|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
1-508 |
0e+00 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 1020.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 1 MGSANNEYEFLSEIGLTSHNLGSYVAGKWQANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKR 80
Cdd:PLN02315 1 MGFARKEYEFLSEIGLSSRNLGCYVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 81 GDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGV 160
Cdd:PLN02315 81 GEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 161 ITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLV 240
Cdd:PLN02315 161 ITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 241 SFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQL 320
Cdd:PLN02315 241 SFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 321 LTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIEISADAAVVKEELFAP 400
Cdd:PLN02315 321 LTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVEISPDADVVKEELFGP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 401 VLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSD 480
Cdd:PLN02315 401 VLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSD 480
|
490 500
....*....|....*....|....*...
gi 30695661 481 SWKQYMRRSTCTINYGNELPLAQGINFG 508
Cdd:PLN02315 481 SWKQYMRRSTCTINYGNELPLAQGINFG 508
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
24-496 |
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: 913.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 24 YVAGKWQANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLS 103
Cdd:cd07130 2 VYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 104 LEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGN 183
Cdd:cd07130 82 LEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 184 CVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKT 263
Cdd:cd07130 162 VVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 264 LLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLH 343
Cdd:cd07130 242 LLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 344 TPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIEISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQG 423
Cdd:cd07130 322 TKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQG 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695661 424 LSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTINYG 496
Cdd:cd07130 402 LSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
23-496 |
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: 849.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 23 SYVAGKWQANG-PLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:cd07086 1 GVIGGEWVGSGgETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 102 LSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 182 GNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSG 261
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 262 KTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGP 341
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 342 LHTPESKKNFEKGIEVIKSQGGKILTGGKAVEG--EGNFVEPTIIEISA-DAAVVKEELFAPVLYVLKFKSFGEAVAINN 418
Cdd:cd07086 321 LINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTdDARIVQEETFAPILYVIKFDSLEEAIAINN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30695661 419 SVPQGLSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTINYG 496
Cdd:cd07086 401 DVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
17-495 |
2.93e-171 |
|
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: 491.56 E-value: 2.93e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 17 TSHNLGSYVAGKWQ--ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSK 94
Cdd:COG1012 2 TTPEYPLFIGGEWVaaASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 95 LDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWN 174
Cdd:COG1012 82 REELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 175 ACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLP-GAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQ 253
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEA----GLPaGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 254 QTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPL 333
Cdd:COG1012 238 AAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 334 EKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGE-GNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFG 411
Cdd:COG1012 318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEgGYFVEPTVLAdVTPDMRIAREEIFGPVLSVIPFDDEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 412 EAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTC 491
Cdd:COG1012 398 EAIALANDTEYGLAASVFTRDLARARRVARRL--EAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTV 475
|
....
gi 30695661 492 TINY 495
Cdd:COG1012 476 TIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
31-490 |
3.81e-166 |
|
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: 477.79 E-value: 3.81e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 31 ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKIL 110
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 111 AEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSeRPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGA 190
Cdd:pfam00171 84 AEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 191 PTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSG 269
Cdd:pfam00171 163 ELTPLTALLLAELFEEA----GLPAGVLNVVTGsGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 270 NNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKK 349
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 350 NFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSI 428
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLAnVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30695661 429 FTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRST 490
Cdd:pfam00171 399 FTSDLERALRVARRL--EAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
59-493 |
2.15e-150 |
|
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: 436.64 E-value: 2.15e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 59 EQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSV 138
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 139 IPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLeknnLPGAIF 218
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAG----LPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 219 TAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAG 297
Cdd:cd07078 157 NVVTGdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 298 QRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGE-G 376
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGkG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 377 NFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIP 455
Cdd:cd07078 317 YFVPPTVLTdVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERL--EAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 30695661 456 TNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTI 493
Cdd:cd07078 395 SVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
23-496 |
1.04e-135 |
|
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: 400.96 E-value: 1.04e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 23 SYVAGKW--QANGPLVSTLNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:cd07131 1 NYIGGEWvdSASGETFDSRNPADlEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 100 RLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIAL 179
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 180 VCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVnA 258
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKL----VELFAEAGLPPGVVNVVHGrGEEVGEALVEHPDVDVVSFTGSTEVGERIGETC-A 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 259 RSGKTL-LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGT 337
Cdd:cd07131 236 RPNKRVaLEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 338 LLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEG----EGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGE 412
Cdd:cd07131 316 DMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTdVTPDMRIAQEEIFGPVVALIEVSSLEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 413 AVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGG-REAGSDSWKQYMRRSTC 491
Cdd:cd07131 396 AIEIANDTEYGLSSAIYTEDVNKAFRARRDL--EAGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
....*
gi 30695661 492 TINYG 496
Cdd:cd07131 474 YVDYS 478
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
23-480 |
2.33e-126 |
|
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: 376.97 E-value: 2.33e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 23 SYVAGKWQANGPLVSTLNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:cd07097 3 NYIDGEWVAGGDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 102 LSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:cd07097 83 LTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 182 GNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARS 260
Cdd:cd07097 163 GNTVVFKPAELTPASAWAL----VEILEEAGLPAGVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 261 GKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLG 340
Cdd:cd07097 239 ARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 341 PLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEG--EGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAIN 417
Cdd:cd07097 319 PVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRpdEGYYLAPALFAgVTNDMRIAREEIFGPVAAVIRVRDYDEALAIA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695661 418 NSVPQGLSSSIFTRNPENIFRWIGplGSDCGIVNVNIPTNGAEIGGAFGGEKATG-GGREAGSD 480
Cdd:cd07097 399 NDTEFGLSAGIVTTSLKHATHFKR--RVEAGVVMVNLPTAGVDYHVPFGGRKGSSyGPREQGEA 460
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
63-493 |
5.26e-116 |
|
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: 346.52 E-value: 5.26e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 63 KACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSE 142
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 143 RPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLeknnLPGAIFTAMC 222
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAG----LPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 223 G-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCT 301
Cdd:cd06534 157 GgGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 302 TCRRLLLHESVYDKVLEQLLTsykqvkignplekgtllgplhtpeskknfekgieviksqggkILTGgkavegegnfvep 381
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLVT------------------------------------------VLVD------------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 382 tiieISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEI 461
Cdd:cd06534 262 ----VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERL--RAGTVYINDSSIGVGP 335
|
410 420 430
....*....|....*....|....*....|..
gi 30695661 462 GGAFGGEKATGGGREAGSDSWKQYMRRSTCTI 493
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
39-486 |
6.76e-110 |
|
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: 333.63 E-value: 6.76e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQ 118
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 119 EVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITI 198
Cdd:cd07103 82 YAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 199 AMtklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQtvnaRSGKTL----LELSGNNAI 273
Cdd:cd07103 162 AL----AELAEEAGLPAGVLNVVTGsPAEIGEALCASPRVRKISFTGSTAVGKLLMA----QAADTVkrvsLELGGNAPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 274 IVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEK 353
Cdd:cd07103 234 IVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 354 GIEVIKSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRN 432
Cdd:cd07103 314 LVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLtDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 30695661 433 PENIFRwigpLGS--DCGIVNVNIPTngaeIGGA---FGGEKATGGGREAGSDSWKQYM 486
Cdd:cd07103 394 LARAWR----VAEalEAGMVGINTGL----ISDAeapFGGVKESGLGREGGKEGLEEYL 444
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
24-490 |
2.33e-105 |
|
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: 322.68 E-value: 2.33e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 24 YVAGKW--QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:cd07088 1 YINGEFvpSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 102 LSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 182 GNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARS 260
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEA----GLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 261 GKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLG 340
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 341 PLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGE-GNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINN 418
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEkGYFYEPTVLTnVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAN 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30695661 419 SVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPtNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRST 490
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNEL--EFGETYINRE-NFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKV 465
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
38-487 |
3.83e-102 |
|
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: 314.10 E-value: 3.83e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 38 TLNPANNQPIAQVVEASLEDYEQGLKACEEA--AKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIG 115
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 116 EVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPL 195
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 196 ITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAII 274
Cdd:cd07114 161 STLELAKLAEEA----GFPPGVVNVVTGfGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 275 VMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKG 354
Cdd:cd07114 237 VFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 355 IEVIKSQGGKILTGGKAVEGE----GNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIF 429
Cdd:cd07114 317 VARAREEGARVLTGGERPSGAdlgaGYFFEPTILAdVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIW 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 30695661 430 TRNPENIFRWIGPLgsDCGIVNVNipTNGA-EIGGAFGGEKATGGGREAGSDSWKQYMR 487
Cdd:cd07114 397 TRDLARAHRVARAI--EAGTVWVN--TYRAlSPSSPFGGFKDSGIGRENGIEAIREYTQ 451
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
24-495 |
1.44e-100 |
|
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: 311.85 E-value: 1.44e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 24 YVAGKWQANGPLVSTLNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLL 102
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 103 SLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLeMWNPLGIVGVITAFNFPCAVLGWNACIALVCG 182
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRY-VYRPLGVGAVISPWNFPLAILAGMTTAALVTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 183 NCVVWKGAPTTPLITiamtKLVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGsmvqQTVNARSG 261
Cdd:cd07124 195 NTVVLKPAEDTPVIA----AKLVEILEEAGLPPGVVNFLPGpGEEVGDYLVEHPDVRFIAFTGSREVG----LRIYERAA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 262 KT----------LLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGN 331
Cdd:cd07124 267 KVqpgqkwlkrvIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 332 PLEKGTLLGPLHTPESKKNFEKGIEVIKsQGGKILTGGK--AVEGEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFK 408
Cdd:cd07124 347 PEDPEVYMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEvlELAAEGYFVQPTIFAdVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 409 SFGEAVAINNSVPQGLSSSIFTRNPENI---FRWIgplgsDCGIVNVNIPTNGAEIG-GAFGGEKATG-GGREAGSDSWK 483
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLeraRREF-----EVGNLYANRKITGALVGrQPFGGFKMSGtGSKAGGPDYLL 500
|
490
....*....|..
gi 30695661 484 QYMRRSTCTINY 495
Cdd:cd07124 501 QFMQPKTVTENF 512
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
57-485 |
3.17e-100 |
|
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: 308.31 E-value: 3.17e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 57 DYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNG 136
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 137 SVIPSERPNHMMLEMWNPLGIVGVITAFNFPcAVLGWNA-CIALVCGNCVVWKGAPTTPlITIAMtkLVAEVLEKNNLPG 215
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFP-LILAMRSvAPALALGNAVVLKPDSRTP-VTGGL--LIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 216 AIFTAM-CGGAEIGEAIAKDTRIPLVSFTGSSRVGsmvqQTVNARSGKTL----LELSGNNAIIVMDDADIQLAARSVLF 290
Cdd:cd07104 157 GVLNVVpGGGSEIGDALVEHPRVRMISFTGSTAVG----RHIGELAGRHLkkvaLELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 291 AAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGK 370
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 371 AvegEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRwIGpLGSDCGI 449
Cdd:cd07104 313 Y---EGLFYQPTVLsDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMA-FA-ERLETGM 387
|
410 420 430
....*....|....*....|....*....|....*.
