|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
51-526 |
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: 858.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 51 GVYSGQWQGRGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLV 130
Cdd:cd07130 1 GVYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 131 SLEVGKIYSEGQGEVQEFIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTG 210
Cdd:cd07130 81 SLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 211 NSVLWKGAPSTPLVSVATTKIVAEVLRRNNLPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGK 289
Cdd:cd07130 161 NVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGaIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 290 VILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVG 369
Cdd:cd07130 241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQV--RIGDPLDDGTLVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 370 PVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHdASVVHRETFAPIVYILKAKNVDQAIEWNNE 449
Cdd:cd07130 319 PLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSD-APIVKEETFAPILYVLKFDTLEEAIAWNNE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24666674 450 VEQGLSSAIFTENIGQAFKWIGAKGSDCGIVNINTTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITVNHS 526
Cdd:cd07130 398 VPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
51-526 |
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: 813.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 51 GVYSGQWQGRG-PSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKL 129
Cdd:cd07086 1 GVIGGEWVGSGgETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 130 VSLEVGKIYSEGQGEVQEFIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTT 209
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 210 GNSVLWKGAPSTPLVSVATTKIVAEVLRRNNLPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFG 288
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPgVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 289 KVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLV 368
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQV--RIGDPLDEGTLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 369 GPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQR--DGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEW 446
Cdd:cd07086 319 GPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 447 NNEVEQGLSSAIFTENIGQAFKWIGAKGSDCGIVNINTTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITVNHS 526
Cdd:cd07086 399 NNDVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
34-538 |
0e+00 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 622.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 34 QPEYSFLKELGLERDNPGVY-SGQWQGRGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIV 112
Cdd:PLN02315 5 RKEYEFLSEIGLSSRNLGCYvGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 113 RQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQEFIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAY 192
Cdd:PLN02315 85 RQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 193 NFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVSVATTKIVAEVLRRNNLPPVVTLCQ-GGTDVGQTLVADKRVNLVSFTG 271
Cdd:PLN02315 165 NFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFcGGAEIGEAIAKDTRIPLVSFTG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 272 SCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKY 351
Cdd:PLN02315 245 SSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 352 KQLisKIGHQLEAQTLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITgLPHDASVVHRETFAPI 431
Cdd:PLN02315 325 KQV--KIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 432 VYILKAKNVDQAIEWNNEVEQGLSSAIFTENIGQAFKWIGAKGSDCGIVNINTTTNGAEIGGAFGGEKATGGGRESGSDA 511
Cdd:PLN02315 402 LYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDS 481
|
490 500
....*....|....*....|....*..
gi 24666674 512 WKQYCKRATITVNHSGELACAQGVVFN 538
Cdd:PLN02315 482 WKQYMRRSTCTINYGNELPLAQGINFG 508
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
59-521 |
3.55e-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: 461.23 E-value: 3.55e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 59 GRGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIY 138
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 139 SEGQGEVQEFIDICDYAVGLSRIYSGQLINSeRADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGA 218
Cdd:pfam00171 84 AEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 219 PSTPLVSVATTKIVAEVlrrnNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGG 296
Cdd:pfam00171 163 ELTPLTALLLAELFEEA----GLPAgVLNVVTGsGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 297 NNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQN 376
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKL--KVGDPLDPDTDMGPLISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 377 VENYKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSS 456
Cdd:pfam00171 317 LERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666674 457 AIFTENIGQAFKWigAKGSDCGIVNINTTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATI 521
Cdd:pfam00171 397 GVFTSDLERALRV--ARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
55-525 |
8.21e-156 |
|
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: 453.43 E-value: 8.21e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQWQ--GRGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSL 132
Cdd:COG1012 12 GEWVaaASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 133 EVGKIYSEGQGEVQEFIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNS 212
Cdd:COG1012 92 ETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 213 VLWKGAPSTPLVSVAttkiVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKV 290
Cdd:COG1012 172 VVLKPAEQTPLSALL----LAELLEEAGLPAgVLNVVTGdGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 291 ILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGP 370
Cdd:COG1012 248 TLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKAL--KVGDPLDPGTDMGP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 371 VHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQR-DGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNE 449
Cdd:COG1012 326 LISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALAND 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24666674 450 VEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINTTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITVNH 525
Cdd:COG1012 406 TEYGLAASVFTRDLARARRV--ARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
93-523 |
2.44e-142 |
|
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: 417.38 E-value: 2.44e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 93 AVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQEFIDICDYAVGLSRIYSGQLINSERA 172
Cdd:cd07078 7 ARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 173 DHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVSVATTKIVAEVLrrnnLPP-VVTLCQG- 250
Cdd:cd07078 87 GELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAG----LPPgVLNVVTGd 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 251 GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTT 330
Cdd:cd07078 163 GDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 331 RRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRD-GFYVE 409
Cdd:cd07078 243 SRLLVHESIYDEFVERLVERVKAL--KVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGkGYFVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 410 PTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINTTTNGA 489
Cdd:cd07078 321 PTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRV--AERLEAGTVWINDYSVGA 398
|
410 420 430
....*....|....*....|....*....|....
gi 24666674 490 EIGGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07078 399 EPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
55-526 |
1.50e-130 |
|
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: 389.01 E-value: 1.50e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQWQGRGPSVT--SYDPGTGQP-IAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVS 131
Cdd:cd07131 5 GEWVDSASGETfdSRNPADLEEvVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 132 LEVGKIYSEGQGEVQEFIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGN 211
Cdd:cd07131 85 REMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 212 SVLWKGAPSTPLvsvATTKIVaEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGK 289
Cdd:cd07131 165 TVVFKPAEDTPA---CALKLV-ELFAEAGLPPgVVNVVHGrGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 290 VILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVG 369
Cdd:cd07131 241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRL--RVGDGLDEETDMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 370 PVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRD----GFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIE 445
Cdd:cd07131 319 PLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGgyekGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 446 WNNEVEQGLSSAIFTENIGQAFKWIGAkgSDCGIVNINTTTNGAEIGGAFGGEKATGGG-RESGSDAWKQYCKRATITVN 524
Cdd:cd07131 399 IANDTEYGLSSAIYTEDVNKAFRARRD--LEAGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYVD 476
|
..
gi 24666674 525 HS 526
Cdd:cd07131 477 YS 478
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
50-511 |
1.58e-123 |
|
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: 370.81 E-value: 1.58e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 50 PGVYSGQWQGRGPSVTSYDPG-TGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGK 128
Cdd:cd07097 2 RNYIDGEWVAGGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 129 LVSLEVGKIYSEGQGEVQEFIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALT 208
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 209 TGNSVLWKGAPSTPLVSVAttkiVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRR 286
Cdd:cd07097 162 YGNTVVFKPAELTPASAWA----LVEILEEAGLPAgVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 287 FGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQT 366
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKAL--KVGDALDEGV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 367 LVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRD--GFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAI 444
Cdd:cd07097 316 DIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEAL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24666674 445 EWNNEVEQGLSSAIFTENIGQAFKWIgaKGSDCGIVNINTTTNGAEIGGAFGGEKATG-GGRESGSDA 511
Cdd:cd07097 396 AIANDTEFGLSAGIVTTSLKHATHFK--RRVEAGVVMVNLPTAGVDYHVPFGGRKGSSyGPREQGEAA 461
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
93-523 |
1.32e-110 |
|
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: 333.81 E-value: 1.32e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 93 AVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQEFIDICDYAVGLSRIYSGQLINSERA 172
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 173 DHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVSVATTKIVAEVLrrnnLPP--VVTLCQG 250
Cdd:cd06534 83 GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAG----LPPgvVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 251 GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTT 330
Cdd:cd06534 159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 331 RRIIVHEKLHDQFVKELVgkykqliskighqleaqtlvgpvhtqqnvenykaaiaeakslggtvafggnviqrdgfyvep 410
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV-------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 411 TVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINTTTNGAE 490
Cdd:cd06534 257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRV--AERLRAGTVYINDSSIGVG 334
|
410 420 430
....*....|....*....|....*....|...
gi 24666674 491 IGGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd06534 335 PEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
93-523 |
8.88e-103 |
|
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: 316.01 E-value: 8.88e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 93 AVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQEFIDICDYAVGLSRIYSGQLINSERA 172
Cdd:cd07104 9 AAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILPSDVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 173 DHSILEAWRPLGVVGVISAYNFPnAVFGWNA-AIALTTGNSVLWKGAPSTPlvsVATTKIVAEVLRRNNLPP----VVTl 247
Cdd:cd07104 89 GKESMVRRVPLGVVGVISPFNFP-LILAMRSvAPALALGNAVVLKPDSRTP---VTGGLLIAEIFEEAGLPKgvlnVVP- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 248 cQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRC 327
Cdd:cd07104 164 -GGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQIC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 328 TTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGnviQRDGFY 407
Cdd:cd07104 243 MAAGRILVHESVYDEFVEKLVAKAKAL--PVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGG---TYEGLF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 408 VEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINTTTN 487
Cdd:cd07104 318 YQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAF--AERLETGMVHINDQTV 395
|
410 420 430
....*....|....*....|....*....|....*.
gi 24666674 488 GAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07104 396 NDEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
65-523 |
4.63e-101 |
|
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: 312.34 E-value: 4.63e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 65 TSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGE 144
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 145 VQEFIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPnAVFGWNA-AIALTTGNSVLWKGAPSTPL 223
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYP-LILATKKvAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 224 VSVattkIVAEVLRRNNLPP----VVTlcQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNA 299
Cdd:cd07150 161 IGL----KIAEIMEEAGLPKgvfnVVT--GGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 300 LIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVEN 379
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKL--KVGDPRDPDTVIGPLISPRQVER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 380 YKAAIAEAKSLGGTVAFGGnviQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIF 459
Cdd:cd07150 313 IKRQVEDAVAKGAKLLTGG---KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAIL 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24666674 460 TENIGQAFKWigAKGSDCGIVNINTTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07150 390 TNDLQRAFKL--AERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
67-511 |
2.05e-100 |
|
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: 310.52 E-value: 2.05e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 67 YDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVq 146
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 147 efidicDYAVGL--------SRIYsGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGA 218
Cdd:cd07103 81 ------DYAASFlewfaeeaRRIY-GRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 219 PSTPLVSVAttkiVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGG 296
Cdd:cd07103 154 EETPLSALA----LAELAEEAGLPAgVLNVVTGsPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 297 NNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQN 376
Cdd:cd07103 230 NAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKL--KVGNGLDEGTDMGPLINERA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 377 VENYKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSS 456
Cdd:cd07103 308 VEKVEALVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 24666674 457 AIFTENIGQAFKWigAKGSDCGIVNINTTTngaeIGGA---FGGEKATGGGRESGSDA 511
Cdd:cd07103 388 YVFTRDLARAWRV--AEALEAGMVGINTGL----ISDAeapFGGVKESGLGREGGKEG 439
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
41-524 |
1.70e-97 |
|
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: 304.92 E-value: 1.70e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 41 KELGleRDNPGVYSGQWQGRGPSVTSYDPG-TGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDEL 119
Cdd:cd07124 27 EELG--REYPLVIGGKEVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 120 RKYKEPLGKLVSLEVGKIYSEGQGEVQEFIDICDYAVGLSRIYSGQLINSERADHSILeAWRPLGVVGVISAYNFPNAVF 199
Cdd:cd07124 105 RRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRY-VYRPLGVGAVISPWNFPLAIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 200 GWNAAIALTTGNSVLWKGAPSTPLVSvattKIVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGScqtgR 277
Cdd:cd07124 184 AGMTTAALVTGNTVVLKPAEDTPVIA----AKLVEILEEAGLPPgVVNFLPGpGEEVGDYLVEHPDVRFIAFTGS----R 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 278 DVGVEVQRRFGK----------VILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKEL 347
Cdd:cd07124 256 EVGLRIYERAAKvqpgqkwlkrVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 348 VGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYKAAIAEAKSlGGTVAFGGNVI--QRDGFYVEPTVITGLPHDASVVHR 425
Cdd:cd07124 336 VERTKAL--KVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKS-EGRLLLGGEVLelAAEGYFVQPTIFADVPPDHRLAQE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 426 ETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFT---ENIGQAFKWIgakgsDCGIVNINTTTNGAEIG-GAFGGEKAT 501
Cdd:cd07124 413 EIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSrspEHLERARREF-----EVGNLYANRKITGALVGrQPFGGFKMS 487
|
490 500
....*....|....*....|....
