGLSRmfggaifpsER 173
Cdd:cd07095 8 AARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYH---------ER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 174 --------PQHTILEKWNPLGLVGVISAFNFPcAVFGwNAAI--ALTVGNTVLWKGAPSTSLVSVATTKIVTDVikrnKL 243
Cdd:cd07095 79 tgeratpmAQGRAVLRHRPHGVMAVFGPFNFP-GHLP-NGHIvpALLAGNTVVFKPSELTPAVAELMVELWEEA----GL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 244 PP-IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCL-LELGGNNALIINEDAPQEMALDAAFFGC 321
Cdd:cd07095 153 PPgVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAAYLIVQSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 322 IGTAGQRCTTTRRLIIHAKLY-DSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGG 400
Cdd:cd07095 233 FLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRL--RIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 401 KVIDRAGFFVEPTIIsNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNiQSAFEWLGeSGSDCG 480
Cdd:cd07095 311 ERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDD-EALFERFL-ARIRAG 387
|
410 420 430
....*....|....*....|....*....|...
gi 158296454 481 IVNINTSPSGAEIGGAFGGEKHTGGGRESGSDA 513
Cdd:cd07095 388 IVNWNRPTTGASSTAPFGGVGLSGNHRPSAYYA 420
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
68-508 |
4.95e-58 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 200.09 E-value: 4.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 68 SIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEV 147
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 148 QEFVDICD-YAvglsrMFGGAIFPSE----RPQHTILEkWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPS 222
Cdd:PRK13968 91 AKSANLCDwYA-----EHGPAMLKAEptlvENQQAVIE-YRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 223 TslvsVATTKIVTDVIKRNKLPPIVTLCQGGEDVG-KRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNA 301
Cdd:PRK13968 165 V----MGCAQLIAQVFKDAGIPQGVYGWLNADNDGvSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 302 LIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDN 381
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAAL--KMGDPRDEENALGPMARFDLRDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 382 YLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLF 461
Cdd:PRK13968 319 LHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 158296454 462 TNNIQSAFEWLGEsgSDCGIVNINT-SPSGAEIggAFGGEKHTGGGRE 508
Cdd:PRK13968 399 TTDETQARQMAAR--LECGGVFINGyCASDARV--AFGGVKKSGFGRE 442
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
55-510 |
7.33e-58 |
|
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: 199.65 E-value: 7.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKVQS-IDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVA 133
Cdd:cd07138 4 DGAWVAPAGTETIDvINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 134 LEMGK-ILPEGVGEVQEFVDICDYAVGLSRMFggaifPSERPQHTILEKWNPLGLVGVISAFNFP-----CAVFgwnAAI 207
Cdd:cd07138 84 LEMGApITLARAAQVGLGIGHLRAAADALKDF-----EFEERRGNSLVVREPIGVCGLITPWNWPlnqivLKVA---PAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 208 AltVGNTVLWKgaPSTslVSVATTKIVTDVIKRNKLPPIV-TLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEM 285
Cdd:cd07138 156 A--AGCTVVLK--PSE--VAPLSAIILAEILDEAGLPAGVfNLVNGdGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 286 QRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAkLVKRYASLLKrVGHPLD 365
Cdd:cd07138 230 ADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEE-IAAAAAEAYV-VGDPRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 366 SATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGG----KVIDRaGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASN 441
Cdd:cd07138 308 PATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpgrpEGLER-GYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDD 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158296454 442 LQEAISWNNEVDQGLSSSLFTNNIQSAfEWLGeSGSDCGIVNINTSPsgAEIGGAFGGEKHTGGGRESG 510
Cdd:cd07138 387 EDEAIAIANDTPYGLAGYVWSADPERA-RAVA-RRLRAGQVHINGAA--FNPGAPFGGYKQSGNGREWG 451
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
97-525 |
1.22e-57 |
|
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: 198.18 E-value: 1.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 97 AAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGkilpeGVGEVQEF-VD-----ICDYAVGLSRMFGGAIfP 170
Cdd:cd07105 11 AAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETG-----ATAAWAGFnVDlaagmLREAASLITQIIGGSI-P 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 171 SERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGapstSLVSVATTKIVTDVIKRNKLPP----I 246
Cdd:cd07105 85 SDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKA----SELSPRTHWLIGRVFHEAGLPKgvlnV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 247 VTLC-QGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTA 325
Cdd:cd07105 161 VTHSpEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 326 GQRCTTTRRLIIHAKLYDSFIAKLVKRYASLLKRVGHPldsatlyGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDR 405
Cdd:cd07105 241 GQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL-------GSLVSAAAADRVKELVDDALSKGAKLVVGGLADES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 406 A-GFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEwLGESgSDCGIVNI 484
Cdd:cd07105 314 PsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALA-VAKR-IESGAVHI 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 158296454 485 NTSPSGAEIGGAFGGEKHTGGGRESGSDAWKQYARRSTITV 525
Cdd:cd07105 392 NGMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
55-510 |
2.18e-57 |
|
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: 199.73 E-value: 2.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKVqsIDPASG-RVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVA 133
Cdd:cd07125 39 GEETETGEGAPV--IDPADHeRTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 134 LEMGKILPEGVGEVQEFVDICD-YAVGLSRMFGGAIFPSERPQHTILEkWNPLGLVGVISAFNFPCAVFGWNAAIALTVG 212
Cdd:cd07125 117 AEAGKTLADADAEVREAIDFCRyYAAQARELFSDPELPGPTGELNGLE-LHGRGVFVCISPWNFPLAIFTGQIAAALAAG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 213 NTVLWKGAPSTSLVSVATTKIVTDV-IKRNKLppIVTLCQgGEDVGKRMVSDERIRLMSFTGSTAVGRTvgieMQR---- 287
Cdd:cd07125 196 NTVIAKPAEQTPLIAARAVELLHEAgVPRDVL--QLVPGD-GEEIGEALVAHPRIDGVIFTGSTETAKL----INRalae 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 288 RFGR--CLL-ELGGNNALIINEDAPQEMALD----AAFfgciGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRV 360
Cdd:cd07125 269 RDGPilPLIaETGGKNAMIVDSTALPEQAVKdvvqSAF----GSAGQRCSALRLLYLQEEIAERFIEMLKGAMASL--KV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 361 GHPLDSATLYGPVHNQQAVDNyLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNlpHDAPVVKRETFAPIVYV--FK 438
Cdd:cd07125 343 GDPWDLSTDVGPLIDKPAGKL-LRAHTELMRGEAWLIAPAPLDDGNGYFVAPGIIEI--VGIFDLTTEVFGPILHVirFK 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158296454 439 ASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEWLGESGSdcGIVNINTSPSGAeIGGA--FGGEKHTGGGRESG 510
Cdd:cd07125 420 AEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEA--GNLYINRNITGA-IVGRqpFGGWGLSGTGPKAG 490
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
66-508 |
3.49e-57 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 197.65 E-value: 3.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 66 VQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVG 145
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 146 EVQEFVDICDY-----------------AVGLSRMFGgaifpserpqhtileKWNPLGLVGVISAFNFPCavfgWN---- 204
Cdd:PRK09406 83 EALKCAKGFRYyaehaealladepadaaAVGASRAYV---------------RYQPLGVVLAVMPWNFPL----WQvvrf 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 205 AAIALTVGNTVLWKGA---PSTSLVsvattkiVTDVIKRNKLPP--IVTLCQGGEDVgKRMVSDERIRLMSFTGSTAVGR 279
Cdd:PRK09406 144 AAPALMAGNVGLLKHAsnvPQTALY-------LADLFRRAGFPDgcFQTLLVGSGAV-EAILRDPRVAAATLTGSEPAGR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 280 TVGIEMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkR 359
Cdd:PRK09406 216 AVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAAL--R 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 360 VGHPLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKA 439
Cdd:PRK09406 294 VGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRV 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 440 SNLQEAISWNNEVDQGLSSSLFTNNIQSAFEWLgeSGSDCGIVNIN-TSPSGAEIGgaFGGEKHTGGGRE 508
Cdd:PRK09406 374 ADIDEAIEIANATTFGLGSNAWTRDEAEQERFI--DDLEAGQVFINgMTVSYPELP--FGGVKRSGYGRE 439
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
55-524 |
2.87e-55 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 193.50 E-value: 2.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKV-QSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQ--EWKKIPAPLRGDVIRQIGDELRKYREPLGKL 131
Cdd:PLN02766 26 NGEFVDAASGKTfETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 132 VALEMGKILPEGvgevqEFVDICDyAVGLSRMFGGA-------IFPSERPQH--TILEkwnPLGLVGVISAFNFPCAVFG 202
Cdd:PLN02766 106 DTIDAGKLFALG-----KAVDIPA-AAGLLRYYAGAadkihgeTLKMSRQLQgyTLKE---PIGVVGHIIPWNFPSTMFF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 203 WNAAIALTVGNTVLWKGAPSTSLVSVATTKIVtdviKRNKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRT 280
Cdd:PLN02766 177 MKVAPALAAGCTMVVKPAEQTPLSALFYAHLA----KLAGVPDgVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 281 VgieMQRRFGRCL----LELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASL 356
Cdd:PLN02766 253 I---MQAAATSNLkqvsLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDW 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 357 LkrVGHPLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYV 436
Cdd:PLN02766 330 V--VGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 437 FKASNLQEAISWNNEVDQGLSSSLFTNNIQSAfEWLGESgSDCGIVNINTSpSGAEIGGAFGGEKHTGGGRESGSDAWKQ 516
Cdd:PLN02766 408 MKFKTVEEAIKKANNTKYGLAAGIVTKDLDVA-NTVSRS-IRAGTIWVNCY-FAFDPDCPFGGYKMSGFGRDQGMDALDK 484
|
....*....