gi 30695661 450 VNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQY 485
Cdd:cd07104 388 VHINDQTVNDEPHVPFGGVKASGGGRFGGPASLEEF 423
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
39-481 |
6.74e-98 |
|
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: 303.10 E-value: 6.74e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQ 118
Cdd:cd07150 4 LNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 119 EVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPcAVLGWNA-CIALVCGNCVVWKGAPTTPLIT 197
Cdd:cd07150 84 FTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYP-LILATKKvAFALAAGNTVVLKPSEETPVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 198 IamtkLVAEVLEKNNLPGAIFTAM-CGGAEIGEAIAKDTRIPLVSFTGSSRVGSMvqqtVNARSGKTL----LELSGNNA 272
Cdd:cd07150 163 L----KIAEIMEEAGLPKGVFNVVtGGGAEVGDELVDDPRVRMVTFTGSTAVGRE----IAEKAGRHLkkitLELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 273 IIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFE 352
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 353 KGIEVIKSQGGKILTGGKaveGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTR 431
Cdd:cd07150 315 RQVEDAVAKGAKLLTGGK---YDGNFYQPTVLtDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 30695661 432 NPENIFRWIgpLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDS 481
Cdd:cd07150 392 DLQRAFKLA--ERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWS 439
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
38-485 |
4.45e-95 |
|
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: 295.89 E-value: 4.45e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEG-IGE 116
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 117 VQEVIDMCDFAVGLSRQLNGSVIPSERP--NHMMLEmwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPflNYTVRE---PVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 195 LITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAI 273
Cdd:cd07115 158 LSALRIAELMAEA----GFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 274 IVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEK 353
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 354 GIEVIKSQGGKILTGGKAVEGEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRN 432
Cdd:cd07115 314 YVDVGREEGARLLTGGKRPGARGFFVEPTIFAaVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 30695661 433 PENIFRWIGPLGSdcGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQY 485
Cdd:cd07115 394 LGRAHRVAAALKA--GTVWINT-YNRFDPGSPFGGYKQSGFGREMGREALDEY 443
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
39-490 |
7.29e-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: 294.82 E-value: 7.29e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQ 118
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 119 EVIDMCDFAVGLSRQlngSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITI 198
Cdd:cd07106 82 GAVAWLRYTASLDLP---DEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 199 AMTKLVAEVLeknnlPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGsmvqQTVNARSGKTL----LELSGNNAII 274
Cdd:cd07106 159 KLGELAQEVL-----PPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATG----KKVMASAAKTLkrvtLELGGNDAAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 275 VMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTpesKKNFEKG 354
Cdd:cd07106 230 VLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQN---KMQYDKV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 355 ---IEVIKSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFT 430
Cdd:cd07106 307 kelVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVdDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695661 431 RNPENIFRwigpLGS--DCGIVNVNiptNGAEIGGA--FGGEKATGGGREAGSDSWKQYMRRST 490
Cdd:cd07106 387 SDLERAEA----VARrlEAGTVWIN---THGALDPDapFGGHKQSGIGVEFGIEGLKEYTQTQV 443
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
36-476 |
6.98e-93 |
|
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: 290.40 E-value: 6.98e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 36 VSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIG 115
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 116 EVQEVIDMCDFAVGLSRQLNGSVIPSE----RPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAP 191
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 192 TTPLITIAMTKLVAEVleknNLP-GAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGN 270
Cdd:cd07145 161 NTPLTAIELAKILEEA----GLPpGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 271 NAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKN 350
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 351 FEKGIEVIKSQGGKILTGGKAVegEGNFVEPTIIEI-SADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIF 429
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGKRD--EGSFFPPTVLENdTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 30695661 430 TRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGGRE 476
Cdd:cd07145 395 TNDINRALKVAREL--EAGGVVINDSTRFRWDNLPFGGFKKSGIGRE 439
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
24-486 |
3.92e-92 |
|
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: 289.21 E-value: 3.92e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 24 YVAGKWQ--ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEA--AKIWMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:cd07119 1 YIDGEWVeaASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 100 RLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSerPNHMM-LEMWNPLGIVGVITAFNFPCAVLGWNACIA 178
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDV--PPHVIsRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 179 LVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVN 257
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEA----GLPAGVVNLVTGsGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 258 ARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGT 337
Cdd:cd07119 235 GNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 338 LLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEG----EGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGE 412
Cdd:cd07119 315 EMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFdDVDRTMRIVQEEIFGPVLTVERFDTEEE 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30695661 413 AVAINNSVPQGLSSSIFTRNPENIFRWIGPLGSdcGIVNVN---IPTNGAEiggaFGGEKATGGGREAGSDSWKQYM 486
Cdd:cd07119 395 AIRLANDTPYGLAGAVWTKDIARANRVARRLRA--GTVWINdyhPYFAEAP----WGGYKQSGIGRELGPTGLEEYQ 465
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
23-486 |
5.72e-92 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 289.28 E-value: 5.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 23 SYVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGR 100
Cdd:PLN02278 27 GLIGGKWTDayDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 101 LLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALV 180
Cdd:PLN02278 107 LMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 181 CGNCVVWKGAPTTPLITIAmtklVAEVLEKNNLP-GAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNAR 259
Cdd:PLN02278 187 AGCTVVVKPSELTPLTALA----AAELALQAGIPpGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 260 SGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLL 339
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 340 GPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINN 418
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLgDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAN 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695661 419 SVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVN---IPTNGAeiggAFGGEKATGGGREAGSDSWKQYM 486
Cdd:PLN02278 423 DTEAGLAAYIFTRDLQRAWRVSEAL--EYGIVGVNeglISTEVA----PFGGVKQSGLGREGSKYGIDEYL 487
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
40-476 |
3.34e-91 |
|
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: 285.64 E-value: 3.34e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 40 NPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQE 119
Cdd:cd07149 5 SPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 120 VIDMCDFAVGLSRQLNGSVIP------SErpNHMMLEMWNPLGIVGVITAFNFP----CAVLGwnacIALVCGNCVVWKG 189
Cdd:cd07149 85 AIETLRLSAEEAKRLAGETIPfdaspgGE--GRIGFTIREPIGVVAAITPFNFPlnlvAHKVG----PAIAAGNAVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 190 APTTPLITIAMtklvAEVLEKNNLPGAIFTAMCGGAE-IGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARsgKTLLELS 268
Cdd:cd07149 159 ASQTPLSALKL----AELLLEAGLPKGALNVVTGSGEtVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--KVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 269 GNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESK 348
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 349 KNFEKGIEVIKSQGGKILTGGKAvegEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSS 427
Cdd:cd07149 313 ERIEEWVEEAVEGGARLLTGGKR---DGAILEPTVLTdVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAG 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 30695661 428 IFTRNPENIFRWIGPLgsDCGIVNVN-IPTNGAEiGGAFGGEKATGGGRE 476
Cdd:cd07149 390 VFTNDLQKALKAAREL--EVGGVMINdSSTFRVD-HMPYGGVKESGTGRE 436
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
38-481 |
1.58e-90 |
|
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: 284.07 E-value: 1.58e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGI-GE 116
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 117 VQEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLi 196
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 197 TIAMtklVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVnARSGKTL-LELSGNNAII 274
Cdd:cd07093 159 TAWL---LAELANEAGLPPGVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAA-APNLKPVsLELGGKNPNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 275 VMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKG 354
Cdd:cd07093 235 VFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 355 IEVIKSQGGKILTGGKAVE----GEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIF 429
Cdd:cd07093 315 VELARAEGATILTGGGRPElpdlEGGYFVEPTVITgLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVW 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 30695661 430 TRNPENIFRWIGPLgsDCGIVNVNIPtNGAEIGGAFGGEKATGGGREAGSDS 481
Cdd:cd07093 395 TRDLGRAHRVARRL--EAGTVWVNCW-LVRDLRTPFGGVKASGIGREGGDYS 443
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
22-493 |
8.00e-86 |
|
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: 272.55 E-value: 8.00e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 22 GSYVAGKW--QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKI--WMQVTAPKRGDIVRQIGDALRSKLDY 97
Cdd:cd07091 5 GLFINNEFvdSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 98 LGRLLSLEMGKILAEGI-GEVQEVIDMCDFAVGLSRQLNGSVIPSERpNHMMLEMWNPLGIVGVITAFNFPCAVLGWNAC 176
Cdd:cd07091 85 LAALESLDNGKPLEESAkGDVALSIKCLRYYAGWADKIQGKTIPIDG-NFLAYTRREPIGVCGQIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 177 IALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQT 255
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEA----GFPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 256 VnARSG--KTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPL 333
Cdd:cd07091 240 A-AKSNlkKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 334 EKGTLLGPLhtpESKKNFEK---GIEVIKSQGGKILTGGKAVEGEGNFVEPTI-IEISADAAVVKEELFAPVLYVLKFKS 409
Cdd:cd07091 319 DPDTFQGPQ---VSKAQFDKilsYIESGKKEGATLLTGGERHGSKGYFIQPTVfTDVKDDMKIAKEEIFGPVVTILKFKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 410 FGEAVAINNSVPQGLSSSIFTRNPENIFR----------WIgplgsDC-GIVNVNIPtngaeiggaFGGEKATGGGREAG 478
Cdd:cd07091 396 EDEVIERANDTEYGLAAGVFTKDINKALRvsralkagtvWV-----NTyNVFDAAVP---------FGGFKQSGFGRELG 461
|
490
....*....|....*
gi 30695661 479 SDSWKQYMRRSTCTI 493
Cdd:cd07091 462 EEGLEEYTQVKAVTI 476
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
38-495 |
1.53e-85 |
|
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: 271.17 E-value: 1.53e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEV 117
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 118 QEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLIT 197
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVG-GRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 198 IAMTKLVAEVLEK---NNLPGaiftamcGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAII 274
Cdd:cd07107 160 LRLAELAREVLPPgvfNILPG-------DGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 275 VMDDADIQLAARSvlfAAVG----TAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKN 350
Cdd:cd07107 233 VFPDADPEAAADA---AVAGmnftWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 351 FEKGIEVIKSQGGKILTGGKAVEGE----GNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLS 425
Cdd:cd07107 310 VMHYIDSAKREGARLVTGGGRPEGPalegGFYVEPTVFaDVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLT 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 426 SSIFTRNPENIFRWIgpLGSDCGIVNVNiPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTINY 495
Cdd:cd07107 390 AAIWTNDISQAHRTA--RRVEAGYVWIN-GSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
27-475 |
1.60e-85 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 271.49 E-value: 1.60e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 27 GKWQANGP--LVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSL 104
Cdd:cd07151 1 GEWRDGTSerTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 105 EMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERP---NHMMLEmwnPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPgkeNRVYRE---PLGVVGVISPWNFPLHLSMRSVAPALAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 182 GNCVVWKGAPTTPlITIAMtkLVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDtRIP-LVSFTGSSRVGSMVQQTVNAR 259
Cdd:cd07151 158 GNAVVLKPASDTP-ITGGL--LLAKIFEEAGLPKGVLNVVVGaGSEIGDAFVEH-PVPrLISFTGSTPVGRHIGELAGRH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 260 SGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLL 339
Cdd:cd07151 234 LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 340 GPLHTPESKKNFEKGIEVIKSQGGKILTGGKAvegEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINN 418
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLsDVTNDMEIAREEIFGPVAPIIKADDEEEALELAN 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695661 419 SVPQGLSSSIFTRNPE---NIFRWIgplgsDCGIVNVN-IPTNGaEIGGAFGGEKATGGGR 475
Cdd:cd07151 391 DTEYGLSGAVFTSDLErgvQFARRI-----DAGMTHINdQPVND-EPHVPFGGEKNSGLGR 445
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
39-487 |
3.25e-85 |
|
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: 270.35 E-value: 3.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGI-GEV 117
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 118 QEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLIT 197
Cdd:cd07092 82 PGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 198 IAMTKLVAEVLeknnlPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVM 276
Cdd:cd07092 162 LLLAELAAEVL-----PPGVVNVVCGgGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 277 DDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIE 356
Cdd:cd07092 237 DDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 357 VIKsQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPEN 435
Cdd:cd07092 317 RAP-AHARVLTGGRRAEGPGYFYEPTVVaGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 30695661 436 IFRWIGPLGSDCGIVNVNIPTnGAEIggAFGGEKATGGGREAGSDSWKQYMR 487
Cdd:cd07092 396 AMRLSARLDFGTVWVNTHIPL-AAEM--PHGGFKQSGYGKDLSIYALEDYTR 444
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
38-496 |
9.87e-85 |
|
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: 269.17 E-value: 9.87e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEV 117
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 118 QEVIDMCDFAVGLSRQLNGSVIP--------SERpnhmmlemwNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKG 189
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPlpggsfayTRR---------EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 190 APTTPLITIAMtklvAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSG 269
Cdd:cd07090 152 SPFTPLTALLL----AEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 270 NNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKK 349
Cdd:cd07090 228 KSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 350 NFEKGIEVIKSQGGKILTGGKAVEGE-----GNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQG 423
Cdd:cd07090 308 KVLGYIESAKQEGAKVLCGGERVVPEdglenGFYVSPCVLtDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695661 424 LSSSIFTRNPENIFRWIGPL--GSdCGIVNVNIptNGAEIggAFGGEKATGGGREAGSDSWKQYMRRSTCTINYG 496
Cdd:cd07090 388 LAAGVFTRDLQRAHRVIAQLqaGT-CWINTYNI--SPVEV--PFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
40-476 |
2.41e-84 |
|
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: 267.96 E-value: 2.41e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 40 NPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQE 119
Cdd:cd07147 5 NPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 120 VIDMCDFAVGLSRQLNGSVIP---SERpNHMMLEMWN--PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
Cdd:cd07147 85 AIDTFRIAAEEATRIYGEVLPldiSAR-GEGRQGLVRrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 195 LITIamtkLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARsgKTLLELSGNNAII 274
Cdd:cd07147 164 LSAL----ILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 275 VMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKG 354
Cdd:cd07147 238 VDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 355 IEVIKSQGGKILTGGKAvegEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNP 433
Cdd:cd07147 318 VNEAVDAGAKLLTGGKR---DGALLEPTILEdVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 30695661 434 ENIFRWIGPLgsDCGIVNVN-IPTNGAEiGGAFGGEKATGGGRE 476
Cdd:cd07147 395 EKALRAWDEL--EVGGVVINdVPTFRVD-HMPYGGVKDSGIGRE 435
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
59-478 |
2.49e-84 |
|
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: 267.02 E-value: 2.49e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 59 EQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDF-AVGLSRQLNGS 137
Cdd:cd07100 2 EAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYyAENAEAFLADE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 138 VIPSERPNHMMLemWNPLGIVGVITAFNFPCavlgWN----ACIALVCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNL 213
Cdd:cd07100 82 PIETDAGKAYVR--YEPLGVVLGIMPWNFPF----WQvfrfAAPNLMAGNTVLLKHASNVPGCALAI----EELFREAGF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 214 PGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAV 293
Cdd:cd07100 152 PEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 294 GTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVE 373
Cdd:cd07100 232 QNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 374 GEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNV 452
Cdd:cd07100 312 GPGAFYPPTVLTdVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRL--EAGMVFI 389
|
410 420
....*....|....*....|....*..
