|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
30-335 |
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: 625.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 30 STSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNN 109
Cdd:cd07130 170 TTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNN 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 110 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMF 189
Cdd:cd07130 250 AIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNY 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 190 LGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLgHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT 269
Cdd:cd07130 330 LAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGL-SDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFT 408
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194380572 270 KDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYS 335
Cdd:cd07130 409 TDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
30-335 |
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: 587.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 30 STSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNN 109
Cdd:cd07086 171 TTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNN 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 110 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMF 189
Cdd:cd07086 251 AIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKY 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 190 LGAVEEAKKEGGTVVYGGKVMDR--PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSI 267
Cdd:cd07086 331 LNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSI 410
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194380572 268 FTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYS 335
Cdd:cd07086 411 FTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
30-346 |
1.79e-156 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 448.51 E-value: 1.79e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 30 STSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNN 109
Cdd:PLN02315 192 TTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNN 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 110 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMF 189
Cdd:PLN02315 272 AIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNF 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 190 LGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTgLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT 269
Cdd:PLN02315 352 EKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFT 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194380572 270 KDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYSKDLPLAQGIKF 346
Cdd:PLN02315 431 RNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTINYGNELPLAQGINF 507
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
31-332 |
5.23e-117 |
|
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: 345.35 E-value: 5.23e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 31 TSLISVAVTKIIAKVLednkLPGAICSLTCGGAD-IGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNN 109
Cdd:cd07078 135 TPLTALLLAELLAEAG----LPPGVLNVVTGDGDeVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 110 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMF 189
Cdd:cd07078 211 PLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRV 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 190 LGAVEEAKKEGGTVVYGGKVMDR-PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIF 268
Cdd:cd07078 291 LAYIEDAKAEGAKLLCGGKRLEGgKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVF 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194380572 269 TKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 332
Cdd:cd07078 371 TRDLERALRVA--ERLEAGTVWINDYSVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
41-334 |
2.55e-110 |
|
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: 329.78 E-value: 2.55e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADL 119
Cdd:COG1012 186 LLAELLEEAGLPaGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 120 SLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKE 199
Cdd:COG1012 266 DAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 200 GGTVVYGGKVMDR-PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRW 278
Cdd:COG1012 346 GAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRV 425
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 194380572 279 LgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 334
Cdd:COG1012 426 A--RRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
41-329 |
5.14e-110 |
|
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: 328.34 E-value: 5.14e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADL 119
Cdd:pfam00171 171 LLAELFEEAGLPaGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 120 SLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKE 199
Cdd:pfam00171 251 DAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 200 GGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWL 279
Cdd:pfam00171 331 GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVA 410
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 194380572 280 gpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRST 329
Cdd:pfam00171 411 --RRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
37-335 |
1.69e-82 |
|
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: 258.43 E-value: 1.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 37 AVTKIIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFE 115
Cdd:cd07131 176 ACALKLVELFAEAGLPpGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMD 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 116 DADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEE 195
Cdd:cd07131 256 DADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEI 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 196 AKKEGGTVVYGGKVMDR----PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 271
Cdd:cd07131 336 GKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTED 415
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194380572 272 LGRIFRWLGpkgsDC--GIVNVNIPTSGAEIGGAFGGEKHTGGG-RESGSDAWKQYMRRSTCTINYS 335
Cdd:cd07131 416 VNKAFRARR----DLeaGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYVDYS 478
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
30-332 |
3.12e-76 |
|
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: 238.67 E-value: 3.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 30 STSLISVAVTKIIAKVLednkLPGAICSLTCGGAD-IGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGN 108
Cdd:cd06534 130 LTPLTALALAELLQEAG----LPPGVVNVVPGGGDeVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 109 NAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKkayaqirvgnpwdpnvlygplhtkqavsm 188
Cdd:cd06534 206 SPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDEFVEKLV----------------------------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 189 flgaveeakkeggtvvyggkvmdrpgnyvepTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIF 268
Cdd:cd06534 257 -------------------------------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVF 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194380572 269 TKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 332
Cdd:cd06534 306 TRDLNRALRVA--ERLRAGTVYINDSSIGVGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
41-324 |
9.08e-76 |
|
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: 239.74 E-value: 9.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGlmvqERFGRSL----LELGGNNAIIAFE 115
Cdd:cd07104 144 LIAEIFEEAGLPkGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIG----ELAGRHLkkvaLELGGNNPLIVLD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 116 DADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEE 195
Cdd:cd07104 220 DADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVED 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 196 AKKEGGTVVYGGKvmdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRI 275
Cdd:cd07104 300 AVAAGARLLTGGT---YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERA 376
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 194380572 276 FRwLGpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQY 324
Cdd:cd07104 377 MA-FA-ERLETGMVHINDQTVNDEPHVPFGGVKASGGGRFGGPASLEEF 423
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
52-326 |
5.82e-75 |
|