gi 158296454 517 Y-ARRSTIT 524
Cdd:PLN02766 485 YlQVKSVVT 493
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
71-506 |
2.83e-51 |
|
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: 181.85 E-value: 2.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 71 PASGRVIAEVATGSEQDLERCLTAGVAAYQE---WkkIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEV 147
Cdd:cd07148 6 PFDLKPIGEVPTVDWAAIDKALDTAHALFLDrnnW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 148 QEFVDICDYAVGLSRMFGGAIFP-------SERPQHTILEkwnPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGA 220
Cdd:cd07148 84 TRAIDGVELAADELGQLGGREIPmgltpasAGRIAFTTRE---PIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 221 PSTSLVSVATTKIVTDVikrnKLPPivTLCQG---GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRfGRCLLELG 297
Cdd:cd07148 161 LATPLSCLAFVDLLHEA----GLPE--GWCQAvpcENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 298 GNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQ 377
Cdd:cd07148 234 GAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKL--VVGDPTDPDTEVGPLIRPR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 378 AVDNYLQTVQEAVALGGKVECGGKVIDRAGFfvEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLS 457
Cdd:cd07148 312 EVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQ 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 158296454 458 SSLFTNNIQSAFEWLGESGSDCGIVNINTS------PsgaeiggaFGGEKHTGGG 506
Cdd:cd07148 390 AAVFTKDLDVALKAVRRLDATAVMVNDHTAfrvdwmP--------FAGRRQSGYG 436
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
55-509 |
4.72e-49 |
|
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: 176.49 E-value: 4.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGK-VQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVA 133
Cdd:cd07116 6 GGEWVAPVKGEyFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 134 LEMGKILPEGVG-EVQEFVDICDYAVGLSRMFGGAIfpSERPQHTILEKWN-PLGLVGVISAFNFPCAVFGWNAAIALTV 211
Cdd:cd07116 86 WDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSI--SEIDENTVAYHFHePLGVVGQIIPWNFPLLMATWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 212 GNTVLWKGAPSTSLVSVATTKIVTDVikrnkLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVgieMQRRF 289
Cdd:cd07116 164 GNCVVLKPAEQTPASILVLMELIGDL-----LPPgVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLI---MQYAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 290 GRCL---LELGGNNALIINEDApqeMALDAAFF-----GCIGTA---GQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlk 358
Cdd:cd07116 236 ENIIpvtLELGGKSPNIFFADV---MDADDAFFdkaleGFVMFAlnqGEVCTCPSRALIQESIYDRFMERALERVKAI-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 359 RVGHPLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGkviDRA--------GFFVEPTIISNlpHDAPVVKRETF 430
Cdd:cd07116 311 KQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGG---ERNelggllggGYYVPTTFKGG--NKMRIFQEEIF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 431 APIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEwLGEsGSDCGIVNIN---TSPSGAeiggAFGGEKHTGGGR 507
Cdd:cd07116 386 GPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYR-MGR-GIQAGRVWTNcyhLYPAHA----AFGGYKQSGIGR 459
|
..
gi 158296454 508 ES 509
Cdd:cd07116 460 EN 461
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
70-510 |
2.12e-48 |
|
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: 174.03 E-value: 2.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 70 DPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGV-GEVq 148
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 149 efVDICDYAVGLSRMFGGAIFPSERPQHTILE------KWNPLGLVGVISAFNFPCAVFgWNAAI-ALTVGNTVLWKGAP 221
Cdd:cd07098 81 --LVTCEKIRWTLKHGEKALRPESRPGGLLMFykrarvEYEPLGVVGAIVSWNYPFHNL-LGPIIaALFAGNAIVVKVSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 222 STSLVSVATTKIVTDVIKRNKLPP-IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNN 300
Cdd:cd07098 158 QVAWSSGFFLSIIRECLAACGHDPdLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 301 ALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVD 380
Cdd:cd07098 238 PAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQAL--RQGPPLDGDVDVGAMISPARFD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 381 NYLQTVQEAVALGGKVECGGK----VIDRAGFFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGL 456
Cdd:cd07098 316 RLEELVADAVEKGARLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158296454 457 SSSLFTNNIQSAFEWLgeSGSDCGIVNINtspsgaEIGGA-------FGGEKHTGGGRESG 510
Cdd:cd07098 396 GASVFGKDIKRARRIA--SQLETGMVAIN------DFGVNyyvqqlpFGGVKGSGFGRFAG 448
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
55-509 |
5.51e-47 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 170.91 E-value: 5.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKVQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVAL 134
Cdd:PRK09457 6 NGDWIAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 135 EMGKILPEGVGEVQEFVDICDYAV-------GLSRmfggaifpSERPQHTILEKWNPLGLVGVISAFNFPcavfGW--NA 205
Cdd:PRK09457 86 ETGKPLWEAATEVTAMINKIAISIqayhertGEKR--------SEMADGAAVLRHRPHGVVAVFGPYNFP----GHlpNG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 206 AI--ALTVGNTVLWKGAPSTSLVSVATTKIVTDVikrnKLPP-IVTLCQGGEDVGKRMVSDERIRLMSFTGSTavgRTvG 282
Cdd:PRK09457 154 HIvpALLAGNTVVFKPSELTPWVAELTVKLWQQA----GLPAgVLNLVQGGRETGKALAAHPDIDGLLFTGSA---NT-G 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 283 IEMQRRF----GRCL-LELGGNNALIINE----DAPQEMALDAAFFgcigTAGQRCTTTRRLII-HAKLYDSFIAKLVKR 352
Cdd:PRK09457 226 YLLHRQFagqpEKILaLEMGGNNPLVIDEvadiDAAVHLIIQSAFI----SAGQRCTCARRLLVpQGAQGDAFLARLVAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 353 YASLlkRVGHPL-DSATLYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTIIsNLPHDAPVVKRETFA 431
Cdd:PRK09457 302 AKRL--TVGRWDaEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFG 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158296454 432 PIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEWLGESGSdcGIVNINTSPSGAEIGGAFGGEKHTGGGRES 509
Cdd:PRK09457 379 PLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRA--GIVNWNKPLTGASSAAPFGGVGASGNHRPS 454
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
56-524 |
2.60e-44 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 163.51 E-value: 2.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 56 GEWVAGTAGKVQSI-DPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVAL 134
Cdd:TIGR01722 7 GKFAEGASGTYIPVtNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 135 EMGKILPEGVGEVQEFVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNT 214