gi 24666674 502 G-GGRESGSDAWKQYCKRATITVN 524
Cdd:cd07124 488 GtGSKAGGPDYLLQFMQPKTVTEN 511
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
61-521 |
2.75e-96 |
|
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: 300.34 E-value: 2.75e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 61 GPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSE 140
Cdd:cd07088 12 GETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 141 GQGEVQEFIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPS 220
Cdd:cd07088 92 ARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 221 TPLVSVATTKIVAEVlrrnNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNN 298
Cdd:cd07088 172 TPLNALEFAELVDEA----GLPAgVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 299 ALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVE 378
Cdd:cd07088 248 PAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAV--KVGDPFDAATDMGPLVNEAALD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 379 NYKAAIAEAKSLGGTVAFGGNVIQRD-GFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSA 457
Cdd:cd07088 326 KVEEMVERAVEAGATLLTGGKRPEGEkGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSY 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24666674 458 IFTENIGQAFKwiGAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATI 521
Cdd:cd07088 406 IYTENLNTAMR--ATNELEFGETYIN-RENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
67-523 |
9.60e-95 |
|
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: 295.59 E-value: 9.60e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 67 YDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQ 146
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 147 EFIDICDYAVGLSRIysgQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVSV 226
Cdd:cd07106 82 GAVAWLRYTASLDLP---DEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 227 ATTKIVAEVLrrnnlPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDES 305
Cdd:cd07106 159 KLGELAQEVL-----PPgVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 306 ANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYKAAIA 385
Cdd:cd07106 234 VDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAA--VVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 386 EAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENIGQ 465
Cdd:cd07106 312 DAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 24666674 466 AFKWigAKGSDCGIVNINTTTNgAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07106 392 AEAV--ARRLEAGTVWINTHGA-LDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
67-506 |
1.51e-92 |
|
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: 290.27 E-value: 1.51e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 67 YDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQ 146
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 147 EFIDICDYAVGLSRIYSGQLIN---SERADHSILEAWR-PLGVVGVISAYNFP-NAVfgwnA---AIALTTGNSVLWKGA 218
Cdd:cd07149 84 RAIETLRLSAEEAKRLAGETIPfdaSPGGEGRIGFTIRePIGVVAAITPFNFPlNLV----AhkvGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 219 PSTPLVSVAttkiVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRdvgvEVQRRFG--KVILEL 294
Cdd:cd07149 160 SQTPLSALK----LAELLLEAGLPKgALNVVTGsGETVGDALVTDPRVRMISFTGSPAVGE----AIARKAGlkKVTLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 295 GGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQ 374
Cdd:cd07149 232 GSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKL--VVGDPLDEDTDVGPMISE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 375 QNVENYKAAIAEAKSLGGTVAFGGnviQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGL 454
Cdd:cd07149 310 AEAERIEEWVEEAVEGGARLLTGG---KRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGL 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 24666674 455 SSAIFTENIGQAFKwiGAKGSDCGIVNINTTTNGAEIGGAFGGEKATGGGRE 506
Cdd:cd07149 387 QAGVFTNDLQKALK--AARELEVGGVMINDSSTFRVDHMPYGGVKESGTGRE 436
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
64-523 |
1.22e-91 |
|
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: 288.09 E-value: 1.22e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 64 VTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQG 143
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 144 EVQEFIDICDYAVGLSRIYSGQLINSERADHS----ILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAP 219
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAYEYNerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 220 STPLVSVATTKIVAEVlrrnNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGN 297
Cdd:cd07145 161 NTPLTAIELAKILEEA----GLPPgVINVVTGyGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 298 NALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNV 377
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKL--KVGDPLDESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 378 ENYKAAIAEAKSLGGTVAFGGNVIQrdGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSA 457
Cdd:cd07145 315 ERMENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24666674 458 IFTENIGQAFKWigAKGSDCGIVNINTTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07145 393 VFTNDINRALKV--ARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
66-523 |
1.03e-90 |
|
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: 285.60 E-value: 1.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 66 SYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQ--WRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQG 143
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 144 EVQEFIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPL 223
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 224 VSVATTKIVAEVlrrnNLPP----VVTlcQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNA 299
Cdd:cd07114 161 STLELAKLAEEA----GFPPgvvnVVT--GFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 300 LIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVEN 379
Cdd:cd07114 235 NIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAI--RVGDPLDPETQMGPLATERQLEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 380 YKAAIAEAKSLGGTVAFGGNVIQ----RDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLS 455
Cdd:cd07114 313 VERYVARAREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24666674 456 SAIFTENIGQAFKWigAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07114 393 AGIWTRDLARAHRV--ARAIEAGTVWVN-TYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
67-524 |
2.14e-87 |
|
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: 276.88 E-value: 2.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 67 YDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQ 146
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 147 EFIDICDYAVGLSRIYSGQLInsERADHSILEAWR-PLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVS 225
Cdd:cd07090 82 SSADCLEYYAGLAPTLSGEHV--PLPGGSFAYTRRePLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 226 VattkIVAEVLRRNNLPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDE 304
Cdd:cd07090 160 L----LLAEILTEAGLPDgVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 305 SANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYKAAI 384
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKI--RIGDPLDEDTQMGALISEEHLEKVLGYI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 385 AEAKSLGGTVAFGGNVIQ-----RDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIF 459
Cdd:cd07090 314 ESAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVF 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666674 460 TENIGQAFKWIGAKgsDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITVN 524
Cdd:cd07090 394 TRDLQRAHRVIAQL--QAGTCWIN-TYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVE 455
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
66-523 |
3.20e-86 |
|
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: 274.06 E-value: 3.20e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 66 SYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEV 145
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 146 -----QEFIDICDYAVGLSriysGQLINSERaDHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPS 220
Cdd:cd07093 81 ipraaANFRFFADYILQLD----GESYPQDG-GALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 221 TPLvsvaTTKIVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNN 298
Cdd:cd07093 156 TPL----TAWLLAELANEAGLPPgVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 299 ALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVE 378
Cdd:cd07093 232 PNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKAL--KVGDPLDPDTEVGPLISKEHLE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 379 NYKAAIAEAKSLGGTVAFGGNV----IQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGL 454
Cdd:cd07093 310 KVLGYVELARAEGATILTGGGRpelpDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGL 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666674 455 SSAIFTENIGQAFKWigAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07093 390 AAYVWTRDLGRAHRV--ARRLEAGTVWVN-CWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
67-523 |
5.46e-86 |
|
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: 273.33 E-value: 5.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 67 YDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQ 146
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 147 EFIDICDYAVGLSriysGQLINSERADHSILEAW-------RPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAP 219
Cdd:cd07099 81 LALEAIDWAARNA----PRVLAPRKVPTGLLMPNkkatveyRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 220 STPLVSVATTKIVAEVlrrNNLPPVVTLCQGGTDVGQTLVaDKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNA 299
Cdd:cd07099 157 VTPLVGELLAEAWAAA---GPPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 300 LIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVEN 379
Cdd:cd07099 233 MIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARAL--RPGADDIGDADIGPMTTARQLDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 380 YKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIF 459
Cdd:cd07099 311 VRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666674 460 TENIGQAfkWIGAKGSDCGIVNIN-TTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07099 391 SRDLARA--EAIARRLEAGAVSINdVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
86-506 |
1.68e-85 |
|
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: 271.26 E-value: 1.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 86 LEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQEFIDICD-YAVGLSRIYSG 164
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRyYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 165 QLINSErADHSILEaWRPLGVVGVISAYNFP-NAVFGWnAAIALTTGNSVLWKGAPSTPLVSVAttkiVAEVLRRNNLPP 243
Cdd:cd07100 81 EPIETD-AGKAYVR-YEPLGVVLGIMPWNFPfWQVFRF-AAPNLMAGNTVLLKHASNVPGCALA----IEELFREAGFPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 244 --VVTLCQGGTDVGQtLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIG 321
Cdd:cd07100 154 gvFQNLLIDSDQVEA-IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 322 TSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVI 401
Cdd:cd07100 233 NAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAAL--KVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 402 QRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVN 481
Cdd:cd07100 311 DGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERV--ARRLEAGMVF 388
|
410 420
....*....|....*....|....*.
gi 24666674 482 INT-TTNGAEIggAFGGEKATGGGRE 506
Cdd:cd07100 389 INGmVKSDPRL--PFGGVKRSGYGRE 412
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
68-524 |
9.70e-84 |
|
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: 267.38 E-value: 9.70e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 68 DPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQG-EVQ 146
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 147 EFIDICDYAVGLSRIYSGQLI--NSERADHSILEawrPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLV 224
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIpvRGPFLNYTVRE---PVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 225 SVATTKIVAEVlrrnNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALII 302
Cdd:cd07115 160 ALRIAELMAEA----GFPAgVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 303 DESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYKA 382
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSL--RPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 383 AIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTEN 462
Cdd:cd07115 314 YVDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24666674 463 IGQAFKWigAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITVN 524
Cdd:cd07115 394 LGRAHRV--AAALKAGTVWIN-TYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVN 452
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
72-523 |
2.91e-82 |
|
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: 263.39 E-value: 2.91e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 72 GQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQEFIDI 151
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 152 CDYAVGLSRIYSGQLINSERADHSIleAWR-PLGVVGVISAYNFPnAVFGWNA-AIALTTGNSVLWKGAPSTPlvsVATT 229
Cdd:cd07152 81 LHEAAGLPTQPQGEILPSAPGRLSL--ARRvPLGVVGVISPFNFP-LILAMRSvAPALALGNAVVLKPDPRTP---VSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 230 KIVAEVLRRNNLPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANV 308
Cdd:cd07152 155 VVIARLFEEAGLPAgVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 309 KMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYKAAIAEAK 388
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHL--PVGDPATGQVALGPLINARQLDRVHAIVDDSV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 389 SLGGTVAFGGnviQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENIGQAFK 468
Cdd:cd07152 313 AAGARLEAGG---TYDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMA 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 24666674 469 wIGAKgSDCGIVNINTTTNGAEIGGAFGGEKATG-GGRESGSDAWKQYCKRATITV 523
Cdd:cd07152 390 -LADR-LRTGMLHINDQTVNDEPHNPFGGMGASGnGSRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
55-525 |
9.43e-82 |
|
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: 262.63 E-value: 9.43e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQWQ--GRGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSL 132
Cdd:cd07151 1 GEWRdgTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 133 EVGKIYSEGQGEVQEFIDICDYAVGLSRIYSGQLINS--ERADHSILEAwrPLGVVGVISAYNFPNAVFGWNAAIALTTG 210
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSdvPGKENRVYRE--PLGVVGVISPWNFPLHLSMRSVAPALALG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 211 NSVLWKGAPSTPLVSvatTKIVAEVLRRNNLPP-----VVTlcqGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQR 285
Cdd:cd07151 159 NAVVLKPASDTPITG---GLLLAKIFEEAGLPKgvlnvVVG---AGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 286 RFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQ 365
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKAL--PYGDPSDPD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 366 TLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGnviQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIE 445
Cdd:cd07151 311 TVVGPLINESQVDGLLDKIEQAVEEGATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 446 WNNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINTTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITVNH 525
Cdd:cd07151 388 LANDTEYGLSGAVFTSDLERGVQF--ARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQH 465
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
68-523 |
2.01e-80 |
|
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: 258.90 E-value: 2.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 68 DPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQE 147
Cdd:cd07094 5 NPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 148 FIDICDYAVGLSRIYSGQLI----NSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPL 223
Cdd:cd07094 85 AIDTLRLAAEEAERIRGEEIpldaTQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 224 VSVattkIVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVgvEVQRRFGKVILELGGNNALI 301
Cdd:cd07094 165 SAL----ELAKILVEAGVPEgVLQVVTGeREVLGDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 302 IDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYK 381
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKL--KVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 382 AAIAEAKSLGGTVAFGGnviQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTE 461
Cdd:cd07094 317 RWVEEAVEAGARLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24666674 462 NIGQAFKwiGAKGSDCGIVNINTTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07094 394 DLNVAFK--AAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
55-515 |
5.44e-80 |
|
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: 258.40 E-value: 5.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQWQ--GRGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQ--WRQVPAPVRGEIVRQIGDELRKYKEPLGKLV 130
Cdd:cd07119 4 GEWVeaASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 131 SLEVGKIYSEGQGEVQEFIDICDYAVGLSRIYSGQLInsERADHSILEAWR-PLGVVGVISAYNFPNAVFGWNAAIALTT 209
Cdd:cd07119 84 TLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVY--DVPPHVISRTVRePVGVCGLITPWNYPLLQAAWKLAPALAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 210 GNSVLWKGAPSTPLVSVATTKIVAEVlrrnNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRF 287
Cdd:cd07119 162 GNTVVIKPSEVTPLTTIALFELIEEA----GLPAgVVNLVTGsGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 288 GKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTL 367
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKI--KLGNGLDADTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 368 VGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRD----GFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQA 443
Cdd:cd07119 316 MGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666674 444 IEWNNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINT---TTNGAEiggaFGGEKATGGGRESGSDAWKQY 515
Cdd:cd07119 396 IRLANDTPYGLAGAVWTKDIARANRV--ARRLRAGTVWINDyhpYFAEAP----WGGYKQSGIGRELGPTGLEEY 464
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
68-524 |
1.99e-78 |
|
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: 253.84 E-value: 1.99e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 68 DPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQE 147
Cdd:cd07107 3 NPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 148 FIDICDYAVGLSRIYSGQLI-NSERADH-SILEawrPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVS 225
Cdd:cd07107 83 AAALLDYFAGLVTELKGETIpVGGRNLHyTLRE---PYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 226 VATTKIVAEVlrrnnLPPVV--TLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIID 303
Cdd:cd07107 160 LRLAELAREV-----LPPGVfnILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 304 ESANVKMALDAALFGC-IGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYKA 382
Cdd:cd07107 235 PDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAI--KVGDPTDPATTMGPLVSRQQYDRVMH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 383 AIAEAKSLGGTVAFGG----NVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAI 458
Cdd:cd07107 313 YIDSAKREGARLVTGGgrpeGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAI 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24666674 459 FTENIGQAFKwiGAKGSDCGIVNINTTTNGAeIGGAFGGEKATGGGRESGSDAWKQYCKRATITVN 524
Cdd:cd07107 393 WTNDISQAHR--TARRVEAGYVWINGSSRHF-LGAPFGGVKNSGIGREECLEELLSYTQEKNVNVR 455
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
64-506 |
2.49e-78 |
|
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: 253.32 E-value: 2.49e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 64 VTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQG 143
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 144 EVQEFIDICDYAVGLSRIYSGQLIN---SERADHSILEAWR-PLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAP 219
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldiSARGEGRQGLVRRfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 220 STPLVSVattkIVAEVLRRNNLPP----VVTLcqgGTDVGQTLVADKRVNLVSFTGScqtgRDVGVEVQRRFGK--VILE 293
Cdd:cd07147 161 RTPLSAL----ILGEVLAETGLPKgafsVLPC---SRDDADLLVTDERIKLLSFTGS----PAVGWDLKARAGKkkVVLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 294 LGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHT 373
Cdd:cd07147 230 LGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKAL--KTGDPKDDATDVGPMIS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 374 QQNVENYKAAIAEAKSLGGTVAFGGnviQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQG 453
Cdd:cd07147 308 ESEAERVEGWVNEAVDAGAKLLTGG---KRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFG 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 24666674 454 LSSAIFTENIGQAFKwiGAKGSDCGIVNINTTTNGAEIGGAFGGEKATGGGRE 506
Cdd:cd07147 385 LQAGVFTRDLEKALR--AWDELEVGGVVINDVPTFRVDHMPYGGVKDSGIGRE 435
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
67-506 |
3.16e-77 |
|
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: 250.32 E-value: 3.16e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 67 YDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEG-QGEV 145
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVrDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 146 QEFIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVS 225
Cdd:cd07092 82 PGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 226 VATTKIVAEVLrrnnlPPVV--TLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIID 303
Cdd:cd07092 162 LLLAELAAEVL-----PPGVvnVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 304 ESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYKAA 383
Cdd:cd07092 237 DDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAI--RVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 384 IAEAKSlGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENI 463
Cdd:cd07092 315 VERAPA-HARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDV 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 24666674 464 GQAFKWigAKGSDCGIVNINT-TTNGAEIggAFGGEKATGGGRE 506
Cdd:cd07092 394 GRAMRL--SARLDFGTVWVNThIPLAAEM--PHGGFKQSGYGKD 433
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
68-523 |
5.07e-77 |
|
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: 249.97 E-value: 5.07e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 68 DPGTGQPIAKVRQGNVQELEHTIGLAveaYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQE 147
Cdd:cd07146 5 NPYTGEVVGTVPAGTEEALREALALA---ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 148 FIDICDYAVGLSRIYSGQLINSERADHS----ILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPL 223
Cdd:cd07146 82 AADVLRFAAAEALRDDGESFSCDLTANGkarkIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 224 VSVAttkiVAEVLRRNNLPP-VVTLCQGG-TDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRfgKVILELGGNNALI 301
Cdd:cd07146 162 SAIY----LADLLYEAGLPPdMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--RQLLELGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 302 IDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYK 381
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAAL--VVGDPMDPATDMGTVIDEEAAIQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 382 AAIAEAKSLGGTVAFGGnviQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTE 461
Cdd:cd07146 314 NRVEEAIAQGARVLLGN---QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTN 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666674 462 NIGQAFKWIgaKGSDCGIVNINtttngaEIGG------AFGGEKATG-GGRESGSDAWKQYCKRATITV 523
Cdd:cd07146 391 DLDTIKRLV--ERLDVGTVNVN------EVPGfrselsPFGGVKDSGlGGKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
69-523 |
1.37e-76 |
|
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: 248.79 E-value: 1.37e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 69 PGTGQPIAKVRQGNVQELEHTIGLAVEAYKQ--WRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQ 146
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 147 EFIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPlvsv 226
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 227 ATTKIVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDE 304
Cdd:cd07118 160 GTTLMLAELLIEAGLPAgVVNIVTGyGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 305 SANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYKAAI 384
Cdd:cd07118 240 DADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKV--RVGDPLDPETKVGAIINEAQLAKITDYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 385 AEAKSLGGTVAFGGNVI-QRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENI 463
Cdd:cd07118 318 DAGRAEGATLLLGGERLaSAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24666674 464 GQAFKwiGAKGSDCGIVNINTTTNG-AEIggAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07118 398 DTALT--VARRIRAGTVWVNTFLDGsPEL--PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
66-523 |
6.86e-76 |
|
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: 247.15 E-value: 6.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 66 SYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQ-WRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGE 144
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 145 VQEFIDICDYAVGLSRIYSGQLINSER--ADHSILEawrPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTP 222
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLGPgyFVYTVRE---PHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 223 LVSVAttkiVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNAL 300
Cdd:cd07109 158 LTALR----LAELAEEAGLPAgALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 301 IIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEaQTLVGPVHTQQNVENY 380
Cdd:cd07109 234 IVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRAL--RVGPGLE-DPDLGPLISAKQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 381 KAAIAEAKSLGGTVAFGGNVIQ---RDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSA 457
Cdd:cd07109 311 EGFVARARARGARIVAGGRIAEgapAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAG 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24666674 458 IFTENIGQAFkWIgAKGSDCGIVNINTTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07109 391 VWTRDGDRAL-RV-ARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
40-515 |
1.15e-75 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 247.68 E-value: 1.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 40 LKELGLERDNpGVYSGQWQGRGPSVT--SYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGD 117
Cdd:PLN02278 17 LRNAGLLRTQ-GLIGGKWTDAYDGKTfpVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 118 ELRKYKEPLGKLVSLEVGKIYSEGQGEVQ---EFIDIcdYAVGLSRIYsGQLINSERADHSILEAWRPLGVVGVISAYNF 194
Cdd:PLN02278 96 LIIANKEDLAQLMTLEQGKPLKEAIGEVAygaSFLEY--FAEEAKRVY-GDIIPSPFPDRRLLVLKQPVGVVGAITPWNF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 195 PNAVFGWNAAIALTTGNSVLWKGAPSTPLVSVAttkiVAEVLRRNNLPP-VVTLCQGGT-DVGQTLVADKRVNLVSFTGS 272
Cdd:PLN02278 173 PLAMITRKVGPALAAGCTVVVKPSELTPLTALA----AAELALQAGIPPgVLNVVMGDApEIGDALLASPKVRKITFTGS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 273 CQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYK 352
Cdd:PLN02278 249 TAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 353 QLisKIGHQLEAQTLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIV 432
Cdd:PLN02278 329 KL--VVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 433 YILKAKNVDQAIEWNNEVEQGLSSAIFTENIGQAfkWIGAKGSDCGIVNINTTTNGAEIgGAFGGEKATGGGRESGSDAW 512
Cdd:PLN02278 407 PLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRA--WRVSEALEYGIVGVNEGLISTEV-APFGGVKQSGLGREGSKYGI 483
|
...