gi 30695661 453 NIPT-NGAEIggAFGGEKATGGGREAG 478
Cdd:cd07100 390 NGMVkSDPRL--PFGGVKRSGYGRELG 414
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
38-481 |
2.26e-83 |
|
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: 265.76 E-value: 2.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKIL-AEGIGE 116
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 117 VQEVIDMCDFAVGLSRQLNGSVIPSeRPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLI 196
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPF-GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 197 TIAMTKLVAEVLeknnlPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIV 275
Cdd:cd07108 160 VLLLAEILAQVL-----PAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 276 MDDADIQLAARSVLFAAVGT-AGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKG 354
Cdd:cd07108 235 FPDADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 355 IEV-IKSQGGKILTGGKAVE----GEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSI 428
Cdd:cd07108 315 IDLgLSTSGATVLRGGPLPGegplADGFFVQPTIFsGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 30695661 429 FTRNPENIFRWIGPLgsDCGIVNVNiPTNGAEIGGAFGGEKATGGGREAGSDS 481
Cdd:cd07108 395 WTRDLGRALRAAHAL--EAGWVQVN-QGGGQQPGQSYGGFKQSGLGREASLEG 444
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
21-455 |
4.20e-83 |
|
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: 265.53 E-value: 4.20e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 21 LGSYVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYL 98
Cdd:cd07085 1 LKLFINGEWVEskTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 99 GRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIA 178
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 179 LVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTvNA 258
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAM----RLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYER-AA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 259 RSGKTLLELSG-NNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGT 337
Cdd:cd07085 236 ANGKRVQALGGaKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 338 LLGPLHTPESKKNFEKGIEVIKSQGGKILTGGK--AVEG--EGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGE 412
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGRgvKVPGyeNGNFVGPTILDnVTPDMKIYKEEIFGPVLSIVRVDTLDE 395
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 30695661 413 AVAINNSVPQGLSSSIFTRNPENIFRWIgpLGSDCGIVNVNIP 455
Cdd:cd07085 396 AIAIINANPYGNGAAIFTRSGAAARKFQ--REVDAGMVGINVP 436
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
39-493 |
1.88e-82 |
|
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: 262.94 E-value: 1.88e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKI-WMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEV 117
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 118 QEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLIT 197
Cdd:cd07109 82 EAAARYFEYYGGAADKLHGETIPLG-PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 198 IAMtklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVM 276
Cdd:cd07109 161 LRL----AELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 277 DDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEkGTLLGPLHTPESKKNFEKGIE 356
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 357 VIKSQGGKILTGGKAVEG---EGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRN 432
Cdd:cd07109 316 RARARGARIVAGGRIAEGapaGGYFVAPTLLdDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695661 433 PENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTI 493
Cdd:cd07109 396 GDRALRVARRL--RAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
39-493 |
2.64e-82 |
|
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: 262.68 E-value: 2.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 39 LNPANNQPIAQVvEASLEDyeQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQ 118
Cdd:cd07146 4 RNPYTGEVVGTV-PAGTEE--ALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 119 EVIDMCDFAVGLSRQLNGSVIPSERPNH----MMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
Cdd:cd07146 81 RAADVLRFAAAEALRDDGESFSCDLTANgkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 195 LITIAMtklvAEVLEKNNLPGAIFTAMCGG-AEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARsgKTLLELSGNNAI 273
Cdd:cd07146 161 LSAIYL----ADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--RQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 274 IVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEK 353
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 354 GIEVIKSQGGKILTGGkavEGEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRN 432
Cdd:cd07146 315 RVEEAIAQGARVLLGN---QRQGALYAPTVLDhVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30695661 433 PENIFRWIGPLgsDCGIVNVNiptngaEIGG------AFGGEKATG-GGREAGSDSWKQYMRRSTCTI 493
Cdd:cd07146 392 LDTIKRLVERL--DVGTVNVN------EVPGfrselsPFGGVKDSGlGGKEGVREAMKEMTNVKTYSL 451
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
23-486 |
2.84e-81 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 260.99 E-value: 2.84e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 23 SYVAGKW--QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGR 100
Cdd:PRK11241 13 ALINGEWldANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 101 LLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALV 180
Cdd:PRK11241 93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 181 CGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTAMCGGA-EIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNAR 259
Cdd:PRK11241 173 AGCTMVLKPASQTPFSALAL----AELAIRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 260 SGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLL 339
Cdd:PRK11241 249 IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 340 GPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTI-IEISADAAVVKEELFAPVLYVLKFKSFGEAVAINN 418
Cdd:PRK11241 329 GPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTIlVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30695661 419 SVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIgGAFGGEKATGGGREAGSDSWKQYM 486
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEAL--EYGIVGINTGIISNEV-APFGGIKASGLGREGSKYGIEDYL 473
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
38-478 |
8.87e-81 |
|
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: 258.82 E-value: 8.87e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEV 117
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 118 QEVIDMCDFAVGLSRQLN---GSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDakaERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 195 LITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAI 273
Cdd:cd07110 161 LTELELAEIAAEA----GLPPGVLNVVTGtGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 274 IVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEK 353
Cdd:cd07110 237 IVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 354 GIEVIKSQGGKILTGGKAVE--GEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFT 430
Cdd:cd07110 317 FIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFaDVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 30695661 431 RNPENIFRWIGPLgsDCGIVNVNIPtNGAEIGGAFGGEKATGGGREAG 478
Cdd:cd07110 397 RDAERCDRVAEAL--EAGIVWINCS-QPCFPQAPWGGYKRSGIGRELG 441
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
39-493 |
9.73e-81 |
|
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: 258.81 E-value: 9.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 39 LNPANNQPIAQVVEASLEDYEQGLKACEEA--AKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGE 116
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 117 VQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPli 196
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 197 tiAMTKLVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIV 275
Cdd:cd07118 160 --GTTLMLAELLIEAGLPAGVVNIVTGyGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 276 MDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGI 355
Cdd:cd07118 238 FADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 356 EVIKSQGGKILTGGKAVE-GEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNP 433
Cdd:cd07118 318 DAGRAEGATLLLGGERLAsAAGLFYQPTIFtDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695661 434 ENIFRWIGPLGSdcGIVNVN-IPTNGAEIggAFGGEKATGGGREAGSDSWKQYMRRSTCTI 493
Cdd:cd07118 398 DTALTVARRIRA--GTVWVNtFLDGSPEL--PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
40-476 |
2.06e-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: 257.75 E-value: 2.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 40 NPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQE 119
Cdd:cd07094 5 NPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 120 VIDMCDFAVGLSRQLNGSVIPSE----RPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPL 195
Cdd:cd07094 85 AIDTLRLAAEEAERIRGEEIPLDatqgSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 196 ITIAMtklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVqqTVNARSGKTLLELSGNNAII 274
Cdd:cd07094 165 SALEL----AKILVEAGVPEGVLQVVTGeREVLGDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 275 VMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKG 354
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 355 IEVIKSQGGKILTGGkavEGEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNP 433
Cdd:cd07094 319 VEEAVEAGARLLCGG---ERDGALFKPTVLEdVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 30695661 434 ENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGGRE 476
Cdd:cd07094 396 NVAFKAAEKL--EVGGVMVNDSSAFRTDWMPFGGVKESGVGRE 436
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
36-495 |
4.06e-79 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 256.33 E-value: 4.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 36 VSTLNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGI 114
Cdd:TIGR01237 48 IVSINPCDkSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 115 GEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
Cdd:TIGR01237 128 AEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 195 LITIAMtklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSmvqqTVNARSGK----------T 263
Cdd:TIGR01237 208 VIAAKF----VEILEEAGLPKGVVQFVPGsGSEVGDYLVDHPKTSLITFTGSREVGT----RIFERAAKvqpgqkhlkrV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 264 LLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLH 343
Cdd:TIGR01237 280 IAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVI 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 344 TPESKKNFEKGIEVIKSQgGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQ 422
Cdd:TIGR01237 360 DQKSFNKIMEYIEIGKAE-GRLVSGGCGDDSKGYFIGPTIFaDVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEY 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695661 423 GLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGS-DSWKQYMRRSTCTINY 495
Cdd:TIGR01237 439 GLTGGVISNNRDHINRAKAEF--EVGNLYFNRNITGAIVGyQPFGGFKMSGTDSKAGGpDYLALFMQAKTVTEMF 511
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
35-438 |
5.69e-79 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 256.02 E-value: 5.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 35 LVSTlNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEG 113
Cdd:PRK03137 52 IVSI-NPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 114 IGEVQEVIDMCDFavgLSRQ---LNGSVIPSERP---NHMMLEmwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVW 187
Cdd:PRK03137 131 DADTAEAIDFLEY---YARQmlkLADGKPVESRPgehNRYFYI---PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 188 KGAPTTPLITiamTKLVaEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSmvqqTVNARSGKT--- 263
Cdd:PRK03137 205 KPASDTPVIA---AKFV-EVLEEAGLPAGVVNFVPGsGSEVGDYLVDHPKTRFITFTGSREVGL----RIYERAAKVqpg 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 264 -------LLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPlEKG 336
Cdd:PRK03137 277 qiwlkrvIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP-EDN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 337 TLLGPLHTPESKKNFEKGIEVIKsQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVA 415
Cdd:PRK03137 356 AYMGPVINQASFDKIMSYIEIGK-EEGRLVLGGEGDDSKGYFIQPTIFaDVDPKARIMQEEIFGPVVAFIKAKDFDHALE 434
|
410 420
....*....|....*....|...
gi 30695661 416 INNSVPQGLSSSIFTRNPENIFR 438
Cdd:PRK03137 435 IANNTEYGLTGAVISNNREHLEK 457
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
39-486 |
2.44e-78 |
|
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: 252.55 E-value: 2.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAP-KRGDIVRQIGDALRSKLDYLGRLLSLEMGKILA-EGIGE 116
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWSTDAeERARCLRQLHEALEARKEELRALLVAEVGAPVMtARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 117 VQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEM----WNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPT 192
Cdd:cd07089 82 VDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGRrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 193 TPLITIAMTKLVAEVleknNLPGAIFTAMCGG-AEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNN 271
Cdd:cd07089 162 TPLSALLLGEIIAET----DLPAGVVNVVTGSdNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 272 AIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNF 351
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 352 EKGIEVIKSQGGKILTGGKAVEG--EGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSI 428
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGRPAGldKGFYVEPTLFaDVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 30695661 429 FTRNPENIFRWIGPLgsDCGIVNVNiPTNGAEIGGAFGGEKATGGGREAGSDSWKQYM 486
Cdd:cd07089 398 WSADVDRAYRVARRI--RTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
47-486 |
3.46e-78 |
|
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: 251.83 E-value: 3.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 47 IAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDF 126
Cdd:cd07152 4 LGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 127 AVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCaVLGWNACI-ALVCGNCVVWKGAPTTPlitIAMTKLVA 205
Cdd:cd07152 84 AAGLPTQPQGEILPSA-PGRLSLARRVPLGVVGVISPFNFPL-ILAMRSVApALALGNAVVLKPDPRTP---VSGGVVIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 206 EVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGsmvqQTVNARSGKTL----LELSGNNAIIVMDDADI 281
Cdd:cd07152 159 RLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVG----RKVGEAAGRHLkkvsLELGGKNALIVLDDADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 282 QLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQ 361
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 362 GGKILTGGKAvegEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRwi 440
Cdd:cd07152 315 GARLEAGGTY---DGLFYRPTVLsGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMA-- 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 30695661 441 gpLGS--DCGIVNVNIPTNGAEIGGAFGGEKATG-GGREAGSDSWKQYM 486
Cdd:cd07152 390 --LADrlRTGMLHINDQTVNDEPHNPFGGMGASGnGSRFGGPANWEEFT 436
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
15-494 |
5.27e-78 |
|
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: 252.45 E-value: 5.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 15 GLTSHNLGSYVAGKW--QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKI-W-MQVTAPKRGDIVRQIGDA 90
Cdd:cd07143 1 GKYEQPTGLFINGEFvdSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWgLKVSGSKRGRCLSKLADL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 91 LRSKLDYLGRLLSLEMGK-ILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCA 169
Cdd:cd07143 81 MERNLDYLASIEALDNGKtFGTAKRVDVQASADTFRYYGGWADKIHGQVIETD-IKKLTYTRHEPIGVCGQIIPWNFPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 170 VLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRV 248
Cdd:cd07143 160 MCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEA----GFPPGVINVVSGyGRTCGNAISSHMDIDKVAFTGSTLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 249 GSMVQQTVnARSG--KTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQ 326
Cdd:cd07143 236 GRKVMEAA-AKSNlkKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 327 VKIGNPLEKGTLLGPlhtPESKKNFEKGIEVI---KSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVL 402
Cdd:cd07143 315 LKVGDPFAEDTFQGP---QVSQIQYERIMSYIesgKAEGATVETGGKRHGNEGYFIEPTIFtDVTEDMKIVKEEIFGPVV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 403 YVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSW 482
Cdd:cd07143 392 AVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANAL--KAGTVWVNC-YNLLHHQVPFGGYKQSGIGRELGEYAL 468
|
490
....*....|..
gi 30695661 483 KQYMRRSTCTIN 494
Cdd:cd07143 469 ENYTQIKAVHIN 480
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
24-478 |
2.31e-77 |
|
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: 250.18 E-value: 2.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 24 YVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEA--AKIWMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:cd07139 2 FIGGRWVApsGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 100 RLLSLEMGK-ILAEGIGEVQEVIDMCDFAVGLSRQLNgsvIPSERPNHMM---LEMWNPLGIVGVITAFNFPCAVLGWNA 175
Cdd:cd07139 82 RLWTAENGMpISWSRRAQGPGPAALLRYYAALARDFP---FEERRPGSGGghvLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 176 CIALVCGNCVVWKGAPTTPLitiaMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQT 255
Cdd:cd07139 159 APALAAGCTVVLKPSPETPL----DAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 256 VNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEK 335
Cdd:cd07139 235 CGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 336 GTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEG--EGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGE 412
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGldRGWFVEPTLFaDVDNDMRIAQEEIFGPVLSVIPYDDEDD 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30695661 413 AVAINNSVPQGLSSSIFTRNPE---NIFRWIgplgsDCGIVNVNIPTngAEIGGAFGGEKATGGGREAG 478
Cdd:cd07139 395 AVRIANDSDYGLSGSVWTADVErglAVARRI-----RTGTVGVNGFR--LDFGAPFGGFKQSGIGREGG 456
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
22-476 |
2.37e-76 |
|
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: 248.03 E-value: 2.37e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 22 GSYVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:cd07559 2 DNFINGEWVApsKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 100 RLLSLEMGKILAEGIG-EVQEVIDMCDFAVGLSRQLNGSVIPSERpNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIA 178
Cdd:cd07559 82 VAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSLSEIDE-DTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 179 LVCGNCVVWKGAPTTPLITIAMTKLVAEVLEK---NNLPGAiftamcgGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQT 255
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDLLPKgvvNVVTGF-------GSEAGKPLASHPRIAKLAFTGSTTVGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 256 VNARSGKTLLELSGNNAIIVMDDA-----DIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIG 330
Cdd:cd07559 234 AAENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 331 NPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEG----EGNFVEPTIIE-ISADAAVVKEELFAPVLYVL 405
Cdd:cd07559 314 NPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLggldKGYFYEPTLIKgGNNDMRIFQEEIFGPVLAVI 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695661 406 KFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWigPLGSDCGIVNVN----IPTngaeiGGAFGGEKATGGGRE 476
Cdd:cd07559 394 TFKDEEEAIAIANDTEYGLGGGVWTRDINRALRV--ARGIQTGRVWVNcyhqYPA-----HAPFGGYKKSGIGRE 461
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
57-478 |
4.00e-76 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 246.03 E-value: 4.00e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 57 DYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNG 136
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 137 SViPSERPNHMMLEMWNPLGIVGVITAFNFPcAVLGwNACI--ALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLP 214
Cdd:cd07095 81 ER-ATPMAQGRAVLRHRPHGVMAVFGPFNFP-GHLP-NGHIvpALLAGNTVVFKPSELTP----AVAELMVELWEEAGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 215 GAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTL-LELSGNNAIIVMDDADIQLAARSVLFAAV 293
Cdd:cd07095 154 PGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 294 GTAGQRCTTCRRLLLHES-VYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAV 372
Cdd:cd07095 234 LTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 373 EGEGNFVEPTIIEISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPEnIFRWIGpLGSDCGIVNV 452
Cdd:cd07095 314 VAGTAFLSPGIIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEA-LFERFL-ARIRAGIVNW 391
|
410 420
....*....|....*....|....*.
gi 30695661 453 NIPTNGAEIGGAFGGEKATGGGREAG 478
Cdd:cd07095 392 NRPTTGASSTAPFGGVGLSGNHRPSA 417
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
39-494 |
6.61e-76 |
|
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: 247.88 E-value: 6.61e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 39 LNPA-NNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEV 117
Cdd:cd07125 51 IDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 118 QEVIDMCDFAVGLSRQLNGSVI---PSERPNHMMLEmwnPLGIVGVITAFNFPCAV-LGWNACiALVCGNCVVWKGAPTT 193
Cdd:cd07125 131 REAIDFCRYYAAQARELFSDPElpgPTGELNGLELH---GRGVFVCISPWNFPLAIfTGQIAA-ALAAGNTVIAKPAEQT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 194 PLITIAMTKLV------AEVLekNNLPGAiftamcgGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLL-- 265
Cdd:cd07125 207 PLIAARAVELLheagvpRDVL--QLVPGD-------GEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPILPli 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 266 -ELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHT 344
Cdd:cd07125 278 aETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLID 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 345 PESKKNFEKGIEVIKSQgGKILTGGKAVEGEGNFVEPTIIEISADaAVVKEELFAPVLYVLKFKSF--GEAVAINNSVPQ 422
Cdd:cd07125 358 KPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGI-FDLTTEVFGPILHVIRFKAEdlDEAIEDINATGY 435
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695661 423 GLSSSIFTRNPENIFRWIGPLGSdcGIVNVNIPTNGAeIGGA--FGGEKATGGGREAGSDSW-KQYMRRSTCTIN 494
Cdd:cd07125 436 GLTLGIHSRDEREIEYWRERVEA--GNLYINRNITGA-IVGRqpFGGWGLSGTGPKAGGPNYlLRFGNEKTVSLN 507
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
24-487 |
4.93e-75 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 244.33 E-value: 4.93e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 24 YVAGKW--QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKI--WMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:cd07142 7 FINGQFvdAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 100 RLLSLEMGKILAEG-IGEVQEVIDMCDFAVGLSRQLNGSVIPSERPnHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIA 178
Cdd:cd07142 87 ALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGP-HHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 179 LVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVN 257
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSALLAAKLAAEA----GLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 258 ARSGKTL-LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKG 336
Cdd:cd07142 242 KSNLKPVtLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 337 TLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVA 415
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFsDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30695661 416 INNSVPQGLSSSIFTRNPENIFRWIGPLGSdcGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMR 487
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKA--GTVWVNC-YDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
22-432 |
5.64e-75 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 244.43 E-value: 5.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 22 GSYVAGkwqaNGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:PRK13473 9 GELVAG----EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 102 LSLEMGK-ILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALV 180
Cdd:PRK13473 85 ESLNCGKpLHLALNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 181 CGNCVVWKGAPTTPLITIAMTKLVAEVLeknnlPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVnAR 259
Cdd:PRK13473 165 AGNTVVLKPSEITPLTALKLAELAADIL-----PPGVLNVVTGrGATVGDALVGHPKVRMVSLTGSIATGKHVLSAA-AD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 260 SGK-TLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTL 338
Cdd:PRK13473 239 SVKrTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 339 LGPLHTPESKKNFEKGIEVIKSQG-GKILTGGKAVEGEGNFVEPTIIeisADAA----VVKEELFAPVLYVLKFKSFGEA 413
Cdd:PRK13473 319 LGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLL---AGARqddeIVQREVFGPVVSVTPFDDEDQA 395
|
410
....*....|....*....