Cdd:TIGR01722 87 EHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 215 VLWKGAPSTSLVSVATTKIVTDVikrnKLPP-IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCL 293
Cdd:TIGR01722 167 FVLKPSEKVPSAAVKLAELFSEA----GAPDgVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 294 LELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLyDSFIAKLVKRYASLlkRVGHPLDSATLYGPV 373
Cdd:TIGR01722 243 ALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKI--RIGPGDDPGAEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 374 HNQQAVDNYLQTVQEAVALGGKVECGGKVIDRAGF----FVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWN 449
Cdd:TIGR01722 320 ITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158296454 450 NEVDQGLSSSLFTNNIQSAFEWLGEsgSDCGIVNINTsPSGAEIG-GAFGGEKHT--GGGRESGSDAWKQYARRSTIT 524
Cdd:TIGR01722 400 NASPYGNGTAIFTRDGAAARRFQHE--IEVGQVGVNV-PIPVPLPyFSFTGWKDSffGDHHIYGKQGTHFYTRGKTVT 474
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
64-510 |
3.94e-43 |
|
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: 160.46 E-value: 3.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 64 GKVQSI-DPASGR-VIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILP 141
Cdd:TIGR01238 50 GEAQPVtNPADRRdIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 142 EGVGEVQEFVDICDYAVGLSRmfggAIFPSERPQhtilekwnPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAP 221
Cdd:TIGR01238 130 NAIAEVREAVDFCRYYAKQVR----DVLGEFSVE--------SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 222 STSLVSVATTKIVTDVikrnKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRF---GRCLLEL 296
Cdd:TIGR01238 198 QTSLIAYRAVELMQEA----GFPAgTIQLLPGrGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAET 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 297 GGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQ 376
Cdd:TIGR01238 274 GGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQEL--KVGVPHLLTTDVGPVIDA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 377 QAVDNYLQTVQEAVALGGKVECGGKVIDRA---GFFVEPTIISnlPHDAPVVKRETFAPIVYV--FKASNLQEAISWNNE 451
Cdd:TIGR01238 352 EAKQNLLAHIEHMSQTQKKIAQLTLDDSRAcqhGTFVAPTLFE--LDDIAELSEEVFGPVLHVvrYKARELDQIVDQINQ 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 452 VDQGLSSSLFTnNIQSAFEWLgESGSDCGIVNINTSPSGAEIG-GAFGGEKHTGGGRESG 510
Cdd:TIGR01238 430 TGYGLTMGVHS-RIETTYRWI-EKHARVGNCYVNRNQVGAVVGvQPFGGQGLSGTGPKAG 487
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
59-447 |
8.35e-43 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 163.83 E-value: 8.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 59 VAGTAGKVQSIDPASGR-VIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMG 137
Cdd:PRK11904 557 INGEGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAG 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 138 KILPEGVGEVQEFVDICD-YAVGLSRMFGGAIF---PS-ERpqhtilekwNPLGLVG-----VISAFNFPCAVF-GWNAA 206
Cdd:PRK11904 637 KTLQDAIAEVREAVDFCRyYAAQARRLFGAPEKlpgPTgES---------NELRLHGrgvfvCISPWNFPLAIFlGQVAA 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 207 iALTVGNTVLWKGAPSTSLVSVATTK------IVTDVIKrnklppivtLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGR 279
Cdd:PRK11904 708 -ALAAGNTVIAKPAEQTPLIAAEAVKllheagIPKDVLQ---------LLPGdGATVGAALTADPRIAGVAFTGSTETAR 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 280 TVGIEMQRRFGR--CLL-ELGGNNALIINEDA-PQEMALDA---AFfgciGTAGQRCTTTRRLIIHAKLYDSFIAKLVKR 352
Cdd:PRK11904 778 IINRTLAARDGPivPLIaETGGQNAMIVDSTAlPEQVVDDVvtsAF----RSAGQRCSALRVLFVQEDIADRVIEMLKGA 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 353 YASLlkRVGHPLDSATLYGPVHNQQAVDN---YLQTVQEAVALGGKVECGGKVidRAGFFVEPTIISnLPhDAPVVKRET 429
Cdd:PRK11904 854 MAEL--KVGDPRLLSTDVGPVIDAEAKANldaHIERMKREARLLAQLPLPAGT--ENGHFVAPTAFE-ID-SISQLEREV 927
|
410 420
....*....|....*....|
gi 158296454 430 FAPIVYV--FKASNLQEAIS 447
Cdd:PRK11904 928 FGPILHVirYKASDLDKVID 947
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
71-446 |
3.73e-42 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 161.96 E-value: 3.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 71 PA-SGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQE 149
Cdd:PRK11905 574 PAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVRE 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 150 FVDICD-YAVGLSRMFGGAIFPserpqhtilekwnPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSLVSV 228
Cdd:PRK11905 654 AVDFLRyYAAQARRLLNGPGHK-------------PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAA 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 229 ATTKIVTDV-IKRNKLppiVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGR--CLL-ELGGNNALII 304
Cdd:PRK11905 721 RAVRLLHEAgVPKDAL---QLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPpvPLIaETGGQNAMIV 797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 305 NEDAPQEMALDA----AFfgciGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVD 380
Cdd:PRK11905 798 DSSALPEQVVADviasAF----DSAGQRCSALRVLCLQEDVADRVLTMLKGAMDEL--RIGDPWRLSTDVGPVIDAEAQA 871
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158296454 381 NYLQTVQEAVALGGKV-ECGGKVIDRAGFFVEPTII--SNLphdaPVVKRETFAPIVYV--FKASNLQEAI 446
Cdd:PRK11905 872 NIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLIeiDSI----SDLEREVFGPVLHVvrFKADELDRVI 938
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
55-442 |
3.72e-40 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 156.25 E-value: 3.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKVQSidPASGR-VIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVA 133
Cdd:COG4230 563 AGEAASGEARPVRN--PADHSdVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLV 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 134 LEMGKILPEGVGEVQEFVDICD-YAVGLSRMFGgaifpserpQHTILEkwnPLGLVGVISAFNFPCAVF-GWNAAiALTV 211
Cdd:COG4230 641 REAGKTLPDAIAEVREAVDFCRyYAAQARRLFA---------APTVLR---GRGVFVCISPWNFPLAIFtGQVAA-ALAA 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 212 GNTVLWKGAPSTSLVSVATTKIV------TDVikrnklppiVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIE 284
Cdd:COG4230 708 GNTVLAKPAEQTPLIAARAVRLLheagvpADV---------LQLLPGdGETVGAALVADPRIAGVAFTGSTETARLINRT 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 285 MQRRFGRCLL---ELGGNNALIINEDAPQEM----ALDAAFfgciGTAGQRCTTTRRLIIHAKLYDSFIAklvkryasLL 357
Cdd:COG4230 779 LAARDGPIVPliaETGGQNAMIVDSSALPEQvvddVLASAF----DSAGQRCSALRVLCVQEDIADRVLE--------ML 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 358 K------RVGHPLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKV-ECGGKVIDRAGFFVEPTI--ISNLPHdapvVKRE 428
Cdd:COG4230 847 KgamaelRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLieIDSISD----LERE 922
|
410
....*....|....*.