gi 24666674 513 KQY 515
Cdd:PLN02278 484 DEY 486
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
68-523 |
2.19e-74 |
|
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: 243.04 E-value: 2.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 68 DPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGK-IYSEGQGEVQ 146
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNaLRTQARPEAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 147 EFIDICDYAVGLSRIYSGQLI--NSERADHSILEawrPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLV 224
Cdd:cd07108 83 VLADLFRYFGGLAGELKGETLpfGPDVLTYTVRE---PLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 225 SVATTKIVAEVLrrnnlPPVV--TLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALII 302
Cdd:cd07108 160 VLLLAEILAQVL-----PAGVlnVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 303 DESANVKMALDAALFGCIGT-SGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYK 381
Cdd:cd07108 235 FPDADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKL--KIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 382 AAIAEAKSL-GGTVAFGGN----VIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSS 456
Cdd:cd07108 313 GYIDLGLSTsGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24666674 457 AIFTENIGQAFKwiGAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGSDAW-KQYCKRATITV 523
Cdd:cd07108 393 YVWTRDLGRALR--AAHALEAGWVQVN-QGGGQQPGQSYGGFKQSGLGREASLEGMlEHFTQKKTVNI 457
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
67-483 |
7.81e-74 |
|
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: 241.38 E-value: 7.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 67 YDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQ 146
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 147 EFIDICDYavgLSRIYSGQLINSERADHSILE---AWRPLGVVGVISAYNFPNAVfGWNAAI-ALTTGNSVLWKGAPSTP 222
Cdd:cd07102 81 GMLERARY---MISIAEEALADIRVPEKDGFEryiRREPLGVVLIIAPWNYPYLT-AVNAVIpALLAGNAVILKHSPQTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 223 LVSVATTKIVAEVLrrnnLPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALI 301
Cdd:cd07102 157 LCGERFAAAFAEAG----LPEgVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 302 IDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYK 381
Cdd:cd07102 233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGY--KLGDPLDPSTTLGPVVSARAADFVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 382 AAIAEAKSLGGTVAFGGNVIQRD---GFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAI 458
Cdd:cd07102 311 AQIADAIAKGARALIDGALFPEDkagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASV 390
|
410 420
....*....|....*....|....*
gi 24666674 459 FTENIgQAFKWIGAKgSDCGIVNIN 483
Cdd:cd07102 391 WTKDI-ARAEALGEQ-LETGTVFMN 413
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
67-521 |
3.60e-73 |
|
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: 239.84 E-value: 3.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 67 YDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQW-RQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGK-IYSEGQGE 144
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGApVMTARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 145 VQEFIDICDYAVGLSRIYSGQLINSERADHSILE---AWR-PLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPS 220
Cdd:cd07089 82 VDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGrrvVRRePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 221 TPLVSVATTKIVAEVlrrnNLPP----VVTlcQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGG 296
Cdd:cd07089 162 TPLSALLLGEIIAET----DLPAgvvnVVT--GSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 297 NNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPV--HTQ 374
Cdd:cd07089 236 KSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEAL--PVGDPADPGTVMGPLisAAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 375 QN-VENYkaaIAEAKSLGGTVAFGGNVIQR--DGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVE 451
Cdd:cd07089 314 RDrVEGY---IARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 452 QGLSSAIFTENIGQAFKWigAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATI 521
Cdd:cd07089 391 YGLSGGVWSADVDRAYRV--ARRIRTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
38-524 |
3.97e-73 |
|
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: 240.77 E-value: 3.97e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 38 SFLKELGLERDNPGVYS-GQWQgrgpsVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQ-WRQVPAPVRGEIVRQI 115
Cdd:cd07144 3 SYDQPTGLFINNEFVKSsDGET-----IKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 116 GDELRKYKEPLGKLVSLEVGKIY-SEGQGEVQEFIDICDYAVGLSRIYSGQLINSERADHS-ILEawRPLGVVGVISAYN 193
Cdd:cd07144 78 ADLVEKNRDLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAyTLH--EPYGVCGQIIPWN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 194 FPNAVFGWNAAIALTTGNSVLWKGAPSTPLvsvaTTKIVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTG 271
Cdd:cd07144 156 YPLAMAAWKLAPALAAGNTVVIKPAENTPL----SLLYFANLVKEAGFPPgVVNIIPGyGAVAGSALAEHPDVDKIAFTG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 272 SCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKY 351
Cdd:cd07144 232 STATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 352 KQlISKIGHQLEAQTLVGPV--HTQQN-VENYkaaIAEAKSLGGTVAFGGNVIQRD---GFYVEPTVITGLPHDASVVHR 425
Cdd:cd07144 312 KQ-NYKVGSPFDDDTVVGPQvsKTQYDrVLSY---IEKGKKEGAKLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 426 ETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGR 505
Cdd:cd07144 388 EIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRV--ARELEAGMVWIN-SSNDSDVGVPFGGFKMSGIGR 464
|
490
....*....|....*....
gi 24666674 506 ESGSDAWKQYCKRATITVN 524
Cdd:cd07144 465 ELGEYGLETYTQTKAVHIN 483
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
61-523 |
1.46e-72 |
|
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: 239.03 E-value: 1.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 61 GPSVTSYDPGTGQPIAKVRQGNVQELEhtigLAVEAYKQ------WRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEV 134
Cdd:cd07091 18 GKTFPTINPATEEVICQVAEADEEDVD----AAVKAARAafetgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 135 GKIYSEG-QGEVQEFIDICDYAVGLSRIYSGQLINSERADHS--ILEawrPLGVVGVISAYNFPNAVFGWNAAIALTTGN 211
Cdd:cd07091 94 GKPLEESaKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAytRRE---PIGVCGQIIPWNFPLLMLAWKLAPALAAGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 212 SVLWKGAPSTPLvsvaTTKIVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEV-QRRFG 288
Cdd:cd07091 171 TVVLKPAEQTPL----SALYLAELIKEAGFPPgVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAaKSNLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 289 KVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLV 368
Cdd:cd07091 247 KVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKR--VVGDPFDPDTFQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 369 GPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNN 448
Cdd:cd07091 325 GPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERAN 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666674 449 EVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07091 405 DTEYGLAAGVFTKDINKALRV--SRALKAGTVWVN-TYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
68-523 |
7.14e-70 |
|
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: 231.04 E-value: 7.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 68 DPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKiysegqGEVQE 147
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGK------ARRHA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 148 FIDICDYAVGlSRIYS---GQLINSERADHSI------LEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGA 218
Cdd:cd07101 76 FEEVLDVAIV-ARYYArraERLLKPRRRRGAIpvltrtTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 219 PSTPLvsvaTTKIVAEVLRRNNLP----PVVtlCQGGTDVGQTLVAdkRVNLVSFTGSCQTGRDVGVEVQRRFGKVILEL 294
Cdd:cd07101 155 SQTAL----TALWAVELLIEAGLPrdlwQVV--TGPGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRRLIGCSLEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 295 GGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQ 374
Cdd:cd07101 227 GGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRAL--RLGAALDYGPDMGSLISQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 375 QNVENYKAAIAEAKSLGGTVAFGGNVIQRDG--FYvEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQ 452
Cdd:cd07101 305 AQLDRVTAHVDDAVAKGATVLAGGRARPDLGpyFY-EPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDY 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24666674 453 GLSSAIFTENIGQAFKwIGAKgSDCGIVNINT--TTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07101 384 GLNASVWTRDGARGRR-IAAR-LRAGTVNVNEgyAAAWASIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
85-516 |
1.54e-69 |
|
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: 229.47 E-value: 1.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 85 ELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQEFIDICDYAVGLSRIYSG 164
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 165 QLiNSERADHSILEAWRPLGVVGVISAYNFPNAVFgwNAAI--ALTTGNSVLWKGAPSTPLVSVATTKIVAEVlrrnNLP 242
Cdd:cd07095 81 ER-ATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLP--NGHIvpALLAGNTVVFKPSELTPAVAELMVELWEEA----GLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 243 P-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVI-LELGGNNALIIDESANVKMALDAALFGCI 320
Cdd:cd07095 154 PgVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 321 GTSGQRCTTTRRIIVHEK-LHDQFVKELVGKYKQLIskIGHQLEAQTLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGN 399
Cdd:cd07095 234 LTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLR--IGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAME 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 400 VIQRDGFYVEPTVI--TGLphdASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENiGQAFKWIGAKgSDC 477
Cdd:cd07095 312 RLVAGTAFLSPGIIdvTDA---ADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDD-EALFERFLAR-IRA 386
|
410 420 430
....*....|....*....|....*....|....*....
gi 24666674 478 GIVNINTTTNGAEIGGAFGGEKATGGGRESGSDAwKQYC 516
Cdd:cd07095 387 GIVNWNRPTTGASSTAPFGGVGLSGNHRPSAYYA-ADYC 424
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
41-502 |
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 24666674 41 KELGleRDNPGVYSGQWQGRGPSVTSYDPG-TGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDEL 119
Cdd:PRK03137 31 KELG--QDYPLIIGGERITTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAII 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 120 RKYKEPLGKLVSLEVGKIYSEGQGEVQEFIDICD-YAVGLSRIYSGQLINSERADHSILeAWRPLGVVGVISAYNFPNAV 198
Cdd:PRK03137 109 RRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEyYARQMLKLADGKPVESRPGEHNRY-FYIPLGVGVVISPWNFPFAI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 199 FGWNAAIALTTGNSVLWKGAPSTPLVSVattKIVaEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGScqtg 276
Cdd:PRK03137 188 MAGMTLAAIVAGNTVLLKPASDTPVIAA---KFV-EVLEEAGLPAgVVNFVPGsGSEVGDYLVDHPKTRFITFTGS---- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 277 RDVGVEV----------QRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKE 346
Cdd:PRK03137 260 REVGLRIyeraakvqpgQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 347 LVGKYKQLisKIGHQlEAQTLVGPVHTQQNVENYKAAIAEAKSLGGTVAfGGNVIQRDGFYVEPTVITGLPHDASVVHRE 426
Cdd:PRK03137 340 VVELTKEL--TVGNP-EDNAYMGPVINQASFDKIMSYIEIGKEEGRLVL-GGEGDDSKGYFIQPTIFADVDPKARIMQEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24666674 427 TFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENigqAFKWIGAKGS-DCGIVNINTTTNGAEIG-GAFGGEKATG 502
Cdd:PRK03137 416 IFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNN---REHLEKARREfHVGNLYFNRGCTGAIVGyHPFGGFNMSG 490
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
66-523 |
4.87e-68 |
|
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: 226.46 E-value: 4.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 66 SYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYK--QWRQVPApVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQG 143
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 144 EVQEFIDICDYAVGLSRIYSGQLINSERADHSILeAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPL 223
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFSLV-LREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 224 VSVATTKIVAEVlrrNNLPP-VVTL-CQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALI 301
Cdd:cd07120 159 INAAIIRILAEI---PSLPAgVVNLfTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 302 IDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYK 381
Cdd:cd07120 236 VFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAV--KVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 382 AAIAEAKSLGGTVAF-GGNVIQR--DGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAI 458
Cdd:cd07120 314 RMVERAIAAGAEVVLrGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24666674 459 FTENIGQAFKWigAKGSDCGIVNINT-TTNGAEigGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07120 394 WTRDLARAMRV--ARAIRAGTVWINDwNKLFAE--AEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
68-523 |
1.08e-67 |
|
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: 226.17 E-value: 1.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 68 DPGTGQPIAKVRQGNVQELEHTIGLAVEAYK-QWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQG-EV 145
Cdd:cd07113 21 NPATEQVIASVASATEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfEV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 146 QEFIDICDYAVGLSRIYSGQLIN-------SERadHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGA 218
Cdd:cd07113 101 GQSANFLRYFAGWATKINGETLApsipsmqGER--YTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 219 PSTPLvsvaTTKIVAEVLRRNNLPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGN 297
Cdd:cd07113 179 EFTPL----TLLRVAELAKEAGIPDgVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 298 NALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDqfvkELVGKYKQLIS--KIGHQLEAQTLVGPVHTQQ 375
Cdd:cd07113 255 NAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFD----ELVTKLKQALSsfQVGSPMDESVMFGPLANQP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 376 NVENYKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLS 455
Cdd:cd07113 331 HFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLT 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24666674 456 SAIFTENIGQAFKWIGAKGSDCGIVNINTTTNGAEiggAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07113 411 ASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAV---PFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
55-524 |
1.93e-67 |
|
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: 225.41 E-value: 1.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQW--QGRGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSL 132
Cdd:cd07117 7 GEWvkGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 133 EVGKIYSEGQG-EVQEFIDICDYAVGLSRIYSGQLINSERADHSILEAwRPLGVVGVISAYNFPNAVFGWNAAIALTTGN 211
Cdd:cd07117 87 DNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLR-EPIGVVGQIIPWNFPFLMAAWKLAPALAAGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 212 SVLWKGAPSTPLVSVATTKIVAEVLRRNnlppVVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKV 290
Cdd:cd07117 166 TVVIKPSSTTSLSLLELAKIIQDVLPKG----VVNIVTGkGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 291 ILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGP 370
Cdd:cd07117 242 TLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENV--KVGNPLDPDTQMGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 371 VHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRD----GFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEW 446
Cdd:cd07117 320 QVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDM 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24666674 447 NNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITVN 524
Cdd:cd07117 400 ANDSEYGLGGGVFTKDINRALRV--ARAVETGRVWVN-TYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYID 474
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
55-506 |
2.62e-67 |
|
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: 225.30 E-value: 2.62e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQWQG--RGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSL 132
Cdd:cd07559 7 GEWVApsKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 133 EVGKIYSEGQG-EVQEFIDICDYAVGLSRIYSGQL--INSERADHSILEawrPLGVVGVISAYNFPNAVFGWNAAIALTT 209
Cdd:cd07559 87 DNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSLseIDEDTLSYHFHE---PLGVVGQIIPWNFPLLMAAWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 210 GNSVLWKGAPSTPLVSVATTKIVAEVlrrnnLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRF 287
Cdd:cd07559 164 GNTVVLKPASQTPLSILVLMELIGDL-----LPKgVVNVVTGfGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 288 GKVILELGGNNALIIDESANVKMA--LDAALFGCIG---TSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQL 362
Cdd:cd07559 239 IPVTLELGGKSPNIFFDDAMDADDdfDDKAEEGQLGfafNQGEVCTCPSRALVQESIYDEFIERAVERFEAI--KVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 363 EAQTLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRD----GFYVEPTVITGLPHDASVVHRETFAPIVYILKAK 438
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24666674 439 NVDQAIEWNNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRE 506
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRV--ARGIQTGRVWVN-CYHQYPAHAPFGGYKKSGIGRE 461
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
55-506 |
3.81e-67 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 224.79 E-value: 3.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQWQG--RGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSL 132
Cdd:PRK11241 17 GEWLDanNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 133 EVGKIYSEGQGEVQ---EFIDIcdYAVGLSRIYsGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTT 209
Cdd:PRK11241 97 EQGKPLAEAKGEISyaaSFIEW--FAEEGKRIY-GDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 210 GNSVLWKGAPSTPLVSVAttkiVAEVLRRNNLPP----VVTLCQGgtDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQR 285
Cdd:PRK11241 174 GCTMVLKPASQTPFSALA----LAELAIRAGIPAgvfnVVTGSAG--AVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 286 RFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQ 365
Cdd:PRK11241 248 DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKL--HIGDGLEKG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 366 TLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIE 445
Cdd:PRK11241 326 VTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIA 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24666674 446 WNNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINTTTNGAEIgGAFGGEKATGGGRE 506
Cdd:PRK11241 406 QANDTEFGLAAYFYARDLSRVFRV--GEALEYGIVGINTGIISNEV-APFGGIKASGLGRE 463
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
61-522 |
4.91e-67 |
|
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: 224.30 E-value: 4.91e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 61 GPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQ--WRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIY 138
Cdd:cd07142 18 GKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 139 SEG-QGEVQEFIDICDYAVGLSRIYSGQLINSErADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKG 217
Cdd:cd07142 98 EQArYAEVPLAARLFRYYAGWADKIHGMTLPAD-GPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 218 APSTPLVSVATTKIVAEVlrrnNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDV-GVEVQRRFGKVILEL 294
Cdd:cd07142 177 AEQTPLSALLAAKLAAEA----GLPDgVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIImQLAAKSNLKPVTLEL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 295 GGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLIskIGHQLEAQTLVGPVHTQ 374
Cdd:cd07142 253 GGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRV--VGDPFRKGVEQGPQVDK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 375 QNVENYKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGL 454
Cdd:cd07142 331 EQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGL 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666674 455 SSAIFTENIGQAFKWigAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCK-RATIT 522
Cdd:cd07142 411 AAGVFSKNIDTANTL--SRALKAGTVWVN-CYDVFDASIPFGGYKMSGIGREKGIYALNNYLQvKAVVM 476
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
68-508 |
6.89e-67 |
|
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: 223.38 E-value: 6.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 68 DPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQE 147
Cdd:cd07110 3 NPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 148 FIDICDYAVGLS---RIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLV 224
Cdd:cd07110 83 VAGCFEYYADLAeqlDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 225 SVATTKIVAEVlrrnNLPPVV--TLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALII 302
Cdd:cd07110 163 ELELAEIAAEA----GLPPGVlnVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 303 DESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYKA 382