gi 30695661 414 VAINNSVPQGLSSSIFTRN 432
Cdd:PRK13473 396 VRWANDSDYGLASSVWTRD 414
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
21-494 |
7.71e-75 |
|
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: 244.24 E-value: 7.71e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 21 LGSYVAGKW--QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAK-IWMQVTAPKRGDIVRQIGDALRSKLDY 97
Cdd:cd07144 8 TGLFINNEFvkSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFEsWWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 98 LGRLLSLEMGKIL-AEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNAC 176
Cdd:cd07144 88 LAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTS-PNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 177 IALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQT 255
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEA----GFPPGVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTATGRLVMKA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 256 VNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQV-KIGNPLE 334
Cdd:cd07144 243 AAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 335 KGTLLGPLhtpESKKNFEK---GIEVIKSQGGKILTGG---KAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKF 407
Cdd:cd07144 323 DDTVVGPQ---VSKTQYDRvlsYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFtDVPQDMRIVKEEIFGPVVVISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 408 KSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGSdcGIVNVNiPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMR 487
Cdd:cd07144 400 KTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEA--GMVWIN-SSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQ 476
|
....*..
gi 30695661 488 RSTCTIN 494
Cdd:cd07144 477 TKAVHIN 483
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
38-493 |
8.81e-75 |
|
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: 243.79 E-value: 8.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKI---WMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEG- 113
Cdd:cd07141 26 TINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSy 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 114 IGEVQEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTT 193
Cdd:cd07141 106 LVDLPGAIKVLRYYAGWADKIHGKTIPMD-GDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 194 PLITIAMTKLVAE------VLekNNLPGAIFTAmcggaeiGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTL-LE 266
Cdd:cd07141 185 PLTALYLASLIKEagfppgVV--NVVPGYGPTA-------GAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSNLKRVtLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 267 LSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPlhtPE 346
Cdd:cd07141 256 LGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGP---QI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 347 SKKNFEKGIEVIKS---QGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQ 422
Cdd:cd07141 333 DEEQFKKILELIESgkkEGAKLECGGKRHGDKGYFIQPTVFsDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTY 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695661 423 GLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPtNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTI 493
Cdd:cd07141 413 GLAAAVFTKDIDKAITFSNAL--RAGTVWVNCY-NVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
39-434 |
3.29e-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: 3.29e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQ 118
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 119 EVIDMCDFavgLSRQLNGSVIPSERPNHMMLEMW---NPLGIVGVITAFNFP--CAVlgwNACI-ALVCGNCVVWKGAPT 192
Cdd:cd07102 81 GMLERARY---MISIAEEALADIRVPEKDGFERYirrEPLGVVLIIAPWNYPylTAV---NAVIpALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 193 TPLITIAMTKLVAEVLeknnLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNA 272
Cdd:cd07102 155 TPLCGERFAAAFAEAG----LPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 273 IIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFE 352
Cdd:cd07102 231 AYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 353 KGIEVIKSQGGKILTGGK---AVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSI 428
Cdd:cd07102 311 AQIADAIAKGARALIDGAlfpEDKAGGAYLAPTVLtNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASV 390
|
....*.
gi 30695661 429 FTRNPE 434
Cdd:cd07102 391 WTKDIA 396
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
39-487 |
8.46e-74 |
|
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: 240.59 E-value: 8.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQ 118
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 119 EVIDMCDFAVGLSRQLNGsviPSERPNHMMleMWN--------PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGA 190
Cdd:cd07099 81 LALEAIDWAARNAPRVLA---PRKVPTGLL--MPNkkatveyrPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 191 PTTPLITIAMTKLVAEVleknNLPGAIFTAMCGGAEIGEAIAkDTRIPLVSFTGSSRVGsmvqQTVNARSGKTL----LE 266
Cdd:cd07099 156 EVTPLVGELLAEAWAAA----GPPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATG----RKVMAAAAERLipvvLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 267 LSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPE 346
Cdd:cd07099 227 LGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTAR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 347 SKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLS 425
Cdd:cd07099 307 QLDIVRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLtDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695661 426 SSIFTRNPENIFRWIGPLgsDCGIVNVN-IPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMR 487
Cdd:cd07099 387 ASVFSRDLARAEAIARRL--EAGAVSINdVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCR 447
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
3-489 |
4.40e-73 |
|
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: 239.60 E-value: 4.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 3 SANNEYEFLSEIgltSHNLGSYVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKR 80
Cdd:cd07111 7 SAACALAWLDAH---DRSFGHFINGKWVKpeNRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 81 GDIVRQIGDALRSKLDYLGRLLSLEMGKilaegigEVQEVIDmCD-------------FAVGLSRQLNGsvipserpnhm 147
Cdd:cd07111 84 ARHLYRIARHIQKHQRLFAVLESLDNGK-------PIRESRD-CDiplvarhfyhhagWAQLLDTELAG----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 148 mlemWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTAMCGGAEI 227
Cdd:cd07111 145 ----WKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTAL----LFAEICAEAGLPPGVLNIVTGNGSF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 228 GEAIAKDTRIPLVSFTGSSRVGSMVQQTVnARSGKTL-LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRL 306
Cdd:cd07111 217 GSALANHPGVDKVAFTGSTEVGRALRRAT-AGTGKKLsLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 307 LLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIE- 385
Cdd:cd07111 296 LVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTn 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 386 ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWigPLGSDCGIVNVNiPTNGAEIGGAF 465
Cdd:cd07111 376 VPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEV--ALSLKAGVVWIN-GHNLFDAAAGF 452
|
490 500
....*....|....*....|....
gi 30695661 466 GGEKATGGGREAGSDSWKQYMRRS 489
Cdd:cd07111 453 GGYRESGFGREGGKEGLYEYLRPS 476
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
85-432 |
5.23e-73 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 237.33 E-value: 5.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 85 RQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAF 164
Cdd:PRK10090 2 RKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 165 NFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFT 243
Cdd:PRK10090 82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEI----GLPKGVFNLVLGrGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 244 GSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTS 323
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 324 YKQVKIGNPLEKGTL-LGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPT-IIEISADAAVVKEELFAPV 401
Cdd:PRK10090 238 MQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTlLLDVRQEMSIMHEETFGPV 317
|
330 340 350
....*....|....*....|....*....|.
gi 30695661 402 LYVLKFKSFGEAVAINNSVPQGLSSSIFTRN 432
Cdd:PRK10090 318 LPVVAFDTLEEAIAMANDSDYGLTSSIYTQN 348
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
24-494 |
6.85e-73 |
|
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: 238.62 E-value: 6.85e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 24 YVAGKW-QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAP-KRGDIVRQIGDALRSKLDYLGRL 101
Cdd:cd07082 5 LINGEWkESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLeERIDCLHKFADLLKENKEEVANL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 102 LSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMM----LEMWNPLGIVGVITAFNFPCAvLGWNACI 177
Cdd:cd07082 85 LMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKgkiaQVRREPLGVVLAIGPFNYPLN-LTVSKLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 178 -ALVCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQt 255
Cdd:cd07082 164 pALIMGNTVVFKPATQGVLLGIPL----AEAFHDAGFPKGVVNVVTGrGREIGDPLVTHGRIDVISFTGSTEVGNRLKK- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 256 vNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEK 335
Cdd:cd07082 239 -QHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 336 GTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVegEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAV 414
Cdd:cd07082 318 GVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGRE--GGNLIYPTLLDpVTPDMRLAWEEPFGPVLPIIRVNDIEEAI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 415 AINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVN-IPTNGAEIgGAFGGEKATGGGREAGSDSWKQYMRRSTCTI 493
Cdd:cd07082 396 ELANKSNYGLQASIFTKDINKARKLADAL--EVGTVNINsKCQRGPDH-FPFLGRKDSGIGTQGIGDALRSMTRRKGIVI 472
|
.
gi 30695661 494 N 494
Cdd:cd07082 473 N 473
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
24-488 |
8.51e-73 |
|
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: 239.40 E-value: 8.51e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 24 YVAGKWQANGPLVSTLNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLL 102
Cdd:cd07083 22 VIGGEWVDTKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 103 SLEMGKILAEGIGEVQEVIDMCDF-AVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYyARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 182 GNCVVWKGAPTTPLITIAmtklVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARS 260
Cdd:cd07083 182 GNTVIAKPAEDAVVVGYK----VFEIFHEAGFPPGVVQFLPGvGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 261 G------KTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLE 334
Cdd:cd07083 258 PgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 335 KGTLLGPLHTPESKKNFEKGIEVIKSQgGKILTGGKAVEGEGNFVEPTIIEI-SADAAVVKEELFAPVLYVLKFKS--FG 411
Cdd:cd07083 338 NGTDLGPVIDAEQEAKVLSYIEHGKNE-GQLVLGGKRLEGEGYFVAPTVVEEvPPKARIAQEEIFGPVLSVIRYKDddFA 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30695661 412 EAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGSdswKQYMRR 488
Cdd:cd07083 417 EALEVANSTPYGLTGGVYSRKREHLEEARREF--HVGNLYINRKITGALVGvQPFGGFKLSGTNAKTGG---PHYLRR 489
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
38-486 |
7.35e-72 |
|
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: 235.57 E-value: 7.35e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 38 TLNPANNQPIAQVVEASLEDYEQGLKACEEA--AKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGI- 114
Cdd:cd07112 6 TINPATGRVLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 115 GEVQEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
Cdd:cd07112 86 VDVPSAANTFRWYAEAIDKVYGEVAPTG-PDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 195 LITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQtvnaRSGKT-----LLELS 268
Cdd:cd07112 165 LTALRLAELALEA----GLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFLE----YSGQSnlkrvWLECG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 269 GNNAIIVMDDA-DIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLhtpES 347
Cdd:cd07112 237 GKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGAL---VS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 348 KKNFEK---GIEVIKSQGGKILTGGKAV--EGEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVP 421
Cdd:cd07112 314 EAHFDKvlgYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDgVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695661 422 QGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYM 486
Cdd:cd07112 394 YGLAASVWTSDLSRAHRVARRL--RAGTVWVNC-FDEGDITTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
38-486 |
2.15e-71 |
|
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: 234.16 E-value: 2.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPK-RGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGE 116
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHDPRlRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 117 VQEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLI 196
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMIEPE-PGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 197 TIAMTKLVAEVLEknnLP-GAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIV 275
Cdd:cd07120 160 NAAIIRILAEIPS---LPaGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 276 MDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGI 355
Cdd:cd07120 237 FDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 356 EVIKSQGGK-ILTGGKAVEG--EGNFVEPTIIEIS-ADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTR 431
Cdd:cd07120 317 ERAIAAGAEvVLRGGPVTEGlaKGAFLRPTLLEVDdPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 30695661 432 NPENIFRWIGPLgsDCGIVNVNipTNGAEIGGA-FGGEKATGGGREAGSDSWKQYM 486
Cdd:cd07120 397 DLARAMRVARAI--RAGTVWIN--DWNKLFAEAeEGGYRQSGLGRLHGVAALEDFI 448
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
24-487 |
5.09e-71 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 234.39 E-value: 5.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 24 YVAGKWQAN--GPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:PRK13252 10 YIDGAYVEAtsGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 102 LSLEMGKILAEGIgeVQEVI---DMCDFAVGLSRQLNGSVIPSeRPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIA 178
Cdd:PRK13252 90 ETLDTGKPIQETS--VVDIVtgaDVLEYYAGLAPALEGEQIPL-RGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 179 LVCGNCVVWKGAPTTPLITIamtKLvAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGsmvqQTVNA 258
Cdd:PRK13252 167 LAAGNAMIFKPSEVTPLTAL---KL-AEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTG----KKVMA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 259 RSGKTL----LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLE 334
Cdd:PRK13252 239 AAAASLkevtMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 335 KGTLLGPLhtpESKKNFEK---GIEVIKSQGGKILTGGKAVE----GEGNFVEPTI-IEISADAAVVKEELFAPVLYVLK 406
Cdd:PRK13252 319 PATNFGPL---VSFAHRDKvlgYIEKGKAEGARLLCGGERLTeggfANGAFVAPTVfTDCTDDMTIVREEIFGPVMSVLT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 407 FKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNipTNG---AEIggAFGGEKATGGGREAGSDSWK 483
Cdd:PRK13252 396 FDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQL--EAGICWIN--TWGespAEM--PVGGYKQSGIGRENGIATLE 469
|
....
gi 30695661 484 QYMR 487
Cdd:PRK13252 470 HYTQ 473
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
24-486 |
4.29e-70 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 232.32 E-value: 4.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 24 YVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEA-----AKIWMQVTAPKRGDIVRQIGDALRSKLD 96
Cdd:PLN02467 11 FIGGEWREpvLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 97 YLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNG-SVIPSERPnhmMLE-----MWNPLGIVGVITAFNFPCAV 170
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAkQKAPVSLP---METfkgyvLKEPLGVVGLITPWNYPLLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 171 LGWNACIALVCGNCVVWKgapttPLITIAMTKLV-AEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRV 248
Cdd:PLN02467 168 ATWKVAPALAAGCTAVLK-----PSELASVTCLElADICREVGLPPGVLNVVTGlGTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 249 GSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVK 328
Cdd:PLN02467 243 GRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 329 IGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEG--EGNFVEPTII-EISADAAVVKEELFAPVLYVL 405
Cdd:PLN02467 323 ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIItDVTTSMQIWREEVFGPVLCVK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 406 KFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVN--------IPtngaeiggaFGGEKATGGGREA 477
Cdd:PLN02467 403 TFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAF--QAGIVWINcsqpcfcqAP---------WGGIKRSGFGREL 471
|
....*....