gi 158296454 429 TFAPIVYV--FKASNL 442
Cdd:COG4230 923 VFGPVLHVvrYKADEL 938
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
66-468 |
2.36e-39 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 151.44 E-value: 2.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 66 VQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVG 145
Cdd:PLN02419 131 IDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 146 EVQEFVDICDYAVGLSRMFGGAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSL 225
Cdd:PLN02419 211 DIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 226 VSVattkIVTDVIKRNKLPP-IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALII 304
Cdd:PLN02419 291 ASV----ILAELAMEAGLPDgVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLV 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 305 NEDAPQEMALDAAFFGCIGTAGQRCT--TTRRLIIHAKLYDSfiaKLVKRYASLLKRVGHPLDSAtlYGPVHNQQAVDNY 382
Cdd:PLN02419 367 LPDANIDATLNALLAAGFGAAGQRCMalSTVVFVGDAKSWED---KLVERAKALKVTCGSEPDAD--LGPVISKQAKERI 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 383 LQTVQEAVALGGKVECGGKVIDRAGF----FVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSS 458
Cdd:PLN02419 442 CRLIQSGVDDGAKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGA 521
|
410
....*....|
gi 158296454 459 SLFTNNIQSA 468
Cdd:PLN02419 522 AIFTSSGAAA 531
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
54-523 |
1.88e-37 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 144.65 E-value: 1.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 54 YNGEWVAGTAGKV-QSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQ--EWKKIPAPLRGDVIRQIGDELRKYREPLGK 130
Cdd:PRK09847 24 INGEYTAAAENETfETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 131 LVALEMGKILPEGVGEvqefvDICD-------YAVGLSRMFGgAIFPSERPQHTILEKwNPLGLVGVISAFNFPCAVFGW 203
Cdd:PRK09847 104 LETLDTGKPIRHSLRD-----DIPGaarairwYAEAIDKVYG-EVATTSSHELAMIVR-EPVGVIAAIVPWNFPLLLTCW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 204 NAAIALTVGNTVLWKGAPSTSLVSVATTKIVtdviKRNKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTV 281
Cdd:PRK09847 177 KLGPALAAGNSVILKPSEKSPLSAIRLAGLA----KEAGLPDgVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 282 GIEM-QRRFGRCLLELGGNNALIINEDAPQ-EMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLvKRYASLLKR 359
Cdd:PRK09847 253 LKDAgDSNMKRVWLEAGGKSANIVFADCPDlQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALL-KQQAQNWQP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 360 vGHPLDSATLYGPVHNQQAVDNYLQTVQEAVAlGGKVECGGKVIDRAGFfVEPTIISNLPHDAPVVKRETFAPIVYVFKA 439
Cdd:PRK09847 332 -GHPLDPATTMGTLIDCAHADSVHSFIREGES-KGQLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 440 SNLQEAISWNNEVDQGLSSSLFTNNIQSAFEWLGESGSdcGIVNINTSPSGaEIGGAFGGEKHTGGGRESGSDAWKQYAR 519
Cdd:PRK09847 409 TSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKA--GSVFVNNYNDG-DMTVPFGGYKQSGNGRDKSLHALEKFTE 485
|
....
gi 158296454 520 RSTI 523
Cdd:PRK09847 486 LKTI 489
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
56-456 |
1.92e-37 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 147.81 E-value: 1.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 56 GEWVAGTAGKVqsIDPASGR-VIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVAL 134
Cdd:PRK11809 653 DPVAAGEMSPV--INPADPRdIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVR 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 135 EMGKILPEGVGEVQEFVDICDYAVGLSRmfggAIFPSErpQHtilekwNPLGLVGVISAFNFPCAVFGWNAAIALTVGNT 214
Cdd:PRK11809 731 EAGKTFSNAIAEVREAVDFLRYYAGQVR----DDFDND--TH------RPLGPVVCISPWNFPLAIFTGQVAAALAAGNS 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 215 VLWKGAPSTSLVSVATTKIVTDVikrnKLPP-IVTLCQG-GEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRRF--- 289
Cdd:PRK11809 799 VLAKPAEQTPLIAAQAVRILLEA----GVPAgVVQLLPGrGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpq 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 290 GRC---LLELGGNNALIINEDAPQEMA----LDAAFfgciGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGH 362
Cdd:PRK11809 875 GRPiplIAETGGQNAMIVDSSALTEQVvadvLASAF----DSAGQRCSALRVLCLQDDVADRTLKMLRGAMAEC--RMGN 948
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 363 PLDSATLYGPVHNQQAVDNYLQTVQEAVALGGKV---ECGGKVIDRAGFFVEPTIISNLPHDApvVKRETFAPIVYV--F 437
Cdd:PRK11809 949 PDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVfqaARENSEDWQSGTFVPPTLIELDSFDE--LKREVFGPVLHVvrY 1026
|
410
....*....|....*....
gi 158296454 438 KASNLQEAISWNNEVDQGL 456
Cdd:PRK11809 1027 NRNQLDELIEQINASGYGL 1045
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
184-523 |
1.59e-33 |
|
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: 132.34 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 184 PLGLVGVISAFNFP-----CAVFGwnaaiALTVGNTVLWKGapstSLVSVATTKIVTDVIKRNKLPPIVTLCQGGEDVGK 258
Cdd:cd07135 108 PLGVVLIIGPWNYPvllalSPLVG-----AIAAGCTVVLKP----SELTPHTAALLAELVPKYLDPDAFQVVQGGVPETT 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 259 RMVsDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIH 338
Cdd:cd07135 179 ALL-EQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 339 AKLYDSFIAKLVKRYASLLKRVGHPLDSatlYGPVHNQQAVDNYLQTVQEAvalGGKVECGGKViDRAGFFVEPTIISNL 418
Cdd:cd07135 258 PSVYDEFVEELKKVLDEFYPGGANASPD---YTRIVNPRHFNRLKSLLDTT---KGKVVIGGEM-DEATRFIPPTIVSDV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 419 PHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNiQSAFEW-LGE--SGS----DCGI-VNINTSPsg 490
Cdd:cd07135 331 SWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDD-KSEIDHiLTRtrSGGvvinDTLIhVGVDNAP-- 407
|
330 340 350
....*....|....*....|....*....|...