Cdd:cd07110 239 FDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAI--RVGDPLEEGVRLGPLVSQAQYEKVLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 383 AIAEAKSLGGTVAFGGNVIQ--RDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFT 460
Cdd:cd07110 317 FIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 24666674 461 ENIGQAFKWigAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRESG 508
Cdd:cd07110 397 RDAERCDRV--AEALEAGIVWIN-CSQPCFPQAPWGGYKRSGIGRELG 441
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
55-524 |
1.00e-66 |
|
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: 223.60 E-value: 1.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQW-QGRGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQW-RQVPAPVRGEIVRQIGDELRKYKEPLGKLVSL 132
Cdd:cd07082 8 GEWkESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWwPTMPLEERIDCLHKFADLLKENKEEVANLLMW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 133 EVGKIYSEGQGEVQEFIDICDYAVGLSRIYSGQLINSERADHSI-LEAW---RPLGVVGVISAYNFP-NAVFGwNAAIAL 207
Cdd:cd07082 88 EIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKgKIAQvrrEPLGVVLAIGPFNYPlNLTVS-KLIPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 208 TTGNSVLWKGAPSTPLVSVattkIVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQR 285
Cdd:cd07082 167 IMGNTVVFKPATQGVLLGI----PLAEAFHDAGFPKgVVNVVTGrGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 286 RfgKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQ 365
Cdd:cd07082 243 K--RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKL--KVGMPWDNG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 366 TLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNviQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIE 445
Cdd:cd07082 319 VDITPLIDPKSADFVEGLIDDAVAKGATVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 446 WNNEVEQGLSSAIFTENIGQAFKWIGAkgSDCGIVNINT-TTNGAEIgGAFGGEKATGGGRESGSDAWKQYCKRATITVN 524
Cdd:cd07082 397 LANKSNYGLQASIFTKDINKARKLADA--LEVGTVNINSkCQRGPDH-FPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
55-484 |
2.49e-66 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 222.48 E-value: 2.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQW-QGRGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLE 133
Cdd:PRK13473 9 GELvAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 134 VGKIYSEG-QGEVQEFIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNS 212
Cdd:PRK13473 89 CGKPLHLAlNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 213 VLWKGAPSTPLVSVATTKIVAEVLrrnnlPPVV--TLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKV 290
Cdd:PRK13473 169 VVLKPSEITPLTALKLAELAADIL-----PPGVlnVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 291 ILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGP 370
Cdd:PRK13473 244 HLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATL--KVGDPDDEDTELGP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 371 VHTQQNVENYKAAIAEAKSLG-GTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNE 449
Cdd:PRK13473 322 LISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWAND 401
|
410 420 430
....*....|....*....|....*....|....*
gi 24666674 450 VEQGLSSAIFTENIGQAFKwiGAKGSDCGIVNINT 484
Cdd:PRK13473 402 SDYGLASSVWTRDVGRAHR--VSARLQYGCTWVNT 434
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
67-483 |
2.81e-66 |
|
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: 222.39 E-value: 2.81e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 67 YDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIV---RQIgdeLRKYKEPLGKLVSLEVGKIYSEGQG 143
Cdd:cd07085 21 YNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMfkfRQL---LEENLDELARLITLEHGKTLADARG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 144 EVQEFIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPL 223
Cdd:cd07085 98 DVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 224 VSVattkIVAEVLRRNNLPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQtgrdVGVEVQRR---FGKVILELGG-NN 298
Cdd:cd07085 178 AAM----RLAELLQEAGLPDgVLNVVHGGKEAVNALLDHPDIKAVSFVGSTP----VGEYIYERaaaNGKRVQALGGaKN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 299 ALIIDESANVKMALDA---ALFGCigtSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQ 375
Cdd:cd07085 250 HAVVMPDADLEQTANAlvgAAFGA---AGQRCMALSVAVAVGDEADEWIPKLVERAKKL--KVGAGDDPGADMGPVISPA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 376 NVENYKAAIAEAKSLGGTVAFGGNVIQ----RDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVE 451
Cdd:cd07085 325 AKERIEGLIESGVEEGAKLVLDGRGVKvpgyENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANP 404
|
410 420 430
....*....|....*....|....*....|..
gi 24666674 452 QGLSSAIFTENIGQAFKWigAKGSDCGIVNIN 483
Cdd:cd07085 405 YGNGAAIFTRSGAAARKF--QREVDAGMVGIN 434
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
61-530 |
1.38e-65 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 221.68 E-value: 1.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 61 GPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSE 140
Cdd:PRK09407 31 GPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 141 GQGEVqefidiCDYAVGlSRIY---SGQLINSERADHSI------LEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGN 211
Cdd:PRK09407 111 AFEEV------LDVALT-ARYYarrAPKLLAPRRRAGALpvltktTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 212 SVLWKGAPSTPLvsvaTTKIVAEVLRRNNLPP----VVTlcqG-GTDVGQTLVAdkRVNLVSFTGSCQTGRDVGVEVQRR 286
Cdd:PRK09407 184 AVVLKPDSQTPL----TALAAVELLYEAGLPRdlwqVVT---GpGPVVGTALVD--NADYLMFTGSTATGRVLAEQAGRR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 287 FGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQT 366
Cdd:PRK09407 255 LIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAM--RLGAGYDYSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 367 LVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRDG--FYvEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAI 444
Cdd:PRK09407 333 DMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGplFY-EPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 445 EWNNEVEQGLSSAIFTENIGQAFKwIGAKgSDCGIVNIN---TTTNGAeIGGAFGGEKATGGGRESGSDAWKQYCKRATI 521
Cdd:PRK09407 412 ERANDTPYGLNASVWTGDTARGRA-IAAR-IRAGTVNVNegyAAAWGS-VDAPMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
....*....
gi 24666674 522 TVNHSGELA 530
Cdd:PRK09407 489 ATQRVLPLA 497
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
61-524 |
1.47e-65 |
|
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: 220.48 E-value: 1.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 61 GPSVTSYDPGTGQPIAKVRQGnvqeLEHTIGLAVEAYKQ-----W-RQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEV 134
Cdd:cd07143 21 GGTVKVYNPSTGKLITKIAEA----TEADVDIAVEVAHAafetdWgLKVSGSKRGRCLSKLADLMERNLDYLASIEALDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 135 GK-IYSEGQGEVQEFIDICDYAVGLSRIYSGQLI--NSERADHSILEawrPLGVVGVISAYNFPNAVFGWNAAIALTTGN 211
Cdd:cd07143 97 GKtFGTAKRVDVQASADTFRYYGGWADKIHGQVIetDIKKLTYTRHE---PIGVCGQIIPWNFPLLMCAWKIAPALAAGN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 212 SVLWKGAPSTPLVSVATTKIVAEVlrrnNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQR-RFG 288
Cdd:cd07143 174 TIVLKPSELTPLSALYMTKLIPEA----GFPPgVINVVSGyGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKsNLK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 289 KVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLV 368
Cdd:cd07143 250 KVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKL--KVGDPFAEDTFQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 369 GPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNN 448
Cdd:cd07143 328 GPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRAN 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24666674 449 EVEQGLSSAIFTENIGQAFKwiGAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITVN 524
Cdd:cd07143 408 DSTYGLAAAVFTNNINNAIR--VANALKAGTVWVN-CYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
61-523 |
1.96e-65 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 220.52 E-value: 1.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 61 GPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSE 140
Cdd:PRK13252 21 GETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 141 GQ-GEVQEFIDICDYAVGLSRIYSGQLINSERAD--HSILEawrPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKG 217
Cdd:PRK13252 101 TSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSfvYTRRE---PLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 218 APSTPLvsvaTTKIVAEVLRRNNLPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGG 296
Cdd:PRK13252 178 SEVTPL----TALKLAEIYTEAGLPDgVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 297 NNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQN 376
Cdd:PRK13252 254 KSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERI--RIGDPMDPATNFGPLVSFAH 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 377 VENYKAAIAEAKSLGGTVAFGGNVIQRD----GFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQ 452
Cdd:PRK13252 332 RDKVLGYIEKGKAEGARLLCGGERLTEGgfanGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEY 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24666674 453 GLSSAIFTENIGQAFKWIGakGSDCGIVNINTTTNG-AEIggAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:PRK13252 412 GLAAGVFTADLSRAHRVIH--QLEAGICWINTWGESpAEM--PVGGYKQSGIGRENGIATLEHYTQIKSVQV 479
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
113-483 |
4.16e-65 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 217.30 E-value: 4.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 113 RQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQEFIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAY 192
Cdd:PRK10090 2 RKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 193 NFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVSVATTKIVAEVlrrnNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFT 270
Cdd:PRK10090 82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEI----GLPKgVFNLVLGrGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 271 GSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGK 350
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 351 YKQLisKIGHQLEAQTL-VGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFA 429
Cdd:PRK10090 238 MQAV--QFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 24666674 430 PIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENIGQAFKWIgaKGSDCGIVNIN 483
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAI--KGLKFGETYIN 367
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
61-525 |
7.87e-65 |
|
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: 218.90 E-value: 7.87e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 61 GPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYK--QWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIY 138
Cdd:cd07140 20 GKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFEngEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 139 SEG-QGEVQEFIDICDYAVGLSRIYSGQLI--NSERADHSILEAWR-PLGVVGVISAYNFPNAVFGWNAAIALTTGNSVL 214
Cdd:cd07140 100 TLAlKTHVGMSIQTFRYFAGWCDKIQGKTIpiNQARPNRNLTLTKRePIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 215 WKGAPSTPLVSVAttkiVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVE-VQRRFGKVI 291
Cdd:cd07140 180 LKPAQVTPLTALK----FAELTVKAGFPKgVINILPGsGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKScAVSNLKKVS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 292 LELGGNNALII----DESANVKMALDAALFgcigTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTL 367
Cdd:cd07140 256 LELGGKSPLIIfadcDMDKAVRMGMSSVFF----NKGENCIAAGRLFVEESIHDEFVRRVVEEVKKM--KIGDPLDRSTD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 368 VGP----VHTQQNVENYKAAIAEakslGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKN--VD 441
Cdd:cd07140 330 HGPqnhkAHLDKLVEYCERGVKE----GATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 442 QAIEWNNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATI 521
Cdd:cd07140 406 GVLQRANDTEYGLASGVFTKDINKALYV--SDKLEAGTVFVN-TYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
....
gi 24666674 522 TVNH 525
Cdd:cd07140 483 TIEY 486
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
68-521 |
1.94e-64 |
|
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: 217.08 E-value: 1.94e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 68 DPGTGQPIAKVRQGNVQELEHTIGLAVEAYK--QWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQ-GE 144
Cdd:cd07112 8 NPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALaVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 145 VQEFIDICD-YAVGLSRIYsGQLINSERADHSiLEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPL 223
Cdd:cd07112 88 VPSAANTFRwYAEAIDKVY-GEVAPTGPDALA-LITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 224 vsvaTTKIVAEVLRRNNLPPVV--TLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRdvgvevqrRFGK---------VIL 292
Cdd:cd07112 166 ----TALRLAELALEAGLPAGVlnVVPGFGHTAGEALGLHMDVDALAFTGSTEVGR--------RFLEysgqsnlkrVWL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 293 ELGGNNALII-DESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPV 371
Cdd:cd07112 234 ECGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREW--KPGDPLDPATRMGAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 372 HTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRD--GFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNE 449
Cdd:cd07112 312 VSEAHFDKVLGYIESGKAEGARLVAGGKRVLTEtgGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALAND 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24666674 450 VEQGLSSAIFTENIGQAFKwiGAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATI 521
Cdd:cd07112 392 SVYGLAASVWTSDLSRAHR--VARRLRAGTVWVN-CFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
55-508 |
1.99e-63 |
|
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: 214.75 E-value: 1.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQWqgRGPS----VTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAY--KQWRQVPAPVRGEIVRQIGDELRKYKEPLGK 128
Cdd:cd07139 5 GRW--VAPSgsetIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 129 LVSLEVGKIYS-EGQGEVQEFIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIAL 207
Cdd:cd07139 83 LWTAENGMPISwSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 208 TTGNSVLWKGAPSTPLVSVattkIVAEVLRRNNLPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRR 286
Cdd:cd07139 163 AAGCTVVLKPSPETPLDAY----LLAEAAEEAGLPPgVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 287 FGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQT 366
Cdd:cd07139 239 LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAAL--KVGDPLDPAT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 367 LVGPVHT---QQNVENYkaaIAEAKSLGGTVAFGGNVIQR--DGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVD 441
Cdd:cd07139 317 QIGPLASarqRERVEGY---IAKGRAEGARLVTGGGRPAGldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24666674 442 QAIEWNNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINTTTngAEIGGAFGGEKATGGGRESG 508
Cdd:cd07139 394 DAVRIANDSDYGLSGSVWTADVERGLAV--ARRIRTGTVGVNGFR--LDFGAPFGGFKQSGIGREGG 456
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
61-523 |
4.85e-63 |
|
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: 213.75 E-value: 4.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 61 GPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQ---WRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKI 137
Cdd:cd07141 21 GKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 138 YSEGQ-GEVQEFIDICDYAVGLSRIYSGQLINSErADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWK 216
Cdd:cd07141 101 FSKSYlVDLPGAIKVLRYYAGWADKIHGKTIPMD-GDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 217 GAPSTPLvsvaTTKIVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCqtgrDVGVEVQRRFGK----- 289
Cdd:cd07141 180 PAEQTPL----TALYLASLIKEAGFPPgVVNVVPGyGPTAGAAISSHPDIDKVAFTGST----EVGKLIQQAAGKsnlkr 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 290 VILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQliSKIGHQLEAQTLVG 369
Cdd:cd07141 252 VTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKK--RVVGNPFDPKTEQG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 370 PvhtQQNVENYK---AAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEW 446
Cdd:cd07141 330 P---QIDEEQFKkilELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIER 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24666674 447 NNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07141 407 ANNTTYGLAAAVFTKDIDKAITF--SNALRAGTVWVN-CYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
93-523 |
2.84e-62 |
|
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: 210.51 E-value: 2.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 93 AVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGkiyseGQGEVQEF-----IDICDYAVGLSRIYSGQLI 167
Cdd:cd07105 9 AAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETG-----ATAAWAGFnvdlaAGMLREAASLITQIIGGSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 168 NSERADHSILEAWRPLGVVGVISAYNFPnAVFGWNA-AIALTTGNSVLWKGAPSTPLVSVAttkiVAEVLRRNNLPP--- 243
Cdd:cd07105 84 PSDKPGTLAMVVKEPVGVVLGIAPWNAP-VILGTRAiAYPLAAGNTVVLKASELSPRTHWL----IGRVFHEAGLPKgvl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 244 -VVTLC-QGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIG 321
Cdd:cd07105 159 nVVTHSpEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 322 TSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLiskighqLEAQTLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGG-NV 400
Cdd:cd07105 239 NSGQICMSTERIIVHESIADEFVEKLKAAAEKL-------FAGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGlAD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 401 IQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIV 480
Cdd:cd07105 312 ESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAV--AKRIESGAV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 24666674 481 NINTTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07105 390 HINGMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
50-508 |
1.43e-61 |
|
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: 210.51 E-value: 1.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 50 PGVYSGQWQGRGPSVTSYDP-GTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGK 128
Cdd:cd07083 20 PLVIGGEWVDTKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 129 LVSLEVGKIYSEGQGEVQEFIDICDY-AVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIAL 207
Cdd:cd07083 100 TLTYEVGKNWVEAIDDVAEAIDFIRYyARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 208 TTGNSVLWKGAPSTPLVSVAttkiVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQR 285
Cdd:cd07083 180 AVGNTVIAKPAEDAVVVGYK----VFEIFHEAGFPPgVVQFLPGvGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAAR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 286 R------FGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIG 359
Cdd:cd07083 256 LapgqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERL--SVG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 360 HQLEAQTLVGPVHTQQNVENYKAAIAEAKSLGGTVAfGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPI--VYILKA 437
Cdd:cd07083 334 PPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVL-GGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVlsVIRYKD 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24666674 438 KNVDQAIEWNNEVEQGLSSAIFTENIGQAfKWIgAKGSDCGIVNINTTTNGAEIG-GAFGGEKATGGGRESG 508
Cdd:cd07083 413 DDFAEALEVANSTPYGLTGGVYSRKREHL-EEA-RREFHVGNLYINRKITGALVGvQPFGGFKLSGTNAKTG 482
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
55-515 |
1.78e-61 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 210.36 E-value: 1.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQWQ-----GRGPSVtsyDPGTGQPIAKVRQGNVQELEHTIGLAVEAY-----KQWRQVPAPVRGEIVRQIGDELRKYKE 124
Cdd:PLN02467 14 GEWRepvlgKRIPVV---NPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 125 PLGKLVSLEVGKIYSEGQGEVQEFIDICDYAVGL-----SRIYSGQLINSERADHSILeaWRPLGVVGVISAYNFPNAVF 199
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLaealdAKQKAPVSLPMETFKGYVL--KEPLGVVGLITPWNYPLLMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 200 GWNAAIALTTGNSVLWKgaPSTpLVSVaTTKIVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGR 277
Cdd:PLN02467 169 TWKVAPALAAGCTAVLK--PSE-LASV-TCLELADICREVGLPPgVLNVVTGlGTEAGAPLASHPGVDKIAFTGSTATGR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 278 DVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisK 357
Cdd:PLN02467 245 KIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNI--K 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 358 IGHQLEAQTLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQ--RDGFYVEPTVITGLPHDASVVHRETFAPIVYIL 435
Cdd:PLN02467 323 ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 436 KAKNVDQAIEWNNEVEQGLSSAIFT------ENIGQAFkwigakgsDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGS 509
Cdd:PLN02467 403 TFSTEDEAIELANDSHYGLAGAVISndlercERVSEAF--------QAGIVWIN-CSQPCFCQAPWGGIKRSGFGRELGE 473
|
....*.