gi 30695661 478 GSDSWKQYM 486
Cdd:PLN02467 472 GEWGLENYL 480
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
24-478 |
3.99e-68 |
|
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: 225.84 E-value: 3.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 24 YVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:cd07138 2 YIDGAWVApaGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 102 LSLEMG--KILAE------GIGEVQEVIDMC-DFAvgLSRQLNGSVIPSErpnhmmlemwnPLGIVGVITAFNFP----- 167
Cdd:cd07138 82 ITLEMGapITLARaaqvglGIGHLRAAADALkDFE--FEERRGNSLVVRE-----------PIGVCGLITPWNWPlnqiv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 168 CAVLGwnaciALVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSS 246
Cdd:cd07138 149 LKVAP-----ALAAGCTVVLKPSEVAPLSAI----ILAEILDEAGLPAGVFNLVNGdGPVVGEALSAHPDVDMVSFTGST 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 247 RVGSMVQQTVnARSGK-TLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYK 325
Cdd:cd07138 220 RAGKRVAEAA-ADTVKrVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 326 QVKIGNPLEKGTLLGPLhtpESKKNFEKGIEVIKS---QGGKILTGG-KAVEG--EGNFVEPTII-EISADAAVVKEELF 398
Cdd:cd07138 299 AYVVGDPRDPATTLGPL---ASAAQFDRVQGYIQKgieEGARLVAGGpGRPEGleRGYFVKPTVFaDVTPDMTIAREEIF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 399 APVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNipTNGAEIGGAFGGEKATGGGREAG 478
Cdd:cd07138 376 GPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRL--RAGQVHIN--GAAFNPGAPFGGYKQSGNGREWG 451
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
22-476 |
9.45e-68 |
|
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: 9.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 22 GSYVAGKW--QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:cd07117 2 GLFINGEWvkGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 100 RLLSLEMGKILAEGIG-EVQEVIDMCDFAVGLSRQLNGSVIPSERpNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIA 178
Cdd:cd07117 82 MVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDE-DTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 179 LVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKnnlpGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNA 258
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDVLPK----GVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 259 RSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTL 338
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 339 LGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGE----GNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEA 413
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVnVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695661 414 VAINNSVPQGLSSSIFTRNPENIFRWigPLGSDCGIVNVNIpTNGAEIGGAFGGEKATGGGRE 476
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRV--ARAVETGRVWVNT-YNQIPAGAPFGGYKKSGIGRE 456
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
22-495 |
1.63e-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: 224.63 E-value: 1.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 22 GSYVAGKWQANGPL--VSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAP-KRGDIVRQIGDALRSKLDYL 98
Cdd:cd07113 1 GHFIDGRPVAGQSEkrLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTPaERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 99 GRLLSLEMGKI--LAEGIgEVQEVIDMCDFAVGLSRQLNGSV----IPS---ERpnHMMLEMWNPLGIVGVITAFNFPCA 169
Cdd:cd07113 81 AQLETLCSGKSihLSRAF-EVGQSANFLRYFAGWATKINGETlapsIPSmqgER--YTAFTRREPVGVVAGIVPWNFSVM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 170 VLGWNACIALVCGNCVVWKGAPTTPLitiamTKL-VAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRV 248
Cdd:cd07113 158 IAVWKIGAALATGCTIVIKPSEFTPL-----TLLrVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVAT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 249 GSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVK 328
Cdd:cd07113 233 GKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 329 IGNPLEKGTLLGPLhtpESKKNFEK---GIEVIKSQGGKILTGGKAVEGEGNFVEPTIIEI-SADAAVVKEELFAPVLYV 404
Cdd:cd07113 313 VGSPMDESVMFGPL---ANQPHFDKvcsYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLArSADSRLMREETFGPVVSF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 405 LKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNgAEIGGAFGGEKATGGGREAGSDSWKQ 484
Cdd:cd07113 390 VPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRI--EAGTVWVNMHTF-LDPAVPFGGMKQSGIGREFGSAFIDD 466
|
490
....*....|.
gi 30695661 485 YMRRSTCTINY 495
Cdd:cd07113 467 YTELKSVMIRY 477
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
22-492 |
4.77e-66 |
|
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: 220.91 E-value: 4.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 22 GSYVAGKWQANGPLVstlNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:TIGR01722 7 GKFAEGASGTYIPVT---NPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 102 LSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:TIGR01722 84 ITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIAC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 182 GNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTvNARSG 261
Cdd:TIGR01722 164 GNTFVLKPSEKVPSAAV----KLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTT-GSAHG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 262 KTLLELSG-NNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVyDKVLEQLLTSYKQVKIGNPLEKGTLLG 340
Cdd:TIGR01722 239 KRVQALGGaKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGAEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 341 PLHTPESKKNFEKGIEVIKSQGGKILTGGKA--VEG--EGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVA 415
Cdd:TIGR01722 318 PLITPQAKDRVASLIAGGAAEGAEVLLDGRGykVDGyeEGNWVGPTLLErVPPTMKAYQEEIFGPVLCVLEADTLEEAIA 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30695661 416 INNSVPQGLSSSIFTRNPENIFRWigPLGSDCGIVNVNIPTNGAEIGGAFGGEKAT--GGGREAGSDSWKQYMRRSTCT 492
Cdd:TIGR01722 398 LINASPYGNGTAIFTRDGAAARRF--QHEIEVGQVGVNVPIPVPLPYFSFTGWKDSffGDHHIYGKQGTHFYTRGKTVT 474
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
41-486 |
1.27e-64 |
|
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: 216.41 E-value: 1.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 41 PANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEV 120
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 121 IDMCDF-AVGLSRQLNgsviPSERPNHMML-----EMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
Cdd:cd07101 83 AIVARYyARRAERLLK----PRRRRGAIPVltrttVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 195 LITIAMTKLvaevLEKNNLPGAIFTAMCG-GAEIGEAIAKdtRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAI 273
Cdd:cd07101 159 LTALWAVEL----LIEAGLPRDLWQVVTGpGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 274 IVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEK 353
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 354 GIEVIKSQGGKILTGGKAVEGEGN-FVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTR 431
Cdd:cd07101 313 HVDDAVAKGATVLAGGRARPDLGPyFYEPTVLTgVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 30695661 432 NPENIfRWIGPLgSDCGIVNVN---IPTNGAeIGGAFGGEKATGGGREAGSDSWKQYM 486
Cdd:cd07101 393 DGARG-RRIAAR-LRAGTVNVNegyAAAWAS-IDAPMGGMKDSGLGRRHGAEGLLKYT 447
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
57-484 |
3.51e-64 |
|
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: 214.75 E-value: 3.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 57 DYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMG-------KILAEGIGEVQEVIDMCDfavg 129
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGataawagFNVDLAAGMLREAASLIT---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 130 lsrQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPcAVLGWNA-CIALVCGNCVVWKGAPTTPlitiaMT-KLVAEV 207
Cdd:cd07105 77 ---QIIGGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAP-VILGTRAiAYPLAAGNTVVLKASELSP-----RThWLIGRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 208 LEKNNLP-GA---IFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTvnarSGK----TLLELSGNNAIIVMDDA 279
Cdd:cd07105 148 FHEAGLPkGVlnvVTHSPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAET----AAKhlkpVLLELGGKAPAIVLEDA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 280 DIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGnplekGTLLGPLHTPESKKNFEKGIEVIK 359
Cdd:cd07105 224 DLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDAL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 360 SQGGKILTGGKA-VEGEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIF 437
Cdd:cd07105 299 SKGAKLVVGGLAdESPSGTSMPPTILDnVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARAL 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 30695661 438 RWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGGR---EAGSDSWKQ 484
Cdd:cd07105 379 AVAKRI--ESGAVHINGMTVHDEPTLPHGGVKSSGYGRfngKWGIDEFTE 426
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
21-478 |
2.02e-62 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 220.46 E-value: 2.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 21 LGSYVAGKWQAnGPLVST-------LNPANN-QPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALR 92
Cdd:PRK11904 543 IAAFLEKQWQA-GPIINGegearpvVSPADRrRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLE 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 93 SKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERP----NHMMLEmwnPLGIVGVITAFNFPC 168
Cdd:PRK11904 622 ANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPtgesNELRLH---GRGVFVCISPWNFPL 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 169 AV-LGWNACiALVCGNCVVWKGAPTTPLITIAMTKLV------AEVLEKnnLPGAiftamcgGAEIGEAIAKDTRIPLVS 241
Cdd:PRK11904 699 AIfLGQVAA-ALAAGNTVIAKPAEQTPLIAAEAVKLLheagipKDVLQL--LPGD-------GATVGAALTADPRIAGVA 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 242 FTGSSRVGSMVQQTVNARSGK--TLL-ELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLE 318
Cdd:PRK11904 769 FTGSTETARIINRTLAARDGPivPLIaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIE 848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 319 QLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKsQGGKILTGGKAVEG--EGNFVEPTIIEISaDAAVVKEE 396
Cdd:PRK11904 849 MLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMK-REARLLAQLPLPAGteNGHFVAPTAFEID-SISQLERE 926
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 397 LFAPVLYVLKFKSFG-EAV--AINNSvPQGLSSSIFTRNPENIfRWIgplgsdCGIVNV-NIPTNGAEIGGA-----FGG 467
Cdd:PRK11904 927 VFGPILHVIRYKASDlDKVidAINAT-GYGLTLGIHSRIEETA-DRI------ADRVRVgNVYVNRNQIGAVvgvqpFGG 998
|
490
....*....|.
gi 30695661 468 EKATGGGREAG 478
Cdd:PRK11904 999 QGLSGTGPKAG 1009
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
31-487 |
3.73e-62 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 212.36 E-value: 3.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 31 ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEA--AKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGK 108
Cdd:PLN02466 70 ASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 109 ILAEGIG-EVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLeMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVW 187
Cdd:PLN02466 150 PYEQSAKaELPMFARLFRYYAGWADKIHGLTVPADGPHHVQT-LHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 188 KGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQtVNARSG--KTL 264
Cdd:PLN02466 229 KTAEQTPLSALYAAKLLHEA----GLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVLE-LAAKSNlkPVT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 265 LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHT 344
Cdd:PLN02466 304 LELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQID 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 345 PEskkNFEKGIEVIKS---QGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSV 420
Cdd:PLN02466 384 SE---QFEKILRYIKSgveSGATLECGGDRFGSKGYYIQPTVFsNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNT 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695661 421 PQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVN--------IPtngaeiggaFGGEKATGGGREAGSDSWKQYMR 487
Cdd:PLN02466 461 RYGLAAGVFTQNLDTANTLSRAL--RVGTVWVNcfdvfdaaIP---------FGGYKMSGIGREKGIYSLNNYLQ 524
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
22-476 |
4.03e-62 |
|
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: 210.77 E-value: 4.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 22 GSYVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:cd07116 2 DNFIGGEWVApvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 100 RLLSLEMGKILAEGIG-EVQEVIDMCDFAVGLSRQLNGSVipSE-RPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACI 177
Cdd:cd07116 82 VAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSI--SEiDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 178 ALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEknnlPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVN 257
Cdd:cd07116 160 ALAAGNCVVLKPAEQTPASILVLMELIGDLLP----PGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 258 ARSGKTLLELSGNNAII----VM--DDADIQLAARS-VLFAAvgTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIG 330
Cdd:cd07116 236 ENIIPVTLELGGKSPNIffadVMdaDDAFFDKALEGfVMFAL--NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 331 NPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKA----VEGEGNFVEPTIIEISADAAVVKEELFAPVLYVLK 406
Cdd:cd07116 314 NPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelgGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTT 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695661 407 FKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWigPLGSDCGIVNVN----IPTngaeiGGAFGGEKATGGGRE 476
Cdd:cd07116 394 FKDEEEALEIANDTLYGLGAGVWTRDGNTAYRM--GRGIQAGRVWTNcyhlYPA-----HAAFGGYKQSGIGRE 460
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
24-475 |
1.41e-61 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 209.43 E-value: 1.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 24 YVAGKWQA-NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLL 102
Cdd:PRK09457 4 WINGDWIAgQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 103 SLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIpSERPNHMMLEMWNPLGIVGVITAFNFPcAVLGwNACI--ALV 180
Cdd:PRK09457 84 ARETGKPLWEAATEVTAMINKIAISIQAYHERTGEKR-SEMADGAAVLRHRPHGVVAVFGPYNFP-GHLP-NGHIvpALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 181 CGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARS 260
Cdd:PRK09457 161 AGNTVVFKPSELTP----WVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 261 GKTL-LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVY-DKVLEQLLTSYKQVKIGNPL-EKGT 337
Cdd:PRK09457 237 EKILaLEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDaEPQP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 338 LLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIEISADAAVVKEELFAPVLYVLKFKSFGEAVAIN 417
Cdd:PRK09457 317 FMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 418 NSVPQGLSSSIFTRNPE--NIFRwigpLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGR 475
Cdd:PRK09457 397 NNTRFGLSAGLLSDDREdyDQFL----LEIRAGIVNWNKPLTGASSAAPFGGVGASGNHR 452
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
31-495 |
8.56e-60 |
|
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: 204.65 E-value: 8.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 31 ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKI--WMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGK 108
Cdd:cd07140 18 EGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 109 ILAEGIG-EVQEVIDMCDFAVGLSRQLNGSVIP--SERPNH-MMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNC 184
Cdd:cd07140 98 VYTLALKtHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRnLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 185 VVWKGAPTTPLITIAMTKLVAevleKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVnARSG-- 261
Cdd:cd07140 178 VVLKPAQVTPLTALKFAELTV----KAGFPKGVINILPGsGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSC-AVSNlk 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 262 KTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGP 341
Cdd:cd07140 253 KVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 342 lhtPESKKNFEKGIEVIK---SQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSfGEAVAI- 416
Cdd:cd07140 333 ---QNHKAHLDKLVEYCErgvKEGATLVYGGKQVDRPGFFFEPTVFtDVEDHMFIAKEESFGPIMIISKFDD-GDVDGVl 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 417 --NNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTIN 494
Cdd:cd07140 409 qrANDTEYGLASGVFTKDINKALYVSDKL--EAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIE 485
|
.