gi 158296454 491 aeiggaFGGEKHTGGGRESGSDAWKQYARRSTI 523
Cdd:cd07135 408 ------FGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
88-523 |
5.13e-33 |
|
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: 131.21 E-value: 5.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 88 LERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGK---ILPEGVGEVQEFVDICDYAVGLSRMF 164
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKgwmFAENICGDQVQLRARAFVIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 165 GGAIFPSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSLVSVATTKIVTDVIkrnKLP 244
Cdd:cd07084 81 EPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAG---LLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 245 P-IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVGIEMqrRFGRCLLELGGNNALIINEDAPQ--EMALDAAFFGC 321
Cdd:cd07084 158 PeDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQAvdYVAWQCVQDMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 322 IGTaGQRCTTTRRLIIHA-----KLYDSFIAKLVKRyasllkrvghpLDSATLYGPVHNqqavDNYLQTVQEAVALGG-K 395
Cdd:cd07084 236 ACS-GQKCTAQSMLFVPEnwsktPLVEKLKALLARR-----------KLEDLLLGPVQT----FTTLAMIAHMENLLGsV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 396 VECGGKVI--DRAGFFVEPTIISNL--PHDA-----PVVKRETFAPIVYVFKASNLQEA-ISWNNEVDQG-LSSSLFTNN 464
Cdd:cd07084 300 LLFSGKELknHSIPSIYGACVASALfvPIDEilktyELVTEEIFGPFAIVVEYKKDQLAlVLELLERMHGsLTAAIYSND 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158296454 465 IQSAFEWLGESGSDCGIVNINTSPSGAEIGGAFGGEKHTGGGRES--GSDAWKQYARRSTI 523
Cdd:cd07084 380 PIFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGigGPEAIKLVWRCHAE 440
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
24-506 |
2.68e-31 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 126.79 E-value: 2.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 24 SMSGMTKYLVEEDNFAFLRDlglqrvnngvynGEWVAGTAGK-VQSIDPASGRVIAEVATGSEQDLERCLTAGVAAYQEW 102
Cdd:PLN00412 2 AGTGFFAEILDGDVYKYYAD------------GEWRTSSSGKsVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 103 KKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQEFVDICDYA-------VGLSRMFGGAIFP-SERP 174
Cdd:PLN00412 70 AKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTaeegvriLGEGKFLVSDSFPgNERN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 175 QHTILEKWnPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKgaPSTSlVSVATTKIVtDVIKRNKLPP-IVTLCQG- 252
Cdd:PLN00412 150 KYCLTSKI-PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLK--PPTQ-GAVAALHMV-HCFHLAGFPKgLISCVTGk 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 253 GEDVGKRMVSDERIRLMSFTGstavGRTvGIEMQRRFGRCLL--ELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCT 330
Cdd:PLN00412 225 GSEIGDFLTMHPGVNCISFTG----GDT-GIAISKKAGMVPLqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 331 TTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAvdNYLQT-VQEAVALGGKVECGGKvidRAGFF 409
Cdd:PLN00412 300 AVKVVLVMESVADALVEKVNAKVAKL--TVGPPEDDCDITPVVSESSA--NFIEGlVMDAKEKGATFCQEWK---REGNL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 410 VEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFewLGESGSDCGIVNINTSPS 489
Cdd:PLN00412 373 IWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAI--LISDAMETGTVQINSAPA 450
|
490
....*....|....*..
gi 158296454 490 GAEIGGAFGGEKHTGGG 506
Cdd:PLN00412 451 RGPDHFPFQGLKDSGIG 467
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
184-507 |
3.78e-31 |
|
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: 125.33 E-value: 3.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 184 PLGLVGVISAFNFPC------AVfgwnAAIAltVGNTVLWKgaPSTslVSVATTKIVTDVIKRNKLPPIVTLCQGGEDVG 257
Cdd:cd07087 100 PLGVVLIIGPWNYPLqlalapLI----GAIA--AGNTVVLK--PSE--LAPATSALLAKLIPKYFDPEAVAVVEGGVEVA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 258 KRMvSDERIRLMSFTGSTAVGRTVgieMQ---RRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRR 334
Cdd:cd07087 170 TAL-LAEPFDHIFFTGSPAVGKIV---MEaaaKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 335 LIIHAKLYDSFIAKLVKR----YASLlkrvghPLDSATlYGPVHNQQAVD---NYLQtvqeavalGGKVECGGKViDRAG 407
Cdd:cd07087 246 VLVHESIKDELIEELKKAikefYGED------PKESPD-YGRIINERHFDrlaSLLD--------DGKVVIGGQV-DKEE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 408 FFVEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNN--IQSAFewLGE--SGSDCgiVN 483
Cdd:cd07087 310 RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDkaVQERV--LAEtsSGGVC--VN 385
|
330 340 350
....*....|....*....|....*....|.
gi 158296454 484 -------INTSPsgaeiggaFGGEKHTGGGR 507
Cdd:cd07087 386 dvllhaaIPNLP--------FGGVGNSGMGA 408
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
184-464 |
4.87e-30 |
|
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: 122.61 E-value: 4.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 184 PLGLVGVISAFNFPcavfgWNAAI-----ALTVGNTVLWKgaPSTSlvSVATTKIVTDVIKRNKLPPIVTLCQGGEDVGK 258
Cdd:cd07136 100 PYGVVLIIAPWNYP-----FQLALapligAIAAGNTAVLK--PSEL--TPNTSKVIAKIIEETFDEEYVAVVEGGVEENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 259 RMVsDERIRLMSFTGSTAVGRTVgieMQ---RRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRL 335
Cdd:cd07136 171 ELL-DQKFDYIFFTGSVRVGKIV---MEaaaKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 336 IIHAKLYDSFIAKLVKryaSLLKRVG-HPLDSATlYGPVHNQ---QAVDNYLQtvqeavalGGKVECGGKvIDRAGFFVE 411
Cdd:cd07136 247 LVHESVKEKFIKELKE---EIKKFYGeDPLESPD-YGRIINEkhfDRLAGLLD--------NGKIVFGGN-TDRETLYIE 313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 158296454 412 PTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNN 464
Cdd:cd07136 314 PTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSED 366
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
74-511 |
7.34e-30 |
|
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: 123.08 E-value: 7.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 74 GRVIAEVATGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELR-KYREplgKLVALEMgkiLPEGVGEVQEFVD 152
Cdd:cd07123 57 AHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRY---ELNAATM---LGQGKNVWQAEID 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 153 ----ICDYAvglsRMfgGAIFPSE----RPQHTILEKWN-----PL-GLVGVISAFNFpcAVFGWN--AAIALtVGNTVL 216
Cdd:cd07123 131 aaceLIDFL----RF--NVKYAEElyaqQPLSSPAGVWNrleyrPLeGFVYAVSPFNF--TAIGGNlaGAPAL-MGNVVL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 217 WKGAPStslvSVATTKIVTDVIKRNKLPP--IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGR----TVG--IEMQRR 288
Cdd:cd07123 202 WKPSDT----AVLSNYLVYKILEEAGLPPgvINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKslwkQIGenLDRYRT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 289 FGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSAT 368
Cdd:cd07123 278 YPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEI--KMGDPDDFSN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 369 LYGPVHNQQAVDN---YLQTVQEAVALggKVECGGKVIDRAGFFVEPTII-SNLPHDaPVVKRETFAPI--VYVFKASNL 442
Cdd:cd07123 356 FMGAVIDEKAFDRikgYIDHAKSDPEA--EIIAGGKCDDSVGYFVEPTVIeTTDPKH-KLMTEEIFGPVltVYVYPDSDF 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158296454 443 QEAIswnNEVDQ----GLSSSLFTNN---IQSAFEWLGESgsdCGIVNINTSPSGAEIggafgGEKHTGGGRESGS 511
Cdd:cd07123 433 EETL---ELVDTtspyALTGAIFAQDrkaIREATDALRNA---AGNFYINDKPTGAVV-----GQQPFGGARASGT 497
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
184-510 |
7.34e-27 |
|
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: 113.09 E-value: 7.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 184 PLGLVGVISAFNFP-CAVFGWNAAiALTVGNTVLWKgaPS--TSLVSVATTKIVTDVIKRNKlppiVTLCQGGEDVGKRm 260
Cdd:cd07134 100 PKGVCLIISPWNYPfNLAFGPLVS-AIAAGNTAILK--PSelTPHTSAVIAKIIREAFDEDE----VAVFEGDAEVAQA- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 261 vsderirLMS-------FTGSTAVGRTVgieMQ---RRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCT 330
Cdd:cd07134 172 -------LLElpfdhifFTGSPAVGKIV---MAaaaKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 331 TTRRLIIHAKLYDSFIAKLVKRYASLLKRVGHPLDSATlYGPVHNQQAVDNYLQTVQEAVALGGKVECGGKViDRAGFFV 410
Cdd:cd07134 242 APDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPD-LARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQF-DAAQRYI 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 411 EPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNiQSAFEW-LGESGSdcGIVNINTSPS 489
Cdd:cd07134 320 APTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKD-KANVNKvLARTSS--GGVVVNDVVL 396
|
330 340
....*....|....*....|..