gi 24666674 510 DAWKQY 515
Cdd:PLN02467 474 WGLENY 479
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
66-521 |
6.56e-60 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 205.10 E-value: 6.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 66 SYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEV 145
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 146 QEFIDICD-YAVglsriYSGQLINSERA---DHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPST 221
Cdd:PRK13968 91 AKSANLCDwYAE-----HGPAMLKAEPTlveNQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 222 plvsVATTKIVAEVLRRNNLPPVVTLCQGGTDVG-QTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNAL 300
Cdd:PRK13968 166 ----MGCAQLIAQVFKDAGIPQGVYGWLNADNDGvSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 301 IIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPV-------HT 373
Cdd:PRK13968 242 IVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAAL--KMGDPRDEENALGPMarfdlrdEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 374 QQNVEnykAAIAEakslGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQG 453
Cdd:PRK13968 320 HHQVE---ATLAE----GARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFG 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666674 454 LSSAIFTENIGQAFKWigAKGSDCGIVNINT-TTNGAEIggAFGGEKATGGGRESGSDAWKQYCKRATI 521
Cdd:PRK13968 393 LSATIFTTDETQARQM--AARLECGGVFINGyCASDARV--AFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
61-515 |
8.27e-60 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 205.83 E-value: 8.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 61 GPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQ--WRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIY 138
Cdd:PLN02766 35 GKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 139 SEGQgevqeFIDICDyAVGLSRIYSGQlinSERADHSILEAWR---------PLGVVGVISAYNFPNAVFGWNAAIALTT 209
Cdd:PLN02766 115 ALGK-----AVDIPA-AAGLLRYYAGA---ADKIHGETLKMSRqlqgytlkePIGVVGHIIPWNFPSTMFFMKVAPALAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 210 GNSVLWKGAPSTPLVSVattkIVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQR-R 286
Cdd:PLN02766 186 GCTMVVKPAEQTPLSAL----FYAHLAKLAGVPDgVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 287 FGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQliSKIGHQLEAQT 366
Cdd:PLN02766 262 LKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKD--WVVGDPFDPRA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 367 LVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEW 446
Cdd:PLN02766 340 RQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKK 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666674 447 NNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINTTTnGAEIGGAFGGEKATGGGRESGSDAWKQY 515
Cdd:PLN02766 420 ANNTKYGLAAGIVTKDLDVANTV--SRSIRAGTIWVNCYF-AFDPDCPFGGYKMSGFGRDQGMDALDKY 485
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
55-519 |
2.81e-59 |
|
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: 203.78 E-value: 2.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQWQG--RGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSL 132
Cdd:cd07111 28 GKWVKpeNRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 133 EVGKiysegqgEVQEFIDiCD--YAVGLSRIYSGQLINSERAdhsiLEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTG 210
Cdd:cd07111 108 DNGK-------PIRESRD-CDipLVARHFYHHAGWAQLLDTE----LAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 211 NSVLWKGAPSTPLVSVATTKIVAEVlrrnNLPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGK 289
Cdd:cd07111 176 NTVVLKPAEYTPLTALLFAEICAEA----GLPPgVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 290 VILELGGNNALIIDESANVKMA----LDAALFgcigTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQ 365
Cdd:cd07111 252 LSLELGGKSPFIVFDDADLDSAvegiVDAIWF----NQGQVCCAGSRLLVQESVAEELIRKLKERMSHL--RVGDPLDKA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 366 TLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIE 445
Cdd:cd07111 326 IDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24666674 446 WNNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRESGSDAWKQYCKRA 519
Cdd:cd07111 406 LANNTPYGLAASVWSENLSLALEV--ALSLKAGVVWIN-GHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPS 476
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
55-508 |
2.49e-55 |
|
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: 192.72 E-value: 2.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQWQ-GRGPSVTS-YDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSL 132
Cdd:cd07138 5 GAWVaPAGTETIDvINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 133 EVGK-IYSEGQGEVQEFIDICDYAVGLSRIYSGQlinsERADHSILEaWRPLGVVGVISAYNFP-NAVFGwNAAIALTTG 210
Cdd:cd07138 85 EMGApITLARAAQVGLGIGHLRAAADALKDFEFE----ERRGNSLVV-REPIGVCGLITPWNWPlNQIVL-KVAPALAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 211 NSVLWKGAPSTPLvsvaTTKIVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFG 288
Cdd:cd07138 159 CTVVLKPSEVAPL----SAIILAEILDEAGLPAgVFNLVNGdGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 289 KVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFV---KELVGKYkqlisKIGHQLEAQ 365
Cdd:cd07138 235 RVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEeiaAAAAEAY-----VVGDPRDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 366 TLVGPVHTQ---QNVENY-KAAIAEakslGGTVAFGG----NVIQRdGFYVEPTVITGLPHDASVVHRETFAPIVYILKA 437
Cdd:cd07138 310 TTLGPLASAaqfDRVQGYiQKGIEE----GARLVAGGpgrpEGLER-GYFVKPTVFADVTPDMTIAREEIFGPVLSIIPY 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24666674 438 KNVDQAIEWNNEVEQGLSSAIFTENIGQAfKWIgAKGSDCGIVNINTTtnGAEIGGAFGGEKATGGGRESG 508
Cdd:cd07138 385 DDEDEAIAIANDTPYGLAGYVWSADPERA-RAV-ARRLRAGQVHINGA--AFNPGAPFGGYKQSGNGREWG 451
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
61-522 |
9.05e-55 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 193.10 E-value: 9.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 61 GPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQ--WRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIY 138
Cdd:PLN02466 72 GKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 139 SEG-QGEVQEFIDICDYAVGLSRIYSGQLINSErADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKG 217
Cdd:PLN02466 152 EQSaKAELPMFARLFRYYAGWADKIHGLTVPAD-GPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 218 APSTPLVSVATTKIVAEVlrrnNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDV-GVEVQRRFGKVILEL 294
Cdd:PLN02466 231 AEQTPLSALYAAKLLHEA----GLPPgVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVlELAAKSNLKPVTLEL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 295 GGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKElvGKYKQLISKIGHQLEAQTLVGPvhtQ 374
Cdd:PLN02466 307 GGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK--AKARALKRVVGDPFKKGVEQGP---Q 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 375 QNVENYKAAIAEAKS---LGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVE 451
Cdd:PLN02466 382 IDSEQFEKILRYIKSgveSGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTR 461
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24666674 452 QGLSSAIFTENIGQAFKWigAKGSDCGIVNINT-TTNGAEIggAFGGEKATGGGRESGSDAWKQYCK-RATIT 522
Cdd:PLN02466 462 YGLAAGVFTQNLDTANTL--SRALRVGTVWVNCfDVFDAAI--PFGGYKMSGIGREKGIYSLNNYLQvKAVVT 530
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
67-508 |
3.76e-54 |
|
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: 190.87 E-value: 3.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 67 YDP-GTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEV 145
Cdd:cd07125 51 IDPaDHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 146 QEFIDICD-YAVGLSRIYSGQLINSERADHSILEaWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLV 224
Cdd:cd07125 131 REAIDFCRyYAAQARELFSDPELPGPTGELNGLE-LHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 225 SVAttkiVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRdvgvEVQR----RFG---KVILELG 295
Cdd:cd07125 210 AAR----AVELLHEAGVPRdVLQLVPGdGEEIGEALVAHPRIDGVIFTGSTETAK----LINRalaeRDGpilPLIAETG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 296 GNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQ 375
Cdd:cd07125 282 GKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASL--KVGDPWDLSTDVGPLIDKP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 376 NVENYKAAI----AEAKSLggtvaFGGNVIQRDGFYVEPTVITGlphDASVVH-RETFAPIVYILKAK--NVDQAIEWNN 448
Cdd:cd07125 360 AGKLLRAHTelmrGEAWLI-----APAPLDDGNGYFVAPGIIEI---VGIFDLtTEVFGPILHVIRFKaeDLDEAIEDIN 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666674 449 EVEQGLSSAIFTENIGQAFKW---IGAkgsdcGIVNINTTTNGAeIGGA--FGGEKATGGGRESG 508
Cdd:cd07125 432 ATGYGLTLGIHSRDEREIEYWrerVEA-----GNLYINRNITGA-IVGRqpFGGWGLSGTGPKAG 490
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
63-521 |
6.63e-54 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 188.79 E-value: 6.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 63 SVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQ 142
Cdd:PRK09406 2 PIATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 143 GEVQEfidiCDYAVglsRIYSG---QLINSERADHSILEA------WRPLGVVGVISAYNFPNavfgWN----AAIALTT 209
Cdd:PRK09406 82 AEALK----CAKGF---RYYAEhaeALLADEPADAAAVGAsrayvrYQPLGVVLAVMPWNFPL----WQvvrfAAPALMA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 210 GNSVLWKGAPSTPlvsvATTKIVAEVLRRNNLPP--VVTLCQGGTDVgQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRF 287
Cdd:PRK09406 151 GNVGLLKHASNVP----QTALYLADLFRRAGFPDgcFQTLLVGSGAV-EAILRDPRVAAATLTGSEPAGRAVAAIAGDEI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 288 GKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTL 367
Cdd:PRK09406 226 KKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAAL--RVGDPTDPDTD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 368 VGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWN 447
Cdd:PRK09406 304 VGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIA 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666674 448 NEVEQGLSSAIFTENIGQAFKWIgaKGSDCGIVNIN-TTTNGAEIGgaFGGEKATGGGRESGSDAWKQYCKRATI 521
Cdd:PRK09406 384 NATTFGLGSNAWTRDEAEQERFI--DDLEAGQVFINgMTVSYPELP--FGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
55-507 |
2.45e-53 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 188.24 E-value: 2.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQWQ-GRGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLE 133
Cdd:PRK09457 7 GDWIaGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 134 VGKIYSEGQGEVQEFIDICDYAVGLSRIYSGQLINsERADHSILEAWRPLGVVGVISAYNFPNAVFgwNAAI--ALTTGN 211
Cdd:PRK09457 87 TGKPLWEAATEVTAMINKIAISIQAYHERTGEKRS-EMADGAAVLRHRPHGVVAVFGPYNFPGHLP--NGHIvpALLAGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 212 SVLWKGAPSTPLVSVATTKIvaevLRRNNLPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTgrdvGVEVQRRF--- 287
Cdd:PRK09457 164 TVVFKPSELTPWVAELTVKL----WQQAGLPAgVLNLVQGGRETGKALAAHPDIDGLLFTGSANT----GYLLHRQFagq 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 288 -GKVI-LELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLH-DQFVKELVGKYKQLIskIGH-QLE 363
Cdd:PRK09457 236 pEKILaLEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLT--VGRwDAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 364 AQTLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVI--TGLphdASVVHRETFAPIVYILKAKNVD 441
Cdd:PRK09457 314 PQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIIdvTGV---AELPDEEYFGPLLQVVRYDDFD 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666674 442 QAIEWNNEVEQGLSSAIFTENIG---QAFKWIGAkgsdcGIVNINTTTNGAEIGGAFGGEKATGGGRES 507
Cdd:PRK09457 391 EAIRLANNTRFGLSAGLLSDDREdydQFLLEIRA-----GIVNWNKPLTGASSAAPFGGVGASGNHRPS 454
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
67-524 |
9.09e-49 |
|
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: 175.18 E-value: 9.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 67 YDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQ-GEV 145
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 146 qefIDICDYAVGLSRiYSGQLINSERADHSILEAWR-------PLGVVGVISAYNFP--NAvfgWNAAI-ALTTGNSVLW 215
Cdd:cd07098 81 ---LVTCEKIRWTLK-HGEKALRPESRPGGLLMFYKrarveyePLGVVGAIVSWNYPfhNL---LGPIIaALFAGNAIVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 216 KGAPSTPLVSVATTKIVAEVLRRNNLPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILEL 294
Cdd:cd07098 154 KVSEQVAWSSGFFLSIIRECLAACGHDPdLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 295 GGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQ 374
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQAL--RQGPPLDGDVDVGAMISP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 375 QNVENYKAAIAEAKSLGGTVAFGGNVIQRD----GFYVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEV 450
Cdd:cd07098 312 ARFDRLEELVADAVEKGARLLAGGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANST 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 451 EQGLSSAIFTENIGQAFKWigAKGSDCGIVNINtttngaEIGGA-------FGGEKATGGGRESGSDAWKQYCKRATITV 523
Cdd:cd07098 392 EYGLGASVFGKDIKRARRI--ASQLETGMVAIN------DFGVNyyvqqlpFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
.