gi 30695661 495 Y 495
Cdd:cd07140 486 Y 486
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
18-488 |
1.63e-59 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 212.42 E-value: 1.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 18 SHNLGSYVAGKWQAnGPLVST----------LNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQ 86
Cdd:PRK11905 542 DEALNAFAAKTWHA-APLLAGgdvdggtrpvLNPADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILER 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 87 IGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDF-AVGLSRQLNGSVIPserpnhmmlemwnPLGIVGVITAFN 165
Cdd:PRK11905 621 AADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYyAAQARRLLNGPGHK-------------PLGPVVCISPWN 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 166 FPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTG 244
Cdd:PRK11905 688 FPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEA----GVPKDALQLLPGdGRTVGAALVADPRIAGVMFTG 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 245 SSRVGSMVQQTVNARSGK-TLL--ELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLL 321
Cdd:PRK11905 764 STEVARLIQRTLAKRSGPpVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLK 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 322 TSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKI--LTGGKAVEGeGNFVEPTIIEISaDAAVVKEELFA 399
Cdd:PRK11905 844 GAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVhqLPLPAETEK-GTFVAPTLIEID-SISDLEREVFG 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 400 PVLYVLKFKSFG-EAV--AINNSvPQGLSSSIFTRNPENIFRWIGplGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGR 475
Cdd:PRK11905 922 PVLHVVRFKADElDRVidDINAT-GYGLTFGLHSRIDETIAHVTS--RIRAGNIYVNRNIIGAVVGvQPFGGEGLSGTGP 998
|
490
....*....|...
gi 30695661 476 EAGSdswKQYMRR 488
Cdd:PRK11905 999 KAGG---PLYLGR 1008
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
31-487 |
5.15e-59 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 202.74 E-value: 5.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 31 ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAK--IWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGK 108
Cdd:PLN02766 33 ASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 109 ILAEG-IGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMlEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVW 187
Cdd:PLN02766 113 LFALGkAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGY-TLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 188 KGAPTTPLITIamtkLVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVnARSG--KTL 264
Cdd:PLN02766 192 KPAEQTPLSAL----FYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAA-ATSNlkQVS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 265 LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPlht 344
Cdd:PLN02766 267 LELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGP--- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 345 PESKKNFEK---GIEVIKSQGGKILTGGKAVEGEGNFVEPTI-IEISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSV 420
Cdd:PLN02766 344 QVDKQQFEKilsYIEHGKREGATLLTGGKPCGDKGYYIEPTIfTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNT 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 421 PQGLSSSIFTRN---PENIFRWIgplgsDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMR 487
Cdd:PLN02766 424 KYGLAAGIVTKDldvANTVSRSI-----RAGTIWVNC-YFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
23-489 |
1.00e-58 |
|
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: 202.06 E-value: 1.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 23 SYVAGKWQANGPLVSTLNPANNQPI-AQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:TIGR01238 40 PIIGHSYKADGEAQPVTNPADRRDIvGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 102 LSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSvipserpnhmmlEMWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:TIGR01238 120 CVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGE------------FSVESRGVFVCISPWNFPLAIFTGQISAALAA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 182 GNCVVWKGAPTTPLITiamTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNAR-- 259
Cdd:TIGR01238 188 GNTVIAKPAEQTSLIA---YRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRed 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 260 -SGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTL 338
Cdd:TIGR01238 265 aPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 339 LGPLHTPESKKNFEKGIEVIKSQGGKI--LTGGKAVEGE-GNFVEPTIIEISaDAAVVKEELFAPVLYVLKFKS--FGEA 413
Cdd:TIGR01238 345 VGPVIDAEAKQNLLAHIEHMSQTQKKIaqLTLDDSRACQhGTFVAPTLFELD-DIAELSEEVFGPVLHVVRYKAreLDQI 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30695661 414 VAINNSVPQGLSSSIFTRNPENIfRWIGPlGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGSDSWKQYMRRS 489
Cdd:TIGR01238 424 VDQINQTGYGLTMGVHSRIETTY-RWIEK-HARVGNCYVNRNQVGAVVGvQPFGGQGLSGTGPKAGGPHYLYRLTQV 498
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
36-476 |
1.77e-58 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 200.35 E-value: 1.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 36 VSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIG 115
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 116 EVQEVIDMCDF-----------------AVGLSRqlngsvipserpnhmMLEMWNPLGIVGVITAFNFPCAVLGWNACIA 178
Cdd:PRK09406 83 EALKCAKGFRYyaehaealladepadaaAVGASR---------------AYVRYQPLGVVLAVMPWNFPLWQVVRFAAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 179 LVCGNCVVWKGAPTTPlitiaMTKL-VAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVN 257
Cdd:PRK09406 148 LMAGNVGLLKHASNVP-----QTALyLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 258 ARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGT 337
Cdd:PRK09406 223 DEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 338 LLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAI 416
Cdd:PRK09406 303 DVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVItDITPDMRLYTEEVFGPVASLYRVADIDEAIEI 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695661 417 NNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVN-IPTNGAEIGgaFGGEKATGGGRE 476
Cdd:PRK09406 383 ANATTFGLGSNAWTRDEAEQERFIDDL--EAGQVFINgMTVSYPELP--FGGVKRSGYGRE 439
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
38-476 |
1.21e-57 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 198.16 E-value: 1.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEV 117
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 118 QEVIDMCD-FAVGLSRQLNGSviPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTpli 196
Cdd:PRK13968 91 AKSANLCDwYAEHGPAMLKAE--PTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 197 tIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVM 276
Cdd:PRK13968 166 -MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 277 DDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIE 356
Cdd:PRK13968 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 357 VIKSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPEN 435
Cdd:PRK13968 325 ATLAEGARLLLGGEKIAGAGNYYAPTVLaNVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQ 404
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 30695661 436 IFRWIGPLgsDCGIVNVN-IPTNGAEIggAFGGEKATGGGRE 476
Cdd:PRK13968 405 ARQMAARL--ECGGVFINgYCASDARV--AFGGVKKSGFGRE 442
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
16-480 |
3.61e-57 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 198.56 E-value: 3.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 16 LTSHNLGSYVAGKWQANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKL 95
Cdd:PRK09407 14 LTFERLRRLTARVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 96 DYLGRLLSLEMGKILAEGIGEVQEVIDMCDF----AVGLSRqlngsviPSERPNHMML-----EMWNPLGIVGVITAFNF 166
Cdd:PRK09407 94 EELLDLVQLETGKARRHAFEEVLDVALTARYyarrAPKLLA-------PRRRAGALPVltkttELRQPKGVVGVISPWNY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 167 PCAVLGWNACIALVCGNCVVWKGAPTTPLITIAmtklVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKdtRIPLVSFTGS 245
Cdd:PRK09407 167 PLTLAVSDAIPALLAGNAVVLKPDSQTPLTALA----AVELLYEAGLPRDLWQVVTGpGPVVGTALVD--NADYLMFTGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 246 SRVGsmvqQTVNARSGKTL----LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLL 321
Cdd:PRK09407 241 TATG----RVLAEQAGRRLigfsLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 322 TSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGN-FVEPTIIE-ISADAAVVKEELFA 399
Cdd:PRK09407 317 AAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGPlFYEPTVLTgVTPDMELAREETFG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 400 PVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNP---ENIFRWIgplgsDCGIVNVN---IPTNGAeIGGAFGGEKATGG 473
Cdd:PRK09407 397 PVVSVYPVADVDEAVERANDTPYGLNASVWTGDTargRAIAARI-----RAGTVNVNegyAAAWGS-VDAPMGGMKDSGL 470
|
....*..
gi 30695661 474 GREAGSD 480
Cdd:PRK09407 471 GRRHGAE 477
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
18-436 |
9.35e-54 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 195.54 E-value: 9.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 18 SHNLGSYVAGKWQAnGPLVST----------LNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQ 86
Cdd:COG4230 545 SAALAAAAEKQWQA-APLIAGeaasgearpvRNPADhSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILER 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 87 IGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGsvipserpNHMMLEmwnPLGIVGVITAFNF 166
Cdd:COG4230 624 AADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFA--------APTVLR---GRGVFVCISPWNF 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 167 PCAvlgwnacI-------ALVCGNCVVWKGAPTTPLITIAMTKLV------AEVLEKnnLPGAiftamcgGAEIGEAIAK 233
Cdd:COG4230 693 PLA-------IftgqvaaALAAGNTVLAKPAEQTPLIAARAVRLLheagvpADVLQL--LPGD-------GETVGAALVA 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 234 DTRIPLVSFTGSSRVGSMVQQTVNARSGK--TLL-ELSGNNAIIVmdDADIQL--AARSVLFAAVGTAGQRCTTCRRLLL 308
Cdd:COG4230 757 DPRIAGVAFTGSTETARLINRTLAARDGPivPLIaETGGQNAMIV--DSSALPeqVVDDVLASAFDSAGQRCSALRVLCV 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 309 HESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQgGKILTGGKAVEG--EGNFVEPTIIEI 386
Cdd:COG4230 835 QEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAE-GRLVHQLPLPEEcaNGTFVAPTLIEI 913
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 30695661 387 SaDAAVVKEELFAPVLYVLKFKSFG-EAV--AINNSvPQGLSSSIFTRNPENI 436
Cdd:COG4230 914 D-SISDLEREVFGPVLHVVRYKADElDKVidAINAT-GYGLTLGVHSRIDETI 964
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
19-478 |
8.86e-52 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 189.80 E-value: 8.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 19 HNLGSYVAG-------KWQA---------NGPLVSTLNPANNQPI-AQVVEASLEDYEQGLKACEEAAKIWmQVTAP-KR 80
Cdd:PRK11809 628 HRLASLSSAllasahqKWQAapmledpvaAGEMSPVINPADPRDIvGYVREATPAEVEQALESAVNAAPIW-FATPPaER 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 81 GDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQlngsvipsERPNhmmlEMWNPLGIVGV 160
Cdd:PRK11809 707 AAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRD--------DFDN----DTHRPLGPVVC 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 161 ITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLV------AEVLEKnnLPGAiftamcgGAEIGEAIAKD 234
Cdd:PRK11809 775 ISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILleagvpAGVVQL--LPGR-------GETVGAALVAD 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 235 TRIPLVSFTGSSRVGSMVQQTVNAR---SGKT---LLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLL 308
Cdd:PRK11809 846 ARVRGVMFTGSTEVARLLQRNLAGRldpQGRPiplIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCL 925
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 309 HESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGE---GNFVEPTIIE 385
Cdd:PRK11809 926 QDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSEDwqsGTFVPPTLIE 1005
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 386 ISaDAAVVKEELFAPVLYVLKFKS--FGEAV-AINNSvPQGLSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPtnGAEIG 462
Cdd:PRK11809 1006 LD-SFDELKREVFGPVLHVVRYNRnqLDELIeQINAS-GYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMV--GAVVG 1081
|
490
....*....|....*..
gi 30695661 463 -GAFGGEKATGGGREAG 478
Cdd:PRK11809 1082 vQPFGGEGLSGTGPKAG 1098
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
39-474 |
6.74e-48 |
|
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: 171.83 E-value: 6.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 39 LNPANNQPIAQVveaSLEDYEQGLKACEEAAKIWMQVT----APKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGI 114
Cdd:cd07148 4 VNPFDLKPIGEV---PTVDWAAIDKALDTAHALFLDRNnwlpAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 115 GEVQEVIDMCDFAVGLSRQLNGSVIP----SERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGA 190
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLGGREIPmgltPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 191 PTTPLITIAMTKLVAEVleknNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVnARSGKTLLELSGN 270
Cdd:cd07148 161 LATPLSCLAFVDLLHEA----GLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKL-APGTRCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 271 NAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKN 350
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 351 FEKGIEVIKSQGGKILTGGKAVeGEGNFvEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIF 429
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGKRL-SDTTY-APTVLlDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 30695661 430 TRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGG 474
Cdd:cd07148 394 TKDLDVALKAVRRL--DATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
40-478 |
2.50e-47 |
|
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: 170.56 E-value: 2.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 40 NPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEG-IGEVQ 118
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 119 EVIDMCDFavgLSRQLNGSVIPSERPNHMMleMW--------NPLGIVGVITAFNFPCAVLgWNACI-ALVCGNCVVWKG 189
Cdd:cd07098 82 VTCEKIRW---TLKHGEKALRPESRPGGLL--MFykrarveyEPLGVVGAIVSWNYPFHNL-LGPIIaALFAGNAIVVKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 190 APTTPLITIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSG 269
Cdd:cd07098 156 SEQVAWSSGFFLSIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 270 NNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESkk 349
Cdd:cd07098 236 KDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPAR-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 350 nFEKGIEVIK---SQGGKILTGGKAV----EGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVP 421
Cdd:cd07098 314 -FDRLEELVAdavEKGARLLAGGKRYphpeYPQGHYFPPTLLvDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695661 422 QGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNiptngaEIGGA-------FGGEKATGGGREAG 478
Cdd:cd07098 393 YGLGASVFGKDIKRARRIASQL--ETGMVAIN------DFGVNyyvqqlpFGGVKGSGFGRFAG 448
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
22-484 |
1.16e-45 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 168.77 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 22 GSYVAGKwqaNGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:PLN02419 120 GSFVESQ---SSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 102 LSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:PLN02419 197 ITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTC 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 182 GNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSG 261
Cdd:PLN02419 277 GNTFILKPSEKDPGASVILAELAMEA----GLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGK 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 262 KTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLL---HESVYDKVLEQLltsyKQVKIGNPLEKGTL 338
Cdd:PLN02419 353 RIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLVERA----KALKVTCGSEPDAD 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 339 LGPLHTPESKKNFEKGIEVIKSQGGKILTGGK--AVEG--EGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEA 413
Cdd:PLN02419 429 LGPVISKQAKERICRLIQSGVDDGAKLLLDGRdiVVPGyeKGNFIGPTILSgVTPDMECYKEEIFGPVLVCMQANSFDEA 508
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30695661 414 VAINNSVPQGLSSSIFTRNPENIFRWigPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGR-----EAGSDSWKQ 484
Cdd:PLN02419 509 ISIINKNKYGNGAAIFTSSGAAARKF--QMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDlnfygKAGVDFFTQ 582
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
22-476 |
1.14e-43 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 161.22 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 22 GSYVAGkwqANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAK--IWMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:PRK09847 26 GEYTAA---AENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 100 RLLSLEMGKIL-----------AEGIGEVQEVIDmcdfavglsrQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPC 168
Cdd:PRK09847 103 LLETLDTGKPIrhslrddipgaARAIRWYAEAID----------KVYGEVATTS-SHELAMIVREPVGVIAAIVPWNFPL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 169 AVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSR 247
Cdd:PRK09847 172 LLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEA----GLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 248 VGSMVQQTVNARSGKTL-LELSGNNAIIVMDDA-DIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYK 325
Cdd:PRK09847 248 TGKQLLKDAGDSNMKRVwLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 326 QVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAveGEGNFVEPTII-EISADAAVVKEELFAPVLYV 404
Cdd:PRK09847 328 NWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNA--GLAAAIGPTIFvDVDPNASLSREEIFGPVLVV 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30695661 405 LKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGSdcGIVNVNiPTNGAEIGGAFGGEKATGGGRE 476
Cdd:PRK09847 406 TRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKA--GSVFVN-NYNDGDMTVPFGGYKQSGNGRD 474
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
23-479 |
1.75e-42 |
|
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: 158.52 E-value: 1.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 23 SYVAGKWQANGPLVSTLNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKldYLGRL 101
Cdd:cd07123 35 LVIGGKEVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGK--YRYEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 102 LSLEM---GK--ILAEgIGEVQEVIDMCDFAVGLSRQLNGsvipsERPNHMMLEMWN-----PL-GIVGVITAFNFpcAV 170
Cdd:cd07123 113 NAATMlgqGKnvWQAE-IDAACELIDFLRFNVKYAEELYA-----QQPLSSPAGVWNrleyrPLeGFVYAVSPFNF--TA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 171 LGWN--ACIALVcGNCVVWKGAPTtplitiAM--TKLVAEVLEKNNLP-GAIFTAMCGGAEIGEAIAKDTRIPLVSFTGS 245
Cdd:cd07123 185 IGGNlaGAPALM-GNVVLWKPSDT------AVlsNYLVYKILEEAGLPpGVINFVPGDGPVVGDTVLASPHLAGLHFTGS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 246 SRVGSMVQQTV-----NARSGKTLL-ELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQ 319
Cdd:cd07123 258 TPTFKSLWKQIgenldRYRTYPRIVgETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKER 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 320 LLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGG-KILTGGKAVEGEGNFVEPTIIEISA-DAAVVKEEL 397
Cdd:cd07123 338 LLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEaEIIAGGKCDDSVGYFVEPTVIETTDpKHKLMTEEI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 398 FAPVL--YVLKFKSFGEAVA-INNSVPQGLSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPTNGAEIGG-AFGGEKATGG 473
Cdd:cd07123 418 FGPVLtvYVYPDSDFEETLElVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKPTGAVVGQqPFGGARASGT 497
|
....*.