gi 158296454 490 G-AEIGGAFGGEKHTGGGRESG 510
Cdd:cd07134 397 HfLNPNLPFGGVNNSGIGSYHG 418
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
184-506 |
2.27e-26 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 112.43 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 184 PLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKgaPSTslVSVATTKIVTDVIKRNKLPPIVTLCQGGEDVGKRMVSd 263
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLK--PSE--LSPHTSKLMAKLLTKYLDPSYVRVIEGGVEVTTELLK- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 264 ERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYD 343
Cdd:PTZ00381 184 EPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKD 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 344 SFIAKLvKRyaSLLKRVGHPLDSATLYGPVHNQQAVDNyLQTVQEAValGGKVECGGKViDRAGFFVEPTIISNLPHDAP 423
Cdd:PTZ00381 264 KFIEAL-KE--AIKEFFGEDPKKSEDYSRIVNEFHTKR-LAELIKDH--GGKVVYGGEV-DIENKYVAPTIIVNPDLDSP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 424 VVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNN--IQSAFEWLGESGS----DCGIVNINTS-Psgaeigga 496
Cdd:PTZ00381 337 LMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDkrHKELVLENTSSGAvvinDCVFHLLNPNlP-------- 408
|
330
....*....|
gi 158296454 497 FGGEKHTGGG 506
Cdd:PTZ00381 409 FGGVGNSGMG 418
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
55-523 |
3.50e-26 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 111.98 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKVQSIDPASGRVIAEVaTGSEQDLercltAGVAAYQEWKKIPAPL------RGDVIRQIGDELRKYREPL 128
Cdd:cd07128 6 AGQWHAGTGDGRTLHDAVTGEVVARV-SSEGLDF-----AAAVAYAREKGGPALRaltfheRAAMLKALAKYLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 129 GKLVA------------------------------LEMGKILPEGVGEVqefvdicdyavgLSRmfGGAIfpseRPQHTi 178
Cdd:cd07128 80 YALSAatgatrrdswididggigtlfayaslgrreLPNAHFLVEGDVEP------------LSK--DGTF----VGQHI- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 179 lekWNPLGLVGV-ISAFNFPCavfgW----NAAIALTVGNTVLWKGAPSTSLVsvaTTKIVTDVIKRNKLPP--IVTLCQ 251
Cdd:cd07128 141 ---LTPRRGVAVhINAFNFPV----WgmleKFAPALLAGVPVIVKPATATAYL---TEAVVKDIVESGLLPEgaLQLICG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 252 GGEDVGKRMVSDErirLMSFTGSTAVGRTVGIE--MQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGT----- 324
Cdd:cd07128 211 SVGDLLDHLGEQD---VVAFTGSAATAAKLRAHpnIVARSIRFNAEADSLNAAILGPDATPGTPEFDLFVKEVARemtvk 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 325 AGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHNQQAVDNYLQTV----QEAVAL-GGKVECG 399
Cdd:cd07128 288 AGQKCTAIRRAFVPEARVDAVIEALKARLAKV--VVGDPRLEGVRMGPLVSREQREDVRAAVatllAEAEVVfGGPDRFE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 400 GKVIDR-AGFFVEPTII-SNLPHDAPVVKR-ETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEWLGESG 476
Cdd:cd07128 366 VVGADAeKGAFFPPTLLlCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAA 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 158296454 477 SDCGIVNINTSPSGAEIGG--------AFGGEKHTGGGRE-SGSDAWKQYARRSTI 523
Cdd:cd07128 446 PYHGRLLVLNRDSAKESTGhgsplpqlVHGGPGRAGGGEElGGLRGVKHYMQRTAV 501
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
184-464 |
9.73e-25 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 106.80 E-value: 9.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 184 PLGLVGVISAFNFPCA-VFGwNAAIALTVGNTVLWKGAPSTSlvsvATTKIVTDVIKRNKLPPIVTLCQGGEDVGKRMVS 262
Cdd:cd07133 101 PLGVVGIIVPWNYPLYlALG-PLIAALAAGNRVMIKPSEFTP----RTSALLAELLAEYFDEDEVAVVTGGADVAAAFSS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 263 ---DERIrlmsFTGSTAVGRTVgieMqRRFGRCL----LELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRCTTTRRL 335
Cdd:cd07133 176 lpfDHLL----FTGSTAVGRHV---M-RAAAENLtpvtLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 336 IIHAKLYDSFIAKLVKRYASLLKRVGHPLDsatlYGPVHNQQAVDNYLQTVQEAVALGGKV-ECGGKVIDRAGF-FVEPT 413
Cdd:cd07133 248 LVPEDKLEEFVAAAKAAVAKMYPTLADNPD----YTSIINERHYARLQGLLEDARAKGARViELNPAGEDFAATrKLPPT 323
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 158296454 414 IISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNN 464
Cdd:cd07133 324 LVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGED 374
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
184-464 |
9.12e-22 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 97.87 E-value: 9.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 184 PLGLVGVISAFNFPCA-----VFGwnaaiALTVGNTVLWKgapsTSLVSVATTKIVTDVIKRNKLPPIVTLCQGGEDVGK 258
Cdd:cd07137 101 PLGVVLVISAWNFPFLlslepVIG-----AIAAGNAVVLK----PSELAPATSALLAKLIPEYLDTKAIKVIEGGVPETT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 259 RMVsDERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALIINEDAPQEMALD---AAFFGCigTAGQRCTTTRRL 335
Cdd:cd07137 172 ALL-EQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRriaGGKWGC--NNGQACIAPDYV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 336 IIHaklyDSFIAKLVKRYASLLKRV--GHPLDSATLYGPV--HNQQAVDNYLQ--TVQEAVALGGKvecggkvIDRAGFF 409
Cdd:cd07137 249 LVE----ESFAPTLIDALKNTLEKFfgENPKESKDLSRIVnsHHFQRLSRLLDdpSVADKIVHGGE-------RDEKNLY 317
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 158296454 410 VEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNN 464
Cdd:cd07137 318 IEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKN 372
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
181-464 |
1.90e-19 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 90.74 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 181 KWNPLGLVGVISAFNFPCA-----VFGwnaAIAltVGNTVLWKgaPSTslVSVATTKIVTDVIKR---NKLPPIVTlcqG 252
Cdd:cd07132 97 YKEPLGVVLIIGAWNYPLQltlvpLVG---AIA--AGNCVVIK--PSE--VSPATAKLLAELIPKyldKECYPVVL---G 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 253 GEDVGKRMVsDERIRLMSFTGSTAVGRTVgieMQ---RRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIGTAGQRC 329
Cdd:cd07132 165 GVEETTELL-KQRFDYIFYTGSTSVGKIV---MQaaaKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 330 TTTRRLIIHAKLYDSFIAKLVKryaSLLKRVGHPLDSATLYGPVHNqqavDNYLQTVQeAVALGGKVECGGKViDRAGFF 409
Cdd:cd07132 241 IAPDYVLCTPEVQEKFVEALKK---TLKEFYGEDPKESPDYGRIIN----DRHFQRLK-KLLSGGKVAIGGQT-DEKERY 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 158296454 410 VEPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNN 464
Cdd:cd07132 312 IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN 366
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
88-414 |
4.98e-18 |
|
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: 86.83 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 88 LERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGkiLPEG--VGEVqefvdicDYAVGLSRMFG 165
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEArlQGEL-------GRTTGQLRLFA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 166 ---------GAIFPSERPQHTILEKWN------PLGLVGVISAFNFPCA--VFGWNAAIALTVGNTVLWKGAPSTSLVSV 228
Cdd:cd07129 72 dlvregswlDARIDPADPDRQPLPRPDlrrmlvPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAHPAHPGTSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 229 ATTKIVTDVIKRNKLPP-IVTLCQGGE-DVGKRMVSDERIRLMSFTGSTAVGRTVGIEMQRR------FGrcllELGGNN 300
Cdd:cd07129 152 LVARAIRAALRATGLPAgVFSLLQGGGrEVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARpepipfYA----ELGSVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 301 ALIINEDAPQEM--ALDAAFFG-CIGTAGQRCTTTRRLI-IHAKLYDSFIAKLVKRYAsllKRVGHPLdsatLYGPVHnq 376
Cdd:cd07129 228 PVFILPGALAERgeAIAQGFVGsLTLGAGQFCTNPGLVLvPAGPAGDAFIAALAEALA---AAPAQTM----LTPGIA-- 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 158296454 377 qavDNYLQTVQEAVALGGKVECGGKVIDRAGFFVEPTI 414
Cdd:cd07129 299 ---EAYRQGVEALAAAPGVRVLAGGAAAEGGNQAAPTL 333
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
184-510 |
1.09e-17 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 85.93 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 184 PLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKgaPSTslVSVATTKIVTDVIKRNKLPPIVTLCQGGEDVGKRMVsD 263
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLK--PSE--LAPATSAFLAANIPKYLDSKAVKVIEGGPAVGEQLL-Q 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 264 ERIRLMSFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALII-NEDAPQEMA------LDAAFFGCigtAGQRCTTTRRLI 336
Cdd:PLN02203 183 HKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdSLSSSRDTKvavnriVGGKWGSC---AGQACIAIDYVL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 337 IHaklyDSFIAKLVKRYASLLKRV--GHPLDSATLYGPV--HNQQAVDNYLQ--TVQEAVALGGKvecggkvIDRAGFFV 410
Cdd:PLN02203 260 VE----ERFAPILIELLKSTIKKFfgENPRESKSMARILnkKHFQRLSNLLKdpRVAASIVHGGS-------IDEKKLFI 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 411 EPTIISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEWLGESGSdcGIVNIN----- 485
Cdd:PLN02203 329 EPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSS--GSVTFNdaiiq 406
|
330 340
....*....|....*....|....*....