gi 24666674 524 N 524
Cdd:cd07098 464 D 464
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
62-508 |
3.46e-46 |
|
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: 168.94 E-value: 3.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 62 PSVTSYDPGTgqPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEG 141
Cdd:TIGR01238 54 PVTNPADRRD--IVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 142 QGEVQEFIDICDYavglsriYSGQLINSERADHSileawRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPST 221
Cdd:TIGR01238 132 IAEVREAVDFCRY-------YAKQVRDVLGEFSV-----ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 222 PLVSVATTKIVAEVlrrnNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRF---GKVILELGG 296
Cdd:TIGR01238 200 SLIAYRAVELMQEA----GFPAgTIQLLPGrGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 297 NNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLISKIGHQLeaQTLVGPVHTQQN 376
Cdd:TIGR01238 276 QNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLL--TTDVGPVIDAEA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 377 VENYKAAIAEAKSLGGTVA---FGGNVIQRDGFYVEPTVITglPHDASVVHRETFAPIVYIL--KAKNVDQAIEWNNEVE 451
Cdd:TIGR01238 354 KQNLLAHIEHMSQTQKKIAqltLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVryKARELDQIVDQINQTG 431
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 24666674 452 QGLSSAIFTENIGqAFKWIgAKGSDCGIVNINTTTNGAEIG-GAFGGEKATGGGRESG 508
Cdd:TIGR01238 432 YGLTMGVHSRIET-TYRWI-EKHARVGNCYVNRNQVGAVVGvQPFGGQGLSGTGPKAG 487
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
55-507 |
5.52e-44 |
|
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: 162.62 E-value: 5.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQWQG--RGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSL 132
Cdd:cd07116 7 GEWVApvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 133 EVGKIYSEGQG-EVQEFIDICDYAVGLSRIYSGQL--INSERADHSILEawrPLGVVGVISAYNFPNAVFGWNAAIALTT 209
Cdd:cd07116 87 DNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSIseIDENTVAYHFHE---PLGVVGQIIPWNFPLLMATWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 210 GNSVLWKGAPSTPLVSVATTKIVAEVlrrnnLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRF 287
Cdd:cd07116 164 GNCVVLKPAEQTPASILVLMELIGDL-----LPPgVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 288 GKVILELGGNNALIIDESanVKMA----LDAALFGCIG---TSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLISkiGH 360
Cdd:cd07116 239 IPVTLELGGKSPNIFFAD--VMDAddafFDKALEGFVMfalNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQ--GN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 361 QLEAQTLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNVIQR----DGFYVEPTVITGlPHDASVVHRETFAPIVYILK 436
Cdd:cd07116 315 PLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELggllGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTT 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24666674 437 AKNVDQAIEWNNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINtTTNGAEIGGAFGGEKATGGGRES 507
Cdd:cd07116 394 FKDEEEALEIANDTLYGLGAGVWTRDGNTAYRM--GRGIQAGRVWTN-CYHLYPAHAAFGGYKQSGIGREN 461
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
68-522 |
7.07e-43 |
|
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: 159.28 E-value: 7.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 68 DPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQE 147
Cdd:TIGR01722 22 NPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDVAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 148 FIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVSVa 227
Cdd:TIGR01722 102 GLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAV- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 228 ttkIVAEVLRRNNLPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVgVEVQRRFGKVILELGG-NNALIIDES 305
Cdd:TIGR01722 181 ---KLAELFSEAGAPDgVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYI-HTTGSAHGKRVQALGGaKNHMVVMPD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 306 ANVKMALDAALFGCIGTSGQRCTT-TRRIIVHEKlhDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYKAAI 384
Cdd:TIGR01722 257 ADKDAAADALVGAAYGAAGQRCMAiSAAVLVGAA--DEWVPEIRERAEKI--RIGPGDDPGAEMGPLITPQAKDRVASLI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 385 AEAKSLGGTVAFGGNVIQRDGF----YVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFT 460
Cdd:TIGR01722 333 AGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFT 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24666674 461 ENIGQAFKWigAKGSDCGIVNINTTTNGAEIGGAFGGEKAT--GGGRESGSDAWKQYCKRATIT 522
Cdd:TIGR01722 413 RDGAAARRF--QHEIEVGQVGVNVPIPVPLPYFSFTGWKDSffGDHHIYGKQGTHFYTRGKTVT 474
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
69-504 |
3.66e-42 |
|
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: 156.81 E-value: 3.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 69 PGTGQPIAKVRQGNVQELEHTIGLAVEAYK---QWrqVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEV 145
Cdd:cd07148 6 PFDLKPIGEVPTVDWAAIDKALDTAHALFLdrnNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 146 QEFIDICDYAVGLSRIYSGQLI-------NSERADHSILEawrPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGA 218
Cdd:cd07148 84 TRAIDGVELAADELGQLGGREIpmgltpaSAGRIAFTTRE---PIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 219 PSTPLVSVATTKIVAEVlrrnNLPPvvTLCQG---GTDVGQTLVADKRVNLVSFTGSCQtgrdVGVEVQRRFG---KVIL 292
Cdd:cd07148 161 LATPLSCLAFVDLLHEA----GLPE--GWCQAvpcENAVAEKLVTDPRVAFFSFIGSAR----VGWMLRSKLApgtRCAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 293 ELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVH 372
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKL--VVGDPTDPDTEVGPLI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 373 TQQNVENYKAAIAEAKSLGGTVAFGGNVIQRDGFyvEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQ 452
Cdd:cd07148 309 RPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPV 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 24666674 453 GLSSAIFTENIGQAFKwiGAKGSDCGIVNINTTTNGAEIGGAFGGEKATGGG 504
Cdd:cd07148 387 AFQAAVFTKDLDVALK--AVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
75-504 |
2.27e-41 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 159.65 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 75 IAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQEFIDICDY 154
Cdd:PRK11905 581 VGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRY 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 155 avglsriYSGQLINSERADHSileawRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVsvATTKIvaE 234
Cdd:PRK11905 661 -------YAAQARRLLNGPGH-----KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLI--AARAV--R 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 235 VLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGK---VILELGGNNALIIDESANVK 309
Cdd:PRK11905 725 LLHEAGVPKdALQLLPGdGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPpvpLIAETGGQNAMIVDSSALPE 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 310 MALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHT---QQNVENYkaaIAE 386
Cdd:PRK11905 805 QVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDEL--RIGDPWRLSTDVGPVIDaeaQANIEAH---IEA 879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 387 AKSLGGTV---AFGGNViqRDGFYVEPTVI--TGLphdaSVVHRETFAPIVYIL--KAKNVDQAIEWNNEVEQGLSSAIF 459
Cdd:PRK11905 880 MRAAGRLVhqlPLPAET--EKGTFVAPTLIeiDSI----SDLEREVFGPVLHVVrfKADELDRVIDDINATGYGLTFGLH 953
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 24666674 460 T---ENIGQAFKWIGAkgsdcGIVNINTTTNGAEIG-GAFGGEKATGGG 504
Cdd:PRK11905 954 SridETIAHVTSRIRA-----GNIYVNRNIIGAVVGvQPFGGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
73-445 |
1.34e-39 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 154.33 E-value: 1.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 73 QPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQEFIDIC 152
Cdd:COG4230 582 DVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFC 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 153 DYavglsriYSGQLINSERADHsileAWRPLGVVGVISAYNFPNAVF-GWNAAiALTTGNSVLWKGAPSTPLVSVATTKI 231
Cdd:COG4230 662 RY-------YAAQARRLFAAPT----VLRGRGVFVCISPWNFPLAIFtGQVAA-ALAAGNTVLAKPAEQTPLIAARAVRL 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 232 vaevLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRdvgvEVQR----RFGK---VILELGGNNALII 302
Cdd:COG4230 730 ----LHEAGVPAdVLQLLPGdGETVGAALVADPRIAGVAFTGSTETAR----LINRtlaaRDGPivpLIAETGGQNAMIV 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 303 DESA----NVKMALDAAlFGCigtSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPV---HTQQ 375
Cdd:COG4230 802 DSSAlpeqVVDDVLASA-FDS---AGQRCSALRVLCVQEDIADRVLEMLKGAMAEL--RVGDPADLSTDVGPVidaEARA 875
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24666674 376 NVENYKAAIAEAKSLGGTVAFGGNViqRDGFYVEPTVITgLPhDASVVHRETFAPIVYIL--KAKNVDQAIE 445
Cdd:COG4230 876 NLEAHIERMRAEGRLVHQLPLPEEC--ANGTFVAPTLIE-ID-SISDLEREVFGPVLHVVryKADELDKVID 943
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
78-508 |
1.11e-37 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 148.58 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 78 VRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQEfidicdyAVG 157
Cdd:PRK11809 676 VREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVRE-------AVD 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 158 LSRIYSGQLinseRADHSIlEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVSVATTKIvaevLR 237
Cdd:PRK11809 749 FLRYYAGQV----RDDFDN-DTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRI----LL 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 238 RNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRF---GK---VILELGGNNALIIDESA--- 306
Cdd:PRK11809 820 EAGVPAgVVQLLPGrGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqGRpipLIAETGGQNAMIVDSSAlte 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 307 -----NVKMALDAAlfgcigtsGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYK 381
Cdd:PRK11809 900 qvvadVLASAFDSA--------GQRCSALRVLCLQDDVADRTLKMLRGAMAEC--RMGNPDRLSTDIGPVIDAEAKANIE 969
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 382 AAIAEAKSLGGTV---AFGGNVIQRDGFYVEPTVITglPHDASVVHRETFAPIVYILKAK--NVDQAIEWNNEVEQGLSS 456
Cdd:PRK11809 970 RHIQAMRAKGRPVfqaARENSEDWQSGTFVPPTLIE--LDSFDELKREVFGPVLHVVRYNrnQLDELIEQINASGYGLTL 1047
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 24666674 457 AIFT---ENIGQAFKWIGAkgsdcGIVNINTTTNGAEIG-GAFGGEKATGGGRESG 508
Cdd:PRK11809 1048 GVHTridETIAQVTGSAHV-----GNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAG 1098
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
68-504 |
2.04e-37 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 146.04 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 68 DPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKIYSEGQGEVQE 147
Cdd:PLN02419 135 NPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 148 FIDICDYAVGLSRIYSGQLINSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVSVa 227
Cdd:PLN02419 215 GLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASV- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 228 ttkIVAEVLRRNNLPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESA 306
Cdd:PLN02419 294 ---ILAELAMEAGLPDgVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 307 NVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLhDQFVKELVGKYKQLISKIGHQLEAQtlVGPVHTQQNVENYKAAIAE 386
Cdd:PLN02419 371 NIDATLNALLAAGFGAAGQRCMALSTVVFVGDA-KSWEDKLVERAKALKVTCGSEPDAD--LGPVISKQAKERICRLIQS 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 387 AKSLGGTVAFGGNVIQRDGF----YVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTEN 462
Cdd:PLN02419 448 GVDDGAKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSS 527
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 24666674 463 IGQAFKWigAKGSDCGIVNINTTTNGAEIGGAFGGEKATGGG 504
Cdd:PLN02419 528 GAAARKF--QMDIEAGQIGINVPIPVPLPFFSFTGNKASFAG 567
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
59-445 |
2.54e-37 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 147.27 E-value: 2.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 59 GRGPSVTS-YDpgTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGKI 137
Cdd:PRK11904 561 GEARPVVSpAD--RRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKT 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 138 YSEGQGEVQEFIDICDYavglsriYSGQlinSERadhsILEAWRPL---------------GVVGVISAYNFPNAVF-GW 201
Cdd:PRK11904 639 LQDAIAEVREAVDFCRY-------YAAQ---ARR----LFGAPEKLpgptgesnelrlhgrGVFVCISPWNFPLAIFlGQ 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 202 NAAiALTTGNSVLWKGAPSTPLVSVATTKIvaevLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDV 279
Cdd:PRK11904 705 VAA-ALAAGNTVIAKPAEQTPLIAAEAVKL----LHEAGIPKdVLQLLPGdGATVGAALTADPRIAGVAFTGSTETARII 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 280 GVEVQRRFGKV---ILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLis 356
Cdd:PRK11904 780 NRTLAARDGPIvplIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAEL-- 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 357 KIGHQLEAQTLVGPV---HTQQNVENYKAAIAEAKSLGGTVAFGGNViqRDGFYVEPTVITgLPhDASVVHRETFAPIVY 433
Cdd:PRK11904 858 KVGDPRLLSTDVGPVidaEAKANLDAHIERMKREARLLAQLPLPAGT--ENGHFVAPTAFE-ID-SISQLEREVFGPILH 933
|
410
....*....|....
gi 24666674 434 IL--KAKNVDQAIE 445
Cdd:PRK11904 934 VIryKASDLDKVID 947
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
182-462 |
6.24e-36 |
|
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: 138.90 E-value: 6.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 182 PLGVVGVISAYNFP-NAVFGWNAAiALTTGNSVLWKgaPS--TPLVSVATTKIVAEVLRRNNlppvVTLCQGGTDVGQTL 258
Cdd:cd07134 100 PKGVCLIISPWNYPfNLAFGPLVS-AIAAGNTAILK--PSelTPHTSAVIAKIIREAFDEDE----VAVFEGDAEVAQAL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 259 VaDKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEK 338
Cdd:cd07134 173 L-ELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 339 LHDQFVKELVGKYKQLISKIGHQLEAQTLVGPVHtQQNVENYKAAIAEAKSLGGTVAFGGNViQRDGFYVEPTVITGLPH 418
Cdd:cd07134 252 VKDAFVEHLKAEIEKFYGKDAARKASPDLARIVN-DRHFDRLKGLLDDAVAKGAKVEFGGQF-DAAQRYIAPTVLTNVTP 329
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 24666674 419 DASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTEN 462
Cdd:cd07134 330 DMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKD 373
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
41-521 |
6.91e-36 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 140.03 E-value: 6.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 41 KELGLERDNPGVYSGQWQ--GRGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQ--WRQVPAPVRGEIVRQIG 116
Cdd:PRK09847 12 KALSLAIENRLFINGEYTaaAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 117 DELRKYKEPLGKLVSLEVGK-IYSEGQGEVQEFID-ICDYAVGLSRIYsGQLINSERADHSILEAwRPLGVVGVISAYNF 194
Cdd:PRK09847 92 DLMEAHAEELALLETLDTGKpIRHSLRDDIPGAARaIRWYAEAIDKVY-GEVATTSSHELAMIVR-EPVGVIAAIVPWNF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 195 PNAVFGWNAAIALTTGNSVLWKGAPSTPLVSVATTKIVAEVlrrnNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGS 272
Cdd:PRK09847 170 PLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEA----GLPDgVLNVVTGfGHEAGQALSRHNDIDAIAFTGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 273 CQTGR----DVGvevQRRFGKVILELGGNNALII-DESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKEL 347
Cdd:PRK09847 246 TRTGKqllkDAG---DSNMKRVWLEAGGKSANIVfADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 348 vgkyKQLISKI--GHQLEAQTLVGPVHTQQNVENYKAAIAEAKSLGGTVAFGGNviQRDGFYVEPTVITGLPHDASVVHR 425
Cdd:PRK09847 323 ----KQQAQNWqpGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRN--AGLAAAIGPTIFVDVDPNASLSRE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 426 ETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENIGQAFKWigAKGSDCGIVNINTTTNGaEIGGAFGGEKATGGGR 505
Cdd:PRK09847 397 EIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRM--SRRLKAGSVFVNNYNDG-DMTVPFGGYKQSGNGR 473
|
490
....*....|....*.