gi 30695661 474 GREAGS 479
Cdd:cd07123 498 NDKAGS 503
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
142-485 |
3.37e-40 |
|
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: 150.45 E-value: 3.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 142 ERPNHMMLEMWN--------PLGIVGVITAFNFP-----CAVLGwnaciALVCGNCVVWKGAPTTPlitiAMTKLVAEVL 208
Cdd:cd07135 88 EKVKDGPLAFMFgkprirkePLGVVLIIGPWNYPvllalSPLVG-----AIAAGCTVVLKPSELTP----HTAALLAELV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 209 EKNnLPGAIFTAMCGG-AEIGEAIAKdtRIPLVSFTGSSRVGSMVQQTVNarsgKTL----LELSGNNAIIVMDDADIQL 283
Cdd:cd07135 159 PKY-LDPDAFQVVQGGvPETTALLEQ--KFDKIFYTGSGRVGRIIAEAAA----KHLtpvtLELGGKSPVIVTKNADLEL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 284 AARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKgTLLGPLHTPeskKNFEKGIEVIKSQGG 363
Cdd:cd07135 232 AAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANAS-PDYTRIVNP---RHFNRLKSLLDTTKG 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 364 KILTGGKAVEGEgNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGP 442
Cdd:cd07135 308 KVVIGGEMDEAT-RFIPPTIVsDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTR 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 30695661 443 LGSDCGIVN-----VNIPTngaeigGAFGGEKATGGGREAGSDSWKQY 485
Cdd:cd07135 387 TRSGGVVINdtlihVGVDN------APFGGVGDSGYGAYHGKYGFDTF 428
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
154-436 |
5.71e-39 |
|
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: 146.90 E-value: 5.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 154 PLGIVGVITAFNFPcAVLGWNACI-ALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNnLPGAIFTAMCGGAEIGEAIA 232
Cdd:cd07087 100 PLGVVLIIGPWNYP-LQLALAPLIgAIAAGNTVVLKPSELAP----ATSALLAKLIPKY-FDPEAVAVVEGGVEVATALL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 233 KdTRIPLVSFTGSSRVGSMVQQtvnARSgKTL----LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLL 308
Cdd:cd07087 174 A-EPFDHIFFTGSPAVGKIVME---AAA-KHLtpvtLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 309 HESVYDKVLEQLLTSYKQVkIGNPLEKGTLLGPLhtpESKKNFEKGIEVIksQGGKILTGGKaVEGEGNFVEPTIIE-IS 387
Cdd:cd07087 249 HESIKDELIEELKKAIKEF-YGEDPKESPDYGRI---INERHFDRLASLL--DDGKVVIGGQ-VDKEERYIAPTILDdVS 321
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 30695661 388 ADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENI 436
Cdd:cd07087 322 PDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQ 370
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
154-502 |
3.50e-38 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 145.94 E-value: 3.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 154 PLGIVGVITAFNFPcAVLGWNACI-ALVCGNCVVWKGAPTTPLITIAMTKLVAevlekNNLPGAIFTAMCGGAEIGEAIA 232
Cdd:PTZ00381 109 PLGVVLVIGAWNYP-LNLTLIPLAgAIAAGNTVVLKPSELSPHTSKLMAKLLT-----KYLDPSYVRVIEGGVEVTTELL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 233 KDtRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESV 312
Cdd:PTZ00381 183 KE-PFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 313 YDKVLEQLLTSYKQVkIGNPLEKGTLLGPLHTpesKKNFEKGIEVIKSQGGKILTGGKAVEGEgNFVEPTII-EISADAA 391
Cdd:PTZ00381 262 KDKFIEALKEAIKEF-FGEDPKKSEDYSRIVN---EFHTKRLAELIKDHGGKVVYGGEVDIEN-KYVAPTIIvNPDLDSP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 392 VVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGS------DC--GIVNVNIPtngaeigg 463
Cdd:PTZ00381 337 LMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSgavvinDCvfHLLNPNLP-------- 408
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 30695661 464 aFGGEKATGGGREAGSDSWKQYMR-RSTCTINYGNELPLA 502
Cdd:PTZ00381 409 -FGGVGNSGMGAYHGKYGFDTFSHpKPVLNKSTGNSFDLS 447
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
59-489 |
1.78e-37 |
|
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: 143.15 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 59 EQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLD--YLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNG 136
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYdiAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 137 SV--IPSERPNHMMLEMWnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEknnLP 214
Cdd:cd07084 82 PGnhLGQGLKQQSHGYRW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGL---LP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 215 GAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVqqTVNARSGKTLLELSG-NNAIIVMDDADIQLAARSVLFAAV 293
Cdd:cd07084 158 PEDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGfNWKVLGPDAQAVDYVAWQCVQDMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 294 GTAGQRCTTCRRLLLHES-----VYDKVLEQLLTSykqvkignpLEKGTLLGPLHTPeskkNFEKGIEVIKSQGGKILT- 367
Cdd:cd07084 236 ACSGQKCTAQSMLFVPENwsktpLVEKLKALLARR---------KLEDLLLGPVQTF----TTLAMIAHMENLLGSVLLf 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 368 GGKAV------EGEGNFVEP----TIIEISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSV-PQG-LSSSIFTRNPEN 435
Cdd:cd07084 303 SGKELknhsipSIYGACVASalfvPIDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLErMHGsLTAAIYSNDPIF 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 30695661 436 IFRWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREA--GSDSWKQYMRRS 489
Cdd:cd07084 383 LQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGigGPEAIKLVWRCH 438
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
154-490 |
3.48e-36 |
|
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: 139.56 E-value: 3.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 154 PLGIVGVITAFNFPcavlgWNACI-----ALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLpgaifTAMCGGAEIG 228
Cdd:cd07136 100 PYGVVLIIAPWNYP-----FQLALapligAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYV-----AVVEGGVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 229 EAIAkDTRIPLVSFTGSSRVGsmvqQTVNARSGKTL----LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCR 304
Cdd:cd07136 170 QELL-DQKFDYIFFTGSVRVG----KIVMEAAAKHLtpvtLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 305 RLLLHESVYDKVLEQLLtsyKQVKIGNPLEkgtllgPLHTPE-----SKKNFEKGIEVIKsqGGKILTGGKAvEGEGNFV 379
Cdd:cd07136 245 YVLVHESVKEKFIKELK---EEIKKFYGED------PLESPDygriiNEKHFDRLAGLLD--NGKIVFGGNT-DRETLYI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 380 EPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIG--PLGSDC------GIV 450
Cdd:cd07136 313 EPTILdNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLEnlSFGGGCindtimHLA 392
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 30695661 451 NVNIPtngaeiggaFGGEKATGGGREAGSDSW------KQYMRRST 490
Cdd:cd07136 393 NPYLP---------FGGVGNSGMGSYHGKYSFdtfshkKSILKKST 429
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
24-432 |
1.90e-33 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 132.57 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 24 YVAGKWQ--ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:PLN00412 19 YADGEWRtsSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 102 LSLEMGKILAEGIGEVQEVIDMCDFA-------VGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWN 174
Cdd:PLN00412 99 LVKEIAKPAKDAVTEVVRSGDLISYTaeegvriLGEGKFLVSDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 175 ACIALVCGNCVVWKgAPTTPLITIAMTklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGS------SR 247
Cdd:PLN00412 179 IAPALIAGNAVVLK-PPTQGAVAALHM---VHCFHLAGFPKGLISCVTGkGSEIGDFLTMHPGVNCISFTGGdtgiaiSK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 248 VGSMVQQTvnarsgktlLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQV 327
Cdd:PLN00412 255 KAGMVPLQ---------MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 328 KIGNPlEKGTLLGPLHTpESKKNFEKG-IEVIKSQGGKILTGGKAvegEGNFVEPTIIE-ISADAAVVKEELFAPVLYVL 405
Cdd:PLN00412 326 TVGPP-EDDCDITPVVS-ESSANFIEGlVMDAKEKGATFCQEWKR---EGNLIWPLLLDnVRPDMRIAWEEPFGPVLPVI 400
|
410 420
....*....|....*....|....*..
gi 30695661 406 KFKSFGEAVAINNSVPQGLSSSIFTRN 432
Cdd:PLN00412 401 RINSVEEGIHHCNASNFGLQGCVFTRD 427
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
72-478 |
2.03e-31 |
|
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: 125.80 E-value: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 72 WMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAE-GIGEVQEVIDMCDFAVglsRQLNGSVIPSERPNHMMLE 150
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEvDLTEILPVLSEINHAI---KHLKKWMKPKRVRTPLLLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 151 ------MWNPLGIVGVITAFNFP-CAVLGWNACiALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLpgAIFTamcG 223
Cdd:cd07134 91 gtkskiRYEPKGVCLIISPWNYPfNLAFGPLVS-AIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV--AVFE---G 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 224 GAEIGEAIAKdtrIPL--VSFTGSSRVGSMVQqtvnARSGKTL----LELSGNNAIIVMDDADIQLAARSVLFAAVGTAG 297
Cdd:cd07134 165 DAEVAQALLE---LPFdhIFFTGSPAVGKIVM----AAAAKHLasvtLELGGKSPTIVDETADLKKAAKKIAWGKFLNAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 298 QRCTTCRRLLLHESVYDKVLEQLLTSYKQVKignplekGTLLGPLHTPE-----SKKNFE--KG-IEVIKSQGGKILTGG 369
Cdd:cd07134 238 QTCIAPDYVFVHESVKDAFVEHLKAEIEKFY-------GKDAARKASPDlarivNDRHFDrlKGlLDDAVAKGAKVEFGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 370 KAVEGEgNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGS-DC 447
Cdd:cd07134 311 QFDAAQ-RYIAPTVLTnVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSgGV 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 30695661 448 GI-------VNVNIPtngaeiggaFGGEKATGGGREAG 478
Cdd:cd07134 390 VVndvvlhfLNPNLP---------FGGVNNSGIGSYHG 418
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
21-489 |
1.13e-30 |
|
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: 124.69 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 21 LGSYVAGKWQAN-GPLVSTLNPANNQPIAQVVEASLeDYEQGLK-ACEEAAKIWMQVTAPKRGDIVRQIGDALR------ 92
Cdd:cd07128 1 LQSYVAGQWHAGtGDGRTLHDAVTGEVVARVSSEGL-DFAAAVAyAREKGGPALRALTFHERAAMLKALAKYLMerkedl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 93 -------------SKLD------------YLGRLLsLEMGKILAEGIGEVqevidmcdfavgLSRqlNGSVIPSerpnHM 147
Cdd:cd07128 80 yalsaatgatrrdSWIDidggigtlfayaSLGRRE-LPNAHFLVEGDVEP------------LSK--DGTFVGQ----HI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 148 mlemWNPLGIVGV-ITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMtklVAEVLEKNNLPGAIFTAMCGGAe 226
Cdd:cd07128 141 ----LTPRRGVAVhINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAV---VKDIVESGLLPEGALQLICGSV- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 227 iGEAIAKDTRIPLVSFTGSSRVGSM--VQQTVNARSGKTLLEL-SGNNAII----VMDDADIQLAARSVLFAAVGTAGQR 299
Cdd:cd07128 213 -GDLLDHLGEQDVVAFTGSAATAAKlrAHPNIVARSIRFNAEAdSLNAAILgpdaTPGTPEFDLFVKEVAREMTVKAGQK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 300 CTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIkSQGGKILTGGKAVE------ 373
Cdd:cd07128 292 CTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATL-LAEAEVVFGGPDRFevvgad 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 374 -GEGNFVEPTII--EISADAAVVKE-ELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGSDCGI 449
Cdd:cd07128 371 aEKGAFFPPTLLlcDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPYHGR 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 30695661 450 VNVNIPTNGAEIGG--------AFGGEKATGGGRE-AGSDSWKQYMRRS 489
Cdd:cd07128 451 LLVLNRDSAKESTGhgsplpqlVHGGPGRAGGGEElGGLRGVKHYMQRT 499
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
152-498 |
8.31e-29 |
|
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: 118.48 E-value: 8.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 152 WNPLGIVGVITAFNFPCAVL-----GwnaciALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNnLPGAIFTAMCGGAE 226
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQLTlvplvG-----AIAAGNCVVIKPSEVSP----ATAKLLAELIPKY-LDKECYPVVLGGVE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 227 IGEAIAKDtRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRL 306
Cdd:cd07132 168 ETTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 307 LLHESVYDKVLEQLLTSYKQVkIGNPLEKGTLLGPLhtpESKKNFEKGIEVIKsqGGKILTGGKAVEGEgNFVEPTI-IE 385
Cdd:cd07132 247 LCTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRI---INDRHFQRLKKLLS--GGKVAIGGQTDEKE-RYIAPTVlTD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 386 ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGplGSDCGIVNVN----------IP 455
Cdd:cd07132 320 VKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILS--NTSSGGVCVNdtimhytldsLP 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 30695661 456 tngaeiggaFGGEKATGGGREAGSDSWKQYMRRSTCTI-NYGNE 498
Cdd:cd07132 398 ---------FGGVGNSGMGAYHGKYSFDTFSHKRSCLVkSLNME 432
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
21-489 |
1.78e-26 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 112.49 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 21 LGSYVAGKWQA-NGPLVSTLNPANNQPIAQVVEASLeDYEQGLK-ACEEAAKIWMQVTAPKRGDIVRQIGDALR------ 92
Cdd:PRK11903 5 LANYVAGRWQAgSGAGTPLFDPVTGEELVRVSATGL-DLAAAFAfAREQGGAALRALTYAQRAALLAAIVKVLQanrday 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 93 --------------SKLDYLGRLLSLEMGKILAEGIGEVQEVIDmcDFAVGLSRQlngsviPSERPNHMmlemWNPLGIV 158
Cdd:PRK11903 84 ydiatansgttrndSAVDIDGGIFTLGYYAKLGAALGDARLLRD--GEAVQLGKD------PAFQGQHV----LVPTRGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 159 GV-ITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMtklVAEVLEKNNLPGAIFTAMCGGAeiGEAIAKDTRI 237
Cdd:PRK11903 152 ALfINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRM---VKDVVAAGILPAGALSVVCGSS--AGLLDHLQPF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 238 PLVSFTGSSRVGSMVQQ--TVNARSGKTLLELSGNNAIIVMDDAD-----IQLAARSVLFAAVGTAGQRCTTCRRLLLHE 310
Cdd:PRK11903 227 DVVSFTGSAETAAVLRShpAVVQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 311 SVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQgGKILTGGKAVE------GEGNFVEPTII 384
Cdd:PRK11903 307 ALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQ-AEVLFDGGGFAlvdadpAVAACVGPTLL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 385 EIS-ADAA--VVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPTNGAEI 461
Cdd:PRK11903 386 GASdPDAAtaVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADSHGRVHVISPDVAALH 465
|
490 500 510
....*....|....*....|....*....|....*..