gi 158296454 486 ----TSPsgaeiggaFGGEKHTGGGRESG 510
Cdd:PLN02203 407 yacdSLP--------FGGVGESGFGRYHG 427
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
184-523 |
1.30e-15 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 79.32 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 184 PLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKgaPSTslVSVATTKIVTDVIKRNKLPPIVTLCQGGEDVGKRMVSD 263
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLK--PSE--LAPASSALLAKLLEQYLDSSAVRVVEGAVTETTALLEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 264 ERIRLMsFTGSTAVGRTVGIEMQRRFGRCLLELGGNNALIINEDAPQEMALDAAFFGCIG-TAGQRCTTTRRLIIHA--- 339
Cdd:PLN02174 188 KWDKIF-YTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKeya 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 340 -KLYDSFIAKLVKRYASllkrvgHPLDSATLYGPVhNQQAVDNYLQTVQEAvALGGKVECGGKViDRAGFFVEPTIISNL 418
Cdd:PLN02174 267 pKVIDAMKKELETFYGK------NPMESKDMSRIV-NSTHFDRLSKLLDEK-EVSDKIVYGGEK-DRENLKIAPTILLDV 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 419 PHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNiQSAFEWLGESGSDCGIVNINTSPSGAEIGGAFG 498
Cdd:PLN02174 338 PLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHN-KKLKERFAATVSAGGIVVNDIAVHLALHTLPFG 416
|
330 340
....*....|....*....|....*
gi 158296454 499 GEKHTGGGRESGSDAWKQYARRSTI 523
Cdd:PLN02174 417 GVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
55-523 |
5.80e-15 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 77.44 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVAGTAGKVQSIDPASGRVIAEV-ATGseQDLERCLT----AGVAA-----YQEwkkipaplRGDVIRQIGDELRKY 124
Cdd:PRK11903 10 AGRWQAGSGAGTPLFDPVTGEELVRVsATG--LDLAAAFAfareQGGAAlraltYAQ--------RAALLAAIVKVLQAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 125 REPL--------------------GKLVALEMGKILPEGVGEVQEFVDICDYAVGLSRMFGGaifpserpQHTilekWNP 184
Cdd:PRK11903 80 RDAYydiatansgttrndsavdidGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKDPAFQG--------QHV----LVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 185 LGLVGV-ISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSLVsvaTTKIVTDVIKRNKLPP--IVTLCQGGEDVgkrMV 261
Cdd:PRK11903 148 TRGVALfINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWL---TQRMVKDVVAAGILPAgaLSVVCGSSAGL---LD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 262 SDERIRLMSFTGSTAVGRTVGIE--MQRRFGRCLLELGG-NNALIINEDAPQEMALDAAFFGCIG----TAGQRCTTTRR 334
Cdd:PRK11903 222 HLQPFDVVSFTGSAETAAVLRSHpaVVQRSVRVNVEADSlNSALLGPDAAPGSEAFDLFVKEVVRemtvKSGQKCTAIRR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 335 LIIHAKLYDSFIAKLVKRYASLlkRVGHPLDSATLYGPVHN---QQAVDNYLQTVQE--AVALGGKVECGGKVIDRAGFF 409
Cdd:PRK11903 302 IFVPEALYDAVAEALAARLAKT--TVGNPRNDGVRMGPLVSraqLAAVRAGLAALRAqaEVLFDGGGFALVDADPAVAAC 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 410 VEPTII-SNLPHDAPVV-KRETFAPIVYVFKASNLQEAISWNNEVDQGLSSSLFTNNIQSAFEWLGESGSDCGIVNINTS 487
Cdd:PRK11903 380 VGPTLLgASDPDAATAVhDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADSHGRVHVISP 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 158296454 488 PSGAEIGG--------AFGGEKHTGGGRE-SGSDAWKQYARRSTI 523
Cdd:PRK11903 460 DVAALHTGhgnvmpqsLHGGPGRAGGGEElGGLRALAFYHRRSAV 504
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
72-446 |
3.81e-13 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 71.74 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 72 ASGRVIAEVA--------TGSEQDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKilpeg 143
Cdd:cd07127 62 ASGWVGGEVSpygvelgvTYPQCDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQ----- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 144 vGEVQEF-----------VDICDYA-VGLSRMFGGAIFpsERPQ----HTILEK-WN--PLGLVGVISAFNFPCavfgWN 204
Cdd:cd07127 137 -AFMMAFqaggphaqdrgLEAVAYAwREMSRIPPTAEW--EKPQgkhdPLAMEKtFTvvPRGVALVIGCSTFPT----WN 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 205 AA----IALTVGNTVLWKGAPSTSLVSVATTKIVTDVIKRNKLPP-IVTLC--QGGEDVGKRMVSDERIRLMSFTGSTAV 277
Cdd:cd07127 210 GYpglfASLATGNPVIVKPHPAAILPLAITVQVAREVLAEAGFDPnLVTLAadTPEEPIAQTLATRPEVRIIDFTGSNAF 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 278 GRTvgIEMQRRFGRCLLELGGNNALIINE-DAPQEMALDAAFFGCIgTAGQRCTTTRRLIIHA---------KLYDSFIA 347
Cdd:cd07127 290 GDW--LEANARQAQVYTEKAGVNTVVVDStDDLKAMLRNLAFSLSL-YSGQMCTTPQNIYVPRdgiqtddgrKSFDEVAA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 348 KLVkryASLLKRVGHPLDSATLYGPVHNqqavDNYLQTVQEAVALGGkVECGGKVIDRAGF----FVEPTIISNLPHDAP 423
Cdd:cd07127 367 DLA---AAIDGLLADPARAAALLGAIQS----PDTLARIAEARQLGE-VLLASEAVAHPEFpdarVRTPLLLKLDASDEA 438
|
410 420
....*....|....*....|...