gi 24666674 506 ESGSDAWKQYCKRATI 521
Cdd:PRK09847 474 DKSLHALEKFTELKTI 489
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
72-509 |
6.63e-35 |
|
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: 137.72 E-value: 6.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 72 GQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELR-KYKEPLGKLVSLEVGKiySEGQGEVQ---E 147
Cdd:cd07123 57 AHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQGK--NVWQAEIDaacE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 148 FIDI----CDYAvglSRIYSGQLINSERADHSILEaWRPL-GVVGVISAYNFpNAVfGWN--AAIALTtGNSVLWKGAPS 220
Cdd:cd07123 135 LIDFlrfnVKYA---EELYAQQPLSSPAGVWNRLE-YRPLeGFVYAVSPFNF-TAI-GGNlaGAPALM-GNVVLWKPSDT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 221 tplvSVATTKIVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRD------VGVEVQRRFGKVIL 292
Cdd:cd07123 208 ----AVLSNYLVYKILEEAGLPPgVINFVPGdGPVVGDTVLASPHLAGLHFTGSTPTFKSlwkqigENLDRYRTYPRIVG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 293 ELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVH 372
Cdd:cd07123 284 ETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEI--KMGDPDDFSNFMGAVI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 373 TQQNVENYKAAIAEAK-SLGGTVAFGGNVIQRDGFYVEPTVI-TGLPHDASVVhRETFAPI--VYILKAKNVDQAIEWNN 448
Cdd:cd07123 362 DEKAFDRIKGYIDHAKsDPEAEIIAGGKCDDSVGYFVEPTVIeTTDPKHKLMT-EEIFGPVltVYVYPDSDFEETLELVD 440
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666674 449 EV-EQGLSSAIFTEN---IGQAFKwigAKGSDCGIVNINTTTNGAEIggafgGEKATGGGRESGS 509
Cdd:cd07123 441 TTsPYALTGAIFAQDrkaIREATD---ALRNAAGNFYINDKPTGAVV-----GQQPFGGARASGT 497
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
49-483 |
6.75e-35 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 137.19 E-value: 6.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 49 NPGVY----SGQWQ--GRGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKY 122
Cdd:PLN00412 12 DGDVYkyyaDGEWRtsSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 123 KEPLGKLVSLEVGKIYSEGQGEVQEFIDICDYAV--GLSRIYSGQLINS------ERADHSiLEAWRPLGVVGVISAYNF 194
Cdd:PLN00412 92 KAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAeeGVRILGEGKFLVSdsfpgnERNKYC-LTSKIPLGVVLAIPPFNY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 195 PNAVFGWNAAIALTTGNSVLWKgAPSTPLVSvatTKIVAEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGS 272
Cdd:PLN00412 171 PVNLAVSKIAPALIAGNAVVLK-PPTQGAVA---ALHMVHCFHLAGFPKgLISCVTGkGSEIGDFLTMHPGVNCISFTGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 273 cqtgrDVGVEVQRRFGKVIL--ELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGK 350
Cdd:PLN00412 247 -----DTGIAISKKAGMVPLqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 351 YKQLisKIGhQLEAQTLVGPVHTQQNVENYKAAIAEAKSLGGTVAfggNVIQRDGFYVEPTVITGLPHDASVVHRETFAP 430
Cdd:PLN00412 322 VAKL--TVG-PPEDDCDITPVVSESSANFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGP 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 24666674 431 IVYILKAKNVDQAIEWNNEVEQGLSSAIFTENIGQAFKWIGAKgsDCGIVNIN 483
Cdd:PLN00412 396 VLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAM--ETGTVQIN 446
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
182-462 |
4.73e-32 |
|
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: 128.39 E-value: 4.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 182 PLGVVGVISAYNFPnavfgWNAAI-----ALTTGNSVLWKgaPS--TPlvsvATTKIVAEVLRRNNLPPVVTLCQGGTDV 254
Cdd:cd07136 100 PYGVVLIIAPWNYP-----FQLALapligAIAAGNTAVLK--PSelTP----NTSKVIAKIIEETFDEEYVAVVEGGVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 255 GQTLVaDKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRII 334
Cdd:cd07136 169 NQELL-DQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 335 VHEKLHDQFVKELVGKYKQLISKighqleaqtlvgpvHTQQNvENYKAAIAE------AKSL-GGTVAFGGNvIQRDGFY 407
Cdd:cd07136 248 VHESVKEKFIKELKEEIKKFYGE--------------DPLES-PDYGRIINEkhfdrlAGLLdNGKIVFGGN-TDRETLY 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 24666674 408 VEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTEN 462
Cdd:cd07136 312 IEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSED 366
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
182-483 |
7.22e-32 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 128.61 E-value: 7.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 182 PLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKgaPSTplVSVATTKIVAEVLRRNNLPPVVTLCQGGTDVGQTLVaD 261
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLK--PSE--LSPHTSKLMAKLLTKYLDPSYVRVIEGGVEVTTELL-K 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 262 KRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHD 341
Cdd:PTZ00381 184 EPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKD 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 342 QFVKELvgkYKQLISKIGHQLEAQTLVGPVHTQQNVENYKAAIaeaKSLGGTVAFGG--NVIQRdgfYVEPTVITGLPHD 419
Cdd:PTZ00381 264 KFIEAL---KEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELI---KDHGGKVVYGGevDIENK---YVAPTIIVNPDLD 334
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24666674 420 ASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENigQAFKWIGAKGSDCGIVNIN 483
Cdd:PTZ00381 335 SPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGED--KRHKELVLENTSSGAVVIN 396
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
181-521 |
1.78e-31 |
|
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: 126.57 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 181 RPLGVVGVISAYNFPnavfgWNAAI-----ALTTGNSVLWKGAPSTPlvsvATTKIVAEVLRRNNLPPVVTLCQGGTDVG 255
Cdd:cd07135 107 EPLGVVLIIGPWNYP-----VLLALsplvgAIAAGCTVVLKPSELTP----HTAALLAELVPKYLDPDAFQVVQGGVPET 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 256 QTLVaDKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIV 335
Cdd:cd07135 178 TALL-EQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 336 HEKLHDQFVKELVGKYKQLISKIGHQLEAQT-LVGPVHtqqnVENYKAAIAEAKslgGTVAFGGNVIQRDGFyVEPTVIT 414
Cdd:cd07135 257 DPSVYDEFVEELKKVLDEFYPGGANASPDYTrIVNPRH----FNRLKSLLDTTK---GKVVIGGEMDEATRF-IPPTIVS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 415 GLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENigQAFK-WIGAKGSDcGIVNINTTTNGAEIGG 493
Cdd:cd07135 329 DVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDD--KSEIdHILTRTRS-GGVVINDTLIHVGVDN 405
|
330 340
....*....|....*....|....*....
gi 24666674 494 A-FGGEKATGGGRESGSDAWKQYCKRATI 521
Cdd:cd07135 406 ApFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
182-462 |
3.06e-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: 125.72 E-value: 3.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 182 PLGVVGVISAYNFP-NAVFGwNAAIALTTGNSVLWKgaPS--TPlvsvATTKIVAEVLRRNNLPPVVTLCQGGTDVGQTL 258
Cdd:cd07087 100 PLGVVLIIGPWNYPlQLALA-PLIGAIAAGNTVVLK--PSelAP----ATSALLAKLIPKYFDPEAVAVVEGGVEVATAL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 259 VAdKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEK 338
Cdd:cd07087 173 LA-EPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 339 LHDQFVKELVgkyKQLISKIGHQLEAQTLVGPVHTQQNVENYKAAIAeakslGGTVAFGGNViQRDGFYVEPTVITGLPH 418
Cdd:cd07087 252 IKDELIEELK---KAIKEFYGEDPKESPDYGRIINERHFDRLASLLD-----DGKVVIGGQV-DKEERYIAPTILDDVSP 322
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 24666674 419 DASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTEN 462
Cdd:cd07087 323 DSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSED 366
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
86-521 |
3.42e-30 |
|
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: 122.73 E-value: 3.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 86 LEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGkiysegQGEVQEFiDICDYAVGLSriYSGQ 165
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTG------KGWMFAE-NICGDQVQLR--ARAF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 166 LINSERADHSILEA-------------WrPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVSVATTKIV 232
Cdd:cd07084 72 VIYSYRIPHEPGNHlgqglkqqshgyrW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 233 AEVLRrnnLPP-VVTLCQGGTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVqrRFGKVILELGGNNALIIDESANvkmA 311
Cdd:cd07084 151 HYAGL---LPPeDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQ---A 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 312 LDAALFGCIGT----SGQRCTTTRRIIVHEKLHDQFVkelvgkYKQLISKIGHQLEAQTLVGPVHTqqnvENYKAAIAEA 387
Cdd:cd07084 223 VDYVAWQCVQDmtacSGQKCTAQSMLFVPENWSKTPL------VEKLKALLARRKLEDLLLGPVQT----FTTLAMIAHM 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 388 KSLGGT-VAFGGNV---IQRDGFY---VEPTVItgLPHDAS-----VVHRETFAPIVYILKAKNvDQAIEWNNEVEQG-- 453
Cdd:cd07084 293 ENLLGSvLLFSGKElknHSIPSIYgacVASALF--VPIDEIlktyeLVTEEIFGPFAIVVEYKK-DQLALVLELLERMhg 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24666674 454 -LSSAIFTENIGQAFKWIGAKGSDCGIVNINTTTNGAEIGGAFGGEKATGGGRES--GSDAWKQYCKRATI 521
Cdd:cd07084 370 sLTAAIYSNDPIFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGigGPEAIKLVWRCHAE 440
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
180-462 |
3.97e-28 |
|
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: 116.94 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 180 WRPLGVVGVISAYNFP-----NAVFGwnaAIAltTGNSVLWKgaPSTplVSVATTKIVAEVLRR---NNLPPVVTlcqGG 251
Cdd:cd07132 98 KEPLGVVLIIGAWNYPlqltlVPLVG---AIA--AGNCVVIK--PSE--VSPATAKLLAELIPKyldKECYPVVL---GG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 252 TDVGQTLVaDKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTR 331
Cdd:cd07132 166 VEETTELL-KQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 332 RIIVHEKLHDQFVKELvgkyKQLISKI-GHQLEAQTLVGPVHTQQNVENYKAAIaeaksLGGTVAFGGNVIQRDGfYVEP 410
Cdd:cd07132 245 YVLCTPEVQEKFVEAL----KKTLKEFyGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVAIGGQTDEKER-YIAP 314
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24666674 411 TVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTEN 462
Cdd:cd07132 315 TVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN 366
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
182-462 |
2.22e-27 |
|
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: 114.50 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 182 PLGVVGVISAYNFP-NAVFGwNAAIALTTGNSVLWKGAPSTPlvsvATTKIVAEVLRRNNLPPVVTLCQGGTDVGQTLVA 260
Cdd:cd07133 101 PLGVVGIIVPWNYPlYLALG-PLIAALAAGNRVMIKPSEFTP----RTSALLAELLAEYFDEDEVAVVTGGADVAAAFSS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 261 ---DKrvnLVsFTGSCQTGRdvgvEVQRRFGK----VILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRI 333
Cdd:cd07133 176 lpfDH---LL-FTGSTAVGR----HVMRAAAEnltpVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 334 IVHEKLHDQFVKELVGKYKQLISKIghqLEAQTLVGPVhTQQNVENYKAAIAEAKSLGGTV---AFGGNVIQRDGFYVeP 410
Cdd:cd07133 248 LVPEDKLEEFVAAAKAAVAKMYPTL---ADNPDYTSII-NERHYARLQGLLEDARAKGARVielNPAGEDFAATRKLP-P 322
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24666674 411 TVITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTEN 462
Cdd:cd07133 323 TLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGED 374
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
182-508 |
9.98e-26 |
|
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: 109.81 E-value: 9.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 182 PLGVVGVISAYNFP-----NAVFGwnaaiALTTGNSVLWKGAPSTPLVSVATTKIVAEVLRrnnlPPVVTLCQGGTDVGQ 256
Cdd:cd07137 101 PLGVVLVISAWNFPfllslEPVIG-----AIAAGNAVVLKPSELAPATSALLAKLIPEYLD----TKAIKVIEGGVPETT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 257 TLVaDKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGT-SGQRCTTTRRIIV 335
Cdd:cd07137 172 ALL-EQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 336 HEklhdQFVKELVGKYKQLISKIGHQ--LEAQTLVGPV--HTQQNVENykaaIAEAKSLGGTVAFGGNvIQRDGFYVEPT 411
Cdd:cd07137 251 EE----SFAPTLIDALKNTLEKFFGEnpKESKDLSRIVnsHHFQRLSR----LLDDPSVADKIVHGGE-RDEKNLYIEPT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 412 VITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENiGQAFKWIGAKGSDCGIVNINTTTNGAEI 491
Cdd:cd07137 322 ILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKN-KELKRRIVAETSSGGVTFNDTVVQYAID 400
|
330
....*....|....*..
gi 24666674 492 GGAFGGEKATGGGRESG 508
Cdd:cd07137 401 TLPFGGVGESGFGAYHG 417
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
182-468 |
1.45e-21 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 97.87 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 182 PLGVVGVISAYNFP-----NAVFGwnaaiALTTGNSVLWKGAPSTPlvsvATTKIVAEVLRRNNLPPVVTLCQGGTDVGQ 256
Cdd:PLN02203 108 PLGVVLIFSSWNFPiglslEPLIG-----AIAAGNAVVLKPSELAP----ATSAFLAANIPKYLDSKAVKVIEGGPAVGE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 257 TLVaDKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIID---ESANVKMALDAALFGCIGT-SGQRCTTTRR 332
Cdd:PLN02203 179 QLL-QHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScAGQACIAIDY 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 333 IIVHEKLHDQFVKELVGKYKQLISKIGHQLEAQTLVGPVHTQQNVENYkaaiAEAKSLGGTVAFGGNvIQRDGFYVEPTV 412
Cdd:PLN02203 258 VLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNL----LKDPRVAASIVHGGS-IDEKKLFIEPTI 332
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 24666674 413 ITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENigQAFK 468
Cdd:PLN02203 333 LLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNN--EKLK 386
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
54-462 |
4.98e-19 |
|
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: 90.02 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 54 SGQWQ-GRGPSVTSYDPGTGQPIAKVrqgnvqeleHTIGLAVEAYKQW-RQVPAPV--------RGEIVRQIGDELRKYK 123
Cdd:cd07128 6 AGQWHaGTGDGRTLHDAVTGEVVARV---------SSEGLDFAAAVAYaREKGGPAlraltfheRAAMLKALAKYLMERK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 124 EPLGKLVslevgkiYSEGQGEVQEFIDIcDYAVGLSRIYSG---QLINSEradHSILEA----------------WRPLG 184
Cdd:cd07128 77 EDLYALS-------AATGATRRDSWIDI-DGGIGTLFAYASlgrRELPNA---HFLVEGdveplskdgtfvgqhiLTPRR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 185 VVGV-ISAYNFPnaVFGW--NAAIALTTGNSVLWKGAPSTPLVsvaTTKIVAEVLRRNNLPP--VVTLCQGGTDVGQTLV 259
Cdd:cd07128 146 GVAVhINAFNFP--VWGMleKFAPALLAGVPVIVKPATATAYL---TEAVVKDIVESGLLPEgaLQLICGSVGDLLDHLG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 260 ADkrvNLVSFTGSCQTGRDVGVE--VQRRFGKVILELGGNNALIIDESANVKMAlDAALF------GCIGTSGQRCTTTR 331
Cdd:cd07128 221 EQ---DVVAFTGSAATAAKLRAHpnIVARSIRFNAEADSLNAAILGPDATPGTP-EFDLFvkevarEMTVKAGQKCTAIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 332 RIIVHEKLHDQFVKELVGKYKQLisKIGHQLEAQTLVGPVHTQQNVENYKAAIAEAKSlGGTVAFGGN-------VIQRD 404
Cdd:cd07128 297 RAFVPEARVDAVIEALKARLAKV--VVGDPRLEGVRMGPLVSREQREDVRAAVATLLA-EAEVVFGGPdrfevvgADAEK 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 405 GFYVEPTVITGL-PHDASVVHR-ETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTEN 462
Cdd:cd07128 374 GAFFPPTLLLCDdPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
182-521 |
8.20e-19 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 89.33 E-value: 8.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 182 PLGVVGVISAYNFP-----NAVFGwnaaiALTTGNSVLWKGAPSTPLVSVATTKIVAEVLRrnnlPPVVTLCQGGTDVGQ 256
Cdd:PLN02174 112 PLGVVLVISAWNYPfllsiDPVIG-----AISAGNAVVLKPSELAPASSALLAKLLEQYLD----SSAVRVVEGAVTETT 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 257 TLVaDKRVNLVSFTGSCQTGRDVGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIG-TSGQRCTTTRRIIV 335
Cdd:PLN02174 183 ALL-EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 336 HE----KLHDQFVKELVGKYKQliskigHQLEAQTLVGPVHTqqNVENYKAAIAEAKSLGGTVAFGGNViQRDGFYVEPT 411
Cdd:PLN02174 262 TKeyapKVIDAMKKELETFYGK------NPMESKDMSRIVNS--THFDRLSKLLDEKEVSDKIVYGGEK-DRENLKIAPT 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 412 VITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGLSSAIFTENiGQAFKWIGAKGSDCGIVNINTTTNGAEI 491
Cdd:PLN02174 333 ILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHN-KKLKERFAATVSAGGIVVNDIAVHLALH 411
|
330 340 350
....*....|....*....|....*....|
gi 24666674 492 GGAFGGEKATGGGRESGSDAWKQYCKRATI 521
Cdd:PLN02174 412 TLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
92-461 |
8.15e-17 |
|
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: 82.97 E-value: 8.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 92 LAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGkiYSEG--QGEVqefidicDYAVGLSRIYSGQLINS 169
Cdd:cd07129 7 AAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEArlQGEL-------GRTTGQLRLFADLVREG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 170 E----RADHSILEAW-----------RPLGVVGVISAYNFPNA--VFGWNAAIALTTGNSVLWKGAPSTPLVSVATTKIV 232
Cdd:cd07129 78 SwldaRIDPADPDRQplprpdlrrmlVPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAHPAHPGTSELVARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 233 AEVLRRNNLPP-VVTLCQG-GTDVGQTLVADKRVNLVSFTGSCQTGRDVGVEVQRR------FGkvilELGGNNALIIDE 304
Cdd:cd07129 158 RAALRATGLPAgVFSLLQGgGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARpepipfYA----ELGSVNPVFILP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 305 SA--NVKMALDAALFG-CIGTSGQRCTTTRRIIVHE-KLHDQFVkelvgkyKQLISKIGHQlEAQTLVGP-VHtqqnvEN 379
Cdd:cd07129 234 GAlaERGEAIAQGFVGsLTLGAGQFCTNPGLVLVPAgPAGDAFI-------AALAEALAAA-PAQTMLTPgIA-----EA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 380 YKAAIAEAKSLGGTVAFGGNVIQRDGFYVEPTVITglpHDAS------VVHRETFAPIVYILKAKNVDQAIEWNNEVEQG 453
Cdd:cd07129 301 YRQGVEALAAAPGVRVLAGGAAAEGGNQAAPTLFK---VDAAafladpALQEEVFGPASLVVRYDDAAELLAVAEALEGQ 377
|
....*...