gi 30695661 462 GG--------AFGGEKATGGGRE-AGSDSWKQYMRRS 489
Cdd:PRK11903 466 TGhgnvmpqsLHGGPGRAGGGEElGGLRALAFYHRRS 502
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
154-436 |
7.54e-23 |
|
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: 101.02 E-value: 7.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 154 PLGIVGVITAFNFPC--AVLGwnACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLpgAIFTamcGGAEIGEAI 231
Cdd:cd07133 101 PLGVVGIIVPWNYPLylALGP--LIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV--AVVT---GGADVAAAF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 232 akdTRIP---LVsFTGSSRVGSMVQQtvNArsGKTL----LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCR 304
Cdd:cd07133 174 ---SSLPfdhLL-FTGSTAVGRHVMR--AA--AENLtpvtLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 305 RLLLHESVYDKVLEQLLTSYKQvkignplekgtllgplHTPESKKN-----------FE--KG-IEVIKSQGGKILTGGK 370
Cdd:cd07133 246 YVLVPEDKLEEFVAAAKAAVAK----------------MYPTLADNpdytsiinerhYArlQGlLEDARAKGARVIELNP 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30695661 371 AVE--GEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENI 436
Cdd:cd07133 310 AGEdfAATRKLPPTLVlNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQ 378
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
154-482 |
4.39e-22 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 98.64 E-value: 4.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 154 PLGIVGVITAFNFPCA-----VLGwnaciALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNnlpgAIfTAMCGGAEIG 228
Cdd:cd07137 101 PLGVVLVISAWNFPFLlslepVIG-----AIAAGNAVVLKPSELAPATSALLAKLIPEYLDTK----AI-KVIEGGVPET 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 229 EAIAkDTRIPLVSFTGSSRVGSMVQqtvnARSGKTL----LELSGNNAIIVMDDADIQLAARSVLFAAVGT-AGQRCTTC 303
Cdd:cd07137 171 TALL-EQKWDKIFFTGSPRVGRIIM----AAAAKHLtpvtLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 304 RRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLlgplHTPESKKNFE--KGIEVIKSQGGKILTGGkAVEGEGNFVEP 381
Cdd:cd07137 246 DYVLVEESFAPTLIDALKNTLEKFFGENPKESKDL----SRIVNSHHFQrlSRLLDDPSVADKIVHGG-ERDEKNLYIEP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 382 TII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNpENIFRWIGPLGSDCGIVNVNIPTNGAE 460
Cdd:cd07137 321 TILlDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKN-KELKRRIVAETSSGGVTFNDTVVQYAI 399
|
330 340
....*....|....*....|..
gi 30695661 461 IGGAFGGEKATGGGREAGSDSW 482
Cdd:cd07137 400 DTLPFGGVGESGFGAYHGKFSF 421
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
59-428 |
1.99e-20 |
|
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: 93.76 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 59 EQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGE--------------------VQ 118
Cdd:cd07129 2 DAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGElgrttgqlrlfadlvregswLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 119 EVIDMCDFAvglsRQlngsviPSERPNHMMLEMwnPLGIVGVITAFNFPCA--VLGWNACIALVCGNCVVWKGAPTTPLI 196
Cdd:cd07129 82 ARIDPADPD----RQ------PLPRPDLRRMLV--PLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAHPAHPGT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 197 TIAMTKLVAEVLEKNNLPGAIFTAM-CGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNAR-SGKTL-LELSGNNAI 273
Cdd:cd07129 150 SELVARAIRAALRATGLPAGVFSLLqGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARpEPIPFyAELGSVNPV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 274 IVMDDAdiqLAARSVLFAA--VGT----AGQRCTTCRRLLLHESV-YDKVLEQLLTSYKQVKignpleKGTLLgplhTPE 346
Cdd:cd07129 230 FILPGA---LAERGEAIAQgfVGSltlgAGQFCTNPGLVLVPAGPaGDAFIAALAEALAAAP------AQTML----TPG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 347 SKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIEISADA----AVVKEELFAPVLYVLKFKSFGEAVAINNSVPQ 422
Cdd:cd07129 297 IAEAYRQGVEALAAAPGVRVLAGGAAAEGGNQAAPTLFKVDAAAfladPALQEEVFGPASLVVRYDDAAELLAVAEALEG 376
|
....*.
gi 30695661 423 GLSSSI 428
Cdd:cd07129 377 QLTATI 382
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
154-440 |
9.75e-19 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 89.02 E-value: 9.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 154 PLGIVGVITAFNFPCAvLGWNACI-ALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLPGAIfTAMCGGAEIGEAIA 232
Cdd:PLN02203 108 PLGVVLIFSSWNFPIG-LSLEPLIgAIAAGNAVVLKPSELAP----ATSAFLAANIPKYLDSKAV-KVIEGGPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 233 kDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIV--MDDA-DIQLAARSVLFAAVGT-AGQRCTTCRRLLL 308
Cdd:PLN02203 182 -QHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIAIDYVLV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 309 HESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLhtpeSKKNFEKGIEVIK--SQGGKILTGGkAVEGEGNFVEPTII-E 385
Cdd:PLN02203 261 EERFAPILIELLKSTIKKFFGENPRESKSMARIL----NKKHFQRLSNLLKdpRVAASIVHGG-SIDEKKLFIEPTILlN 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 30695661 386 ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNpENIFRWI 440
Cdd:PLN02203 336 PPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNN-EKLKRRI 389
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
154-488 |
8.02e-18 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 85.87 E-value: 8.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEknnlPGAIftAMCGGAEIGEAIAK 233
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLD----SSAV--RVVEGAVTETTALL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 234 DTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVG-TAGQRCTTCRRLLLHESV 312
Cdd:PLN02174 186 EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEY 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 313 YDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTpeskKNFEKGIEVI--KSQGGKILTGGKAvEGEGNFVEPTI-IEISAD 389
Cdd:PLN02174 266 APKVIDAMKKELETFYGKNPMESKDMSRIVNS----THFDRLSKLLdeKEVSDKIVYGGEK-DRENLKIAPTIlLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 390 AAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgSDCGIVNVNIPTNGAEIGGAFGGEK 469
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATV-SAGGIVVNDIAVHLALHTLPFGGVG 419
|
330
....*....|....*....
gi 30695661 470 ATGGGREAGSDSWKQYMRR 488
Cdd:PLN02174 420 ESGMGAYHGKFSFDAFSHK 438
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
154-439 |
6.21e-17 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 83.68 E-value: 6.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 154 PLGIVGVITAFNFPCavlgWNA----CIALVCGNCVVWKGAPTTPLiTIAMTKLVA-EVLEKNNLPGAIFT--AMCGGAE 226
Cdd:cd07127 193 PRGVALVIGCSTFPT----WNGypglFASLATGNPVIVKPHPAAIL-PLAITVQVArEVLAEAGFDPNLVTlaADTPEEP 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 227 IGEAIAKDTRIPLVSFTGSSRVGSMVQQtvNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRL 306
Cdd:cd07127 268 IAQTLATRPEVRIIDFTGSNAFGDWLEA--NARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 307 LL----------HESvYDKVLEQLLTSYKQVkIGNPLEKGTLLGPLHTPESKKNFEKGievikSQGGKILTGGKAVEG-- 374
Cdd:cd07127 346 YVprdgiqtddgRKS-FDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARIAEA-----RQLGEVLLASEAVAHpe 418
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695661 375 -EGNFVE-PTIIEI-SADAAVVKEELFAPVLYVLKFKSFGEAVAI-NNSVPQ--GLSSSIFTRNPENIFRW 439
Cdd:cd07127 419 fPDARVRtPLLLKLdASDEAAYAEERFGPIAFVVATDSTDHSIELaRESVREhgAMTVGVYSTDPEVVERV 489
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
23-408 |
2.98e-12 |
|
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: 68.68 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 23 SYVAGKWQANGPLVSTLNPANNQP---IAQVVEASLEDYEQGLKACEEAAkIWMQVTAPKR----GDIVRQIGDALRSKL 95
Cdd:cd07126 1 NLVAGKWKGASNYTTLLDPLNGDKfisVPDTDEDEINEFVDSLRQCPKSG-LHNPLKNPERyllyGDVSHRVAHELRKPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 96 --DYLGRLLSLEMGKILAEGIGEV---QEVI-----DMCDFavgLSRQLNgsvIPSERPNHMMLEMWNPLGIVGVITAFN 165
Cdd:cd07126 80 veDFFARLIQRVAPKSDAQALGEVvvtRKFLenfagDQVRF---LARSFN---VPGDHQGQQSSGYRWPYGPVAIITPFN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 166 FPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGS 245
Cdd:cd07126 154 FPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLC----GMPATDVDLIHSDGPTMNKILLEANPRMTLFTGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 246 SRVGsmvQQTVNARSGKTLLELSGNN-AIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHEsvyDKVLEQLLTSY 324
Cdd:cd07126 230 SKVA---ERLALELHGKVKLEDAGFDwKILGPDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAHE---NWVQAGILDKL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 325 KQVKIGNPLEKGTlLGPLHTPESKKNFEKGIEVIKSQGGKILTGGK------------AVEGEGNFVEPTIIEISADAAV 392
Cdd:cd07126 304 KALAEQRKLEDLT-IGPVLTWTTERILDHVDKLLAIPGAKVLFGGKpltnhsipsiygAYEPTAVFVPLEEIAIEENFEL 382
|
410
....*....|....*.
gi 30695661 393 VKEELFAPVLYVLKFK 408
Cdd:cd07126 383 VTTEVFGPFQVVTEYK 398
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
139-462 |
1.50e-10 |
|
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: 63.05 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 139 IPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLP-GAI 217
Cdd:cd07081 80 VLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPeNLI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 218 FTAMCGGAEIGEAIAKDTRIPLVSFTGSSrvgSMVQQTvnARSGKTLLEL-SGNNAIIVMDDADIQLAARSVLFAAVGTA 296
Cdd:cd07081 160 GWIDNPSIELAQRLMKFPGIGLLLATGGP---AVVKAA--YSSGKPAIGVgAGNTPVVIDETADIKRAVQSIVKSKTFDN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 297 GQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKgtllgplHTPESKKNFEKGIEVIKSQGGKILT-GGKAVEGE 375
Cdd:cd07081 235 GVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQ-------VQPVILKNGDVNRDIVGQDAYKIAAaAGLKVPQE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 376 GN--FVEPTIIEISADAAvvkEELFAPVLYVLKFKSFGEAVAINNSVPQ----GLSSSIFTRN---PENIFRWIGPLgsD 446
Cdd:cd07081 308 TRilIGEVTSLAEHEPFA---HEKLSPVLAMYRAANFADADAKALALKLeggcGHTSAMYSDNikaIENMNQFANAM--K 382
|
330
....*....|....*.
gi 30695661 447 CGIVNVNIPTNGAEIG 462
Cdd:cd07081 383 TSRFVKNGPCSQGGLG 398
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
154-346 |
1.16e-08 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 57.23 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 154 PLGIVGVITAFNFPCAVLgWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAK 233
Cdd:cd07077 100 PIGVTMHILPSTNPLSGI-TSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILVLYVPHPSDELAEELLS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 234 DTRIPLVSFTGSSrvgSMVQQTVNARSGKTLLELSGNNAIIVMDD-ADIQLAARSVLFAAVgTAGQRCTTCRRLLLHESV 312
Cdd:cd07077 179 HPKIDLIVATGGR---DAVDAAVKHSPHIPVIGFGAGNSPVVVDEtADEERASGSVHDSKF-FDQNACASEQNLYVVDDV 254
|
170 180 190
....*....|....*....|....*....|....*..
gi 30695661 313 YDKVLEQLLT--SYKQVKI-GNPLEKGTLLGPLHTPE 346
Cdd:cd07077 255 LDPLYEEFKLklVVEGLKVpQETKPLSKETTPSFDDE 291
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
56-471 |
2.66e-06 |
|
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: 49.54 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 56 EDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLlslemgkILAE-GIGEVQEVIdmcdfavgLSRQL 134
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEM-------AVEEtGMGRVEDKI--------AKNHL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 135 NGSVIPSERP---------NHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVA 205
Cdd:cd07121 69 AAEKTPGTEDltttawsgdNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELIN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 206 EVLEKNNLPGAIFTAMCGGA-EIGEAIAKDTRIPLVSFTGSSRVGSMVQQtvnarSGKTLLEL-SGNNAIIVMDDADIQL 283
Cdd:cd07121 149 KAIAEAGGPDNLVVTVEEPTiETTNELMAHPDINLLVVTGGPAVVKAALS-----SGKKAIGAgAGNPPVVVDETADIEK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 284 AARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLtSYKQVKIGNP-----LEKGTLLGPLHTPeSKKNFEKGIEVI 358
Cdd:cd07121 224 AARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQ-RNGAYVLNDEqaeqlLEVVLLTNKGATP-NKKWVGKDASKI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695661 359 KSQGGKILTGGKAVegegnfvepTIIEISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGL--SSSIFTRNPENI 436
Cdd:cd07121 302 LKAAGIEVPADIRL---------IIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENL 372
|
410 420 430
....*....|....*....|....*....|....*
gi 30695661 437 FRWIGPLgsDCGIVNVNIPTnGAEIGgaFGGEKAT 471
Cdd:cd07121 373 TKMARAM--QTTIFVKNGPS-YAGLG--VGGEGYT 402
|
|
| |