gi 158296454 424 VVKRETFAPIVYVFKASNLQEAI 446
Cdd:cd07127 439 AYAEERFGPIAFVVATDSTDHSI 461
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
55-465 |
5.23e-08 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 55.58 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 55 NGEWVaGTAGKVQSIDPASGRVIAEVATGSEQD-------LERCLTAGVAayqewKKIPAPLR----GDVIRQIGDELRK 123
Cdd:cd07126 4 AGKWK-GASNYTTLLDPLNGDKFISVPDTDEDEinefvdsLRQCPKSGLH-----NPLKNPERyllyGDVSHRVAHELRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 124 --YREPLGKLVALEMGKILPEGVGEV---QEFV-----DICDYavgLSRMFggAIFPSERPQHTILEKWnPLGLVGVISA 193
Cdd:cd07126 78 peVEDFFARLIQRVAPKSDAQALGEVvvtRKFLenfagDQVRF---LARSF--NVPGDHQGQQSSGYRW-PYGPVAIITP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 194 FNFPCAVFGWNAAIALTVGNTVLWKGapsTSLVSVATTKIVTDVIKRNKLPPIVTLCQGGEDVGKRMVSDERIRLMSFTG 273
Cdd:cd07126 152 FNFPLEIPALQLMGALFMGNKPLLKV---DSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 274 STAVGRTVGIEMQrrfGRCLLELGGNNALIINEDAPQE----MALDAAFFGCigtAGQRCTTTRRLIIHAKLYDsfiAKL 349
Cdd:cd07126 229 SSKVAERLALELH---GKVKLEDAGFDWKILGPDVSDVdyvaWQCDQDAYAC---SGQKCSAQSILFAHENWVQ---AGI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 350 VKRYASLLKRvgHPLDSATLyGPVHN------QQAVDNYLQTVQEAVALGGKVECGGKVIDRAGfFVEPTII------SN 417
Cdd:cd07126 300 LDKLKALAEQ--RKLEDLTI-GPVLTwtteriLDHVDKLLAIPGAKVLFGGKPLTNHSIPSIYG-AYEPTAVfvpleeIA 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 158296454 418 LPHDAPVVKRETFAP--IVYVFKASNLQEAISWNNEVDQGLSSSLFTNNI 465
Cdd:cd07126 376 IEENFELVTTEVFGPfqVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDI 425
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
94-503 |
2.61e-07 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 53.01 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 94 AGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALE--MG----KIL--------PEGVGEVQEFVDICDYAVG 159
Cdd:cd07121 12 AAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEEtgMGrvedKIAknhlaaekTPGTEDLTTTAWSGDNGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 160 LSRM--FG--GAIFPSERPQHTILEkwNPLGLVgvisafnfpcavfgwnAAialtvGNTVLWKGAPSTSLVSVATTKIVT 235
Cdd:cd07121 92 LVEYapFGviGAITPSTNPTETIIN--NSISML----------------AA-----GNAVVFNPHPGAKKVSAYAVELIN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 236 DVIKRNKLPP--IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVgiemqRRFGRCLLELG-GNNALIINEDAPQEM 312
Cdd:cd07121 149 KAIAEAGGPDnlVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAA-----LSSGKKAIGAGaGNPPVVVDETADIEK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 313 ALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLLkrvghpldsatlygpvHNQQAVDNYLQTVQEAVAL 392
Cdd:cd07121 224 AARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQRNGAYVL----------------NDEQAEQLLEVVLLTNKGA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 393 GGKVECGGK----VIDRAGFFVEPT---IISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVDQGL--SSSLFTN 463
Cdd:cd07121 288 TPNKKWVGKdaskILKAAGIEVPADirlIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSK 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 158296454 464 NIqsafEWLGESGSDcgivnINTS------PSGAEIGgaFGGEKHT 503
Cdd:cd07121 368 NV----ENLTKMARA-----MQTTifvkngPSYAGLG--VGGEGYT 402
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
88-499 |
5.10e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 52.27 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 88 LERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALEMGKILPEGVGEVQEFVDICDYAVGLSRMFGGA 167
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 168 IfpSERPQHTILEKWNPLGLVGVISAFNFPCAVFGWNAAIALTVGNTVLWKGAPSTSLVSVATTKIVTDVIKRNKLPP-- 245
Cdd:cd07081 81 L--TGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPEnl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 246 IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVgrtvgIEMQRRFGRCLLELG-GNNALIINEDAPQEMALDAAFFGCIGT 324
Cdd:cd07081 159 IGWIDNPSIELAQRLMKFPGIGLLLATGGPAV-----VKAAYSSGKPAIGVGaGNTPVVIDETADIKRAVQSIVKSKTFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 325 AGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLLKRvghpldsatlygpvhnqqavdNYLQTVQEAVALGGKV------EC 398
Cdd:cd07081 234 NGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTA---------------------EELQQVQPVILKNGDVnrdivgQD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 399 GGKVIDRAGF---------FVEPTIISnlphDAPVVKRETFAPIVYVFKASN----LQEAISWNNEVDQGLSSSLFTNNI 465
Cdd:cd07081 293 AYKIAAAAGLkvpqetrilIGEVTSLA----EHEPFAHEKLSPVLAMYRAANfadaDAKALALKLEGGCGHTSAMYSDNI 368
|
410 420 430
....*....|....*....|....*....|....*...
gi 158296454 466 QsAFEWLGESGSDCG----IVNINTSPSGAEIGGAFGG 499
Cdd:cd07081 369 K-AIENMNQFANAMKtsrfVKNGPCSQGGLGDLYNFRG 405
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
86-503 |
1.15e-05 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 47.97 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 86 QDLERCLTAGVAAYQEWKKIPAPLRGDVIRQIGDELRKYREPLGKLVALE--MG----KIL---------PeGVGEVQEF 150
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEEtgMGrvedKIAknvaaaektP-GVEDLTTE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 151 VDICDYAVGLSRM--FG--GAIFPSERPQHTILEkwnplglvgvisafnfpcavfgwNAAIALTVGNTVLWKGAPSTSLV 226
Cdd:PRK15398 115 ALTGDNGLTLIEYapFGviGAVTPSTNPTETIIN-----------------------NAISMLAAGNSVVFSPHPGAKKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 227 SVATTKIVTDVIKRNKLPP--IVTLCQGGEDVGKRMVSDERIRLMSFTGSTAVGRTVgiemqRRFGRCLLELG-GNNALI 303
Cdd:PRK15398 172 SLRAIELLNEAIVAAGGPEnlVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAA-----MKSGKKAIGAGaGNPPVV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 304 INEDAPQEMALDAAFFGCIGTAGQRCTTTRRLIIHAKLYDSFIAKLVKRYASLLKRvghpldsatlygpvhnQQAvdnyl 383
Cdd:PRK15398 247 VDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEKNGAVLLTA----------------EQA----- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 384 QTVQEAVALGGKV---ECGGK----VIDRAGFFVEPT---IISNLPHDAPVVKRETFAPIVYVFKASNLQEAISWNNEVD 453
Cdd:PRK15398 306 EKLQKVVLKNGGTvnkKWVGKdaakILEAAGINVPKDtrlLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLE 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158296454 454 QGL--SSSLFTNNIQ--SAFEWLgesgsdcgivnINTS------PSGAEIGgaFGGEKHT 503
Cdd:PRK15398 386 HGNrhTAIMHSRNVDnlNKMARA-----------IQTSifvkngPSYAGLG--LGGEGFT 432
|
|
| |