gi 24666674 454 LSSAIFTE 461
Cdd:cd07129 378 LTATIHGE 385
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
182-445 |
3.42e-16 |
|
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: 81.37 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 182 PLGVVGVISAYNFPNavfgWNAA----IALTTGNSVLWKGAPSTPLVSVATTKIVAEVLRRNNLPP-VVTLC--QGGTDV 254
Cdd:cd07127 193 PRGVALVIGCSTFPT----WNGYpglfASLATGNPVIVKPHPAAILPLAITVQVAREVLAEAGFDPnLVTLAadTPEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 255 GQTLVADKRVNLVSFTGSCQTGRdvGVEVQRRFGKVILELGGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRII 334
Cdd:cd07127 269 AQTLATRPEVRIIDFTGSNAFGD--WLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIY 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 335 V---------HEKLHDQFVKELVGKYKQLiskIGHQLEAQTLVGPVhtqQNvENYKAAIAEAKSLGGtVAFGGNVIQRDG 405
Cdd:cd07127 347 VprdgiqtddGRKSFDEVAADLAAAIDGL---LADPARAAALLGAI---QS-PDTLARIAEARQLGE-VLLASEAVAHPE 418
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 24666674 406 F----YVEPTVITGLPHDASVVHRETFAPIVYILKAKNVDQAIE 445
Cdd:cd07127 419 FpdarVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIE 462
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
69-463 |
1.14e-11 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 66.85 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 69 PGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGkiysegQGEVQEF 148
Cdd:PRK15398 21 QTVSPPAAVGEMGVFASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETG------MGRVEDK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 149 IDICDYAVGLS--------RIYSGqlinseraDHSI-LEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAP 219
Cdd:PRK15398 95 IAKNVAAAEKTpgvedlttEALTG--------DNGLtLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 220 STPLVSVATTKIVAEVLRRN----NLppVVTLCQGGTDVGQTLVADKRVNLVSFTGscqtGRDVgVEVQRRFGK-VILEL 294
Cdd:PRK15398 167 GAKKVSLRAIELLNEAIVAAggpeNL--VVTVAEPTIETAQRLMKHPGIALLVVTG----GPAV-VKAAMKSGKkAIGAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 295 GGNNALIIDESANVKMALDAALFGCIGTSGQRCTTTRRIIVHEKLHDQFVKELV--GKYkQLISKIGHQLEAQTLVGPVH 372
Cdd:PRK15398 240 AGNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEknGAV-LLTAEQAEKLQKVVLKNGGT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 373 TQQNVENyKAAIAEAKSLGGTVAFGGNVIqrdgfyveptvITGLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQ 452
Cdd:PRK15398 319 VNKKWVG-KDAAKILEAAGINVPKDTRLL-----------IVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEH 386
|
410
....*....|...
gi 24666674 453 GL--SSAIFTENI 463
Cdd:PRK15398 387 GNrhTAIMHSRNV 399
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
86-465 |
5.56e-11 |
|
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: 64.59 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 86 LEHTIGLAVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVGkiysegQGEVQE-FIDICDYAVGLSRIYSG 164
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETG------MGRVEDkVIKNHFAAEYIYNVYKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 165 QL---INSERADHSILEAWRPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVSVATTKIVAEVLRRNNL 241
Cdd:cd07081 75 EKtcgVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 242 PP--VVTLCQGGTDVGQTLVADKRVNLVSFTGscqtGRDVgVEVQRRFGKVILELG-GNNALIIDESANVKMALDAALFG 318
Cdd:cd07081 155 PEnlIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAV-VKAAYSSGKPAIGVGaGNTPVVIDETADIKRAVQSIVKS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 319 CIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLISkiGHQLEAqtlVGPVHTQQNVENYKAAIAEAKSLGGTVAFgg 398
Cdd:cd07081 230 KTFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLT--AEELQQ---VQPVILKNGDVNRDIVGQDAYKIAAAAGL-- 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24666674 399 NVIQRDG-FYVEPTVITGLPHDASvvhrETFAPIVYILKAKNVDQAIE----WNNEVEQGLSSAIFTENIGQ 465
Cdd:cd07081 303 KVPQETRiLIGEVTSLAEHEPFAH----EKLSPVLAMYRAANFADADAkalaLKLEGGCGHTSAMYSDNIKA 370
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
93-463 |
7.25e-11 |
|
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: 64.18 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 93 AVEAYKQWRQVPAPVRGEIVRQIGDELRKYKEPLGKLVSLEVG------KIYS-EGQGEVQEFIDICDYAV-----GLSR 160
Cdd:cd07121 13 AKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGmgrvedKIAKnHLAAEKTPGTEDLTTTAwsgdnGLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 161 IysgqlinsERAdhsileawrPLGVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVSVATTKIVAEVLRRNN 240
Cdd:cd07121 93 V--------EYA---------PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 241 LPP--VVTLCQGGTDVGQTLVADKRVNLVsftgsCQTGRDVGVEVQRRFGK-VILELGGNNALIIDESANVKMALDAALF 317
Cdd:cd07121 156 GPDnlVVTVEEPTIETTNELMAHPDINLL-----VVTGGPAVVKAALSSGKkAIGAGAGNPPVVVDETADIEKAARDIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 318 GCIGTSGQRCTTTRRIIVHEKLHDQFVKELVGKYKQLISkiGHQLEAQTLVGPVHTQQNVENY----KAAIAEAKSLGGT 393
Cdd:cd07121 231 GASFDNNLPCIAEKEVIAVDSVADYLIAAMQRNGAYVLN--DEQAEQLLEVVLLTNKGATPNKkwvgKDASKILKAAGIE 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24666674 394 VAFGGNVIqrdgfYVEptvitgLPHDASVVHRETFAPIVYILKAKNVDQAIEWNNEVEQGL--SSAIFTENI 463
Cdd:cd07121 309 VPADIRLI-----IVE------TDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNV 369
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
55-445 |
1.65e-10 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 63.57 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 55 GQWQ-GRGPSVTSYDPGTGQPIAKVRQGNVqELEHTIGLAVE---------AYKQwrqvpapvRGEIVRQIGDELRKYKE 124
Cdd:PRK11903 11 GRWQaGSGAGTPLFDPVTGEELVRVSATGL-DLAAAFAFAREqggaalralTYAQ--------RAALLAAIVKVLQANRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 125 PLGKLV-----------SLEV-GKIYSEGQ--------GEVQEFIDICDYAVGLSRIYSGQLInseradhsileaWRPL- 183
Cdd:PRK11903 82 AYYDIAtansgttrndsAVDIdGGIFTLGYyaklgaalGDARLLRDGEAVQLGKDPAFQGQHV------------LVPTr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 184 GVVGVISAYNFPNAVFGWNAAIALTTGNSVLWKGAPSTPLVsvaTTKIVAEVLRRNNLPP--VVTLCQGGTDVgqtLVAD 261
Cdd:PRK11903 150 GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWL---TQRMVKDVVAAGILPAgaLSVVCGSSAGL---LDHL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 262 KRVNLVSFTGSCQTGRDVGVE--VQRRFGKVILELGG-NNALIIDESANVKMALDAALFGCIG----TSGQRCTTTRRII 334
Cdd:PRK11903 224 QPFDVVSFTGSAETAAVLRSHpaVVQRSVRVNVEADSlNSALLGPDAAPGSEAFDLFVKEVVRemtvKSGQKCTAIRRIF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 335 VHEKLHDQFVKELVGKYKQLIskIGHQLEAQTLVGPVHTQQNVENYKAAIAEAKSlGGTVAFGGNV---IQRD---GFYV 408
Cdd:PRK11903 304 VPEALYDAVAEALAARLAKTT--VGNPRNDGVRMGPLVSRAQLAAVRAGLAALRA-QAEVLFDGGGfalVDADpavAACV 380
|
410 420 430
....*....|....*....|....*....|....*....
gi 24666674 409 EPTVI-TGLPHDASVVH-RETFAPIVYILKAKNVDQAIE 445
Cdd:PRK11903 381 GPTLLgASDPDAATAVHdVEVFGPVATLLPYRDAAHALA 419
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
54-463 |
2.18e-09 |
|
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: 59.82 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 54 SGQWQGRGPSVTSYDPGTGQPIAKVRQGNVQELEHTIGLAVEAYKQWRQVP--APVR----GEIVRQIGDELRKYK--EP 125
Cdd:cd07126 4 AGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPlkNPERyllyGDVSHRVAHELRKPEveDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 126 LGKLVSLEVGKIYSEGQGEV---QEFI-----DICDYavgLSRIYS------GQLINSERadhsileaWrPLGVVGVISA 191
Cdd:cd07126 84 FARLIQRVAPKSDAQALGEVvvtRKFLenfagDQVRF---LARSFNvpgdhqGQQSSGYR--------W-PYGPVAIITP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 192 YNFPNAVFGWNAAIALTTGNSVLWKGAPStplVSVATTKIVaEVLRRNNLPPV-VTLCQGGTDVGQTLVADKRVNLVSFT 270
Cdd:cd07126 152 FNFPLEIPALQLMGALFMGNKPLLKVDSK---VSVVMEQFL-RLLHLCGMPATdVDLIHSDGPTMNKILLEANPRMTLFT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 271 GSCQTGRDVGVEVQrrfGKVILELGGNNALI----IDESANVKMALDAALFGCigtSGQRCTTTRRIIVHEKLHDQfvkE 346
Cdd:cd07126 228 GSSKVAERLALELH---GKVKLEDAGFDWKIlgpdVSDVDYVAWQCDQDAYAC---SGQKCSAQSILFAHENWVQA---G 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 347 LVGKYKQLISKigHQLEAQTlVGPVHTQQNvenyKAAIAEAKSL----GGTVAFGG------NVIQRDGFYvEPTVI--- 413
Cdd:cd07126 299 ILDKLKALAEQ--RKLEDLT-IGPVLTWTT----ERILDHVDKLlaipGAKVLFGGkpltnhSIPSIYGAY-EPTAVfvp 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 24666674 414 ---TGLPHDASVVHRETFAP--IVYILKAKNVDQAIEWNNEVEQGLSSAIFTENI 463
Cdd:cd07126 371 leeIAIEENFELVTTEVFGPfqVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDI 425
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
182-348 |
2.83e-07 |
|
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).
Pssm-ID: 143398 Cd Length: 406 Bit Score: 52.82 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 182 PLGVVGVIsaY-NFPN----AvfgwnAAIALTTGNSVLWKGAPSTPLVSVATTKIVAEVLRRNNLPP-VVTL--CQGGTD 253
Cdd:cd07079 109 PLGVIGII--YeSRPNvtvdA-----AALCLKSGNAVILRGGSEALHSNRALVEIIQEALEEAGLPEdAVQLipDTDREA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 254 VGQTLVADKRVNLV------SFTGSCQTGRDVgvevqrrfgKVILELGGNNALIIDESANVKMALDAALFGCIgtsgQR- 326
Cdd:cd07079 182 VQELLKLDDYIDLIiprggaGLIRFVVENATI---------PVIKHGDGNCHVYVDESADLEMAVRIVVNAKT----QRp 248
|
170 180
....*....|....*....|....
gi 24666674 327 --CTTTRRIIVHEKLHDQFVKELV 348
Cdd:cd07079 249 svCNALETLLVHRDIAEEFLPKLA 272
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
182-352 |
8.28e-07 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 51.22 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 182 PLGVVGVIsaynF---PNAVFGwNAAIALTTGNSVLWKGAPSTPLVSVATTKIVAEVLRRNNLPP-VVTLCQgGTD---V 254
Cdd:PRK00197 115 PLGVIGVI----YesrPNVTVD-AAALCLKSGNAVILRGGSEAIHSNRALVAVIQEALEEAGLPAdAVQLVE-TTDraaV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 255 GQTLVADKRVNLV------SFTGSCQTGRDVgvevqrrfgKVILELGGNNALIIDESANVKMALDAALFGCIgtsgQR-- 326
Cdd:PRK00197 189 GELLKLDGYVDVIiprggaGLIRRVVENATV---------PVIEHGDGICHIYVDESADLDKALKIVLNAKT----QRps 255
|
170 180
....*....|....*....|....*..
gi 24666674 327 -CTTTRRIIVHEKLHDQFVKELVGKYK 352
Cdd:PRK00197 256 vCNALETLLVHEAIAEEFLPKLAEALA 282
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
169-462 |
1.44e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 50.57 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 169 SERADHSILEAWRPLGVV-GVISAYNfP--NAVFgwNAAIALTTGNSVLWKGAPSTPLVSVATTKIVAEVLRRNNLPP-- 243
Cdd:cd07122 82 EEDEEKGIVEIAEPVGVIaALIPSTN-PtsTAIF--KALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGAPEgl 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 244 VVTLCQGGTDVGQTLVADKRVNLVSFTG---------SCqtgrdvgvevqrrfGKVILELG-GNNALIIDESANVKMA-- 311
Cdd:cd07122 159 IQWIEEPSIELTQELMKHPDVDLILATGgpgmvkaaySS--------------GKPAIGVGpGNVPAYIDETADIKRAvk 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 312 --LDAALFGCiGTSgqrCTTTRRIIVHEKLHDQFVKELV--GKY------KQLISKI----GHQLEAQTlVGpvhtqqnv 377
Cdd:cd07122 225 diILSKTFDN-GTI---CASEQSVIVDDEIYDEVRAELKrrGAYflneeeKEKLEKAlfddGGTLNPDI-VG-------- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666674 378 enyKAAIAEAKSLGGTVAFGGNVIqrdgfYVEPTVItGLPHDASvvhRETFAPIVYILKAKNVDQAIEWNNEVEQ----G 453
Cdd:cd07122 292 ---KSAQKIAELAGIEVPEDTKVL-----VAEETGV-GPEEPLS---REKLSPVLAFYRAEDFEEALEKARELLEyggaG 359
|
....*....
gi 24666674 454 LSSAIFTEN 462
Cdd:cd07122 360 HTAVIHSND 368
|
|
| |