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: 238.22 E-value: 5.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 52 PGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAV 131
Cdd:cd07114 176 PGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 132 GTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMD 211
Cdd:cd07114 256 AAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGERPS 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 212 RP----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCG 287
Cdd:cd07114 336 GAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRV--ARAIEAG 413
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 194380572 288 IVNVNI-----PTSgaeiggAFGGEKHTGGGRESGSDAWKQYMR 326
Cdd:cd07114 414 TVWVNTyralsPSS------PFGGFKDSGIGRENGIEAIREYTQ 451
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
42-325 |
1.19e-74 |
|
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: 237.33 E-value: 1.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 42 IAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvgLMVQ--ERFGRSLLELGGNNAIIAFEDAD 118
Cdd:cd07103 163 LAELAEEAGLPaGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKL--LMAQaaDTVKRVSLELGGNAPFIVFDDAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 119 LSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKK 198
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 199 EGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRw 278
Cdd:cd07103 321 KGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWR- 399
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 194380572 279 LGpKGSDCGIVNVNIPT-SGAEIggAFGGEKHTGGGRESGSDAWKQYM 325
Cdd:cd07103 400 VA-EALEAGMVGINTGLiSDAEA--PFGGVKESGLGREGGKEGLEEYL 444
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
34-320 |
2.23e-72 |
|
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: 232.14 E-value: 2.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 34 ISVAVTKIIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAII 112
Cdd:cd07097 173 LTPASAWALVEILEEAGLPAGVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLV 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 113 AFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGA 192
Cdd:cd07097 253 VLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRY 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 193 VEEAKKEGGTVVYGGKVMDRP--GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTK 270
Cdd:cd07097 333 IEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTT 412
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 194380572 271 DLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTG-GGRESGSDA 320
Cdd:cd07097 413 SLKHATHFK--RRVEAGVVMVNLPTAGVDYHVPFGGRKGSSyGPREQGEAA 461
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
41-317 |
5.09e-68 |
|
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: 220.64 E-value: 5.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADL 119
Cdd:cd07151 176 LLAKIFEEAGLPKGVLNVVVGaGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 120 SLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKE 199
Cdd:cd07151 256 DAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 200 GGTVVYGGKVMdrpGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWl 279
Cdd:cd07151 336 GATLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQF- 411
|
250 260 270
....*....|....*....|....*....|....*...
gi 194380572 280 gPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESG 317
Cdd:cd07151 412 -ARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNG 448
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
31-326 |
1.87e-66 |
|
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: 216.04 E-value: 1.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 31 TSLISVAVTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNA 110
Cdd:cd07092 157 TPLTTLLLAELAAEVLP----PGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 111 IIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFL 190
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 191 GAVEEAKKeGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTK 270
Cdd:cd07092 313 GFVERAPA-HARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 194380572 271 DLGRIFRWLGPKGSDCGIVNVNIPTSgAEIggAFGGEKHTGGGRESGSDAWKQYMR 326
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLA-AEM--PHGGFKQSGYGKDLSIYALEDYTR 444
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
52-325 |
1.13e-65 |
|
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: 214.41 E-value: 1.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 52 PGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAV 131
Cdd:cd07089 180 AGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCM 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 132 GTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKvmd 211
Cdd:cd07089 260 HNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGG--- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 212 RP-----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGR---IFRWLgpkg 283
Cdd:cd07089 337 RPagldkGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRayrVARRI---- 412
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 194380572 284 sDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYM 325
Cdd:cd07089 413 -RTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
41-318 |
4.42e-64 |
|
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: 209.88 E-value: 4.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKqvglMVQERFGRSL----LELGGNNAIIAFE 115
Cdd:cd07150 164 KIAEIMEEAGLPkGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGR----EIAEKAGRHLkkitLELGGKNPLIVLA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 116 DADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEE 195
Cdd:cd07150 240 DADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 196 AKKEGGTVVYGGKvmdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRI 275
Cdd:cd07150 320 AVAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRA 396
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 194380572 276 FRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGS 318
Cdd:cd07150 397 FKL--AERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGE 437
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
24-315 |
5.37e-64 |
|
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: 209.76 E-value: 5.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 24 RPAAFmsTSLISVAvtkiIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVglmvQERFG--R 100
Cdd:cd07149 157 KPASQ--TPLSALK----LAELLLEAGLPkGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAI----ARKAGlkK 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 101 SLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPL 180
Cdd:cd07149 227 VTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPM 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 181 HTKQAVSMFLGAVEEAKKEGGTVVYGGKvmdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 260
Cdd:cd07149 307 ISEAEAERIEEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSP 383
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 194380572 261 QGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKHTGGGRE 315
Cdd:cd07149 384 YGLQAGVFTNDLQKALKAA--RELEVGGVMINdSSTFRVD-HMPYGGVKESGTGRE 436
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
41-320 |
2.04e-63 |
|
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: 208.19 E-value: 2.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADL 119
Cdd:cd07093 162 LLAELANEAGLPPGVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 120 SLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKE 199
Cdd:cd07093 242 DRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 200 GGTVVYGGKVMDRP----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRI 275
Cdd:cd07093 322 GATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRA 401
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 194380572 276 FRWlgPKGSDCGIVNVN------IPTsgaeiggAFGGEKHTGGGRESGSDA 320
Cdd:cd07093 402 HRV--ARRLEAGTVWVNcwlvrdLRT-------PFGGVKASGIGREGGDYS 443
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
42-332 |
1.48e-62 |
|
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: 206.06 E-value: 1.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 42 IAKVLEDNKLPGAICSLTCGG-ADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERfgRSLLELGGNNAIIAFEDADLS 120
Cdd:cd07146 166 LADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--RQLLELGGNDPLIVMDDADLE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 121 LVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEG 200
Cdd:cd07146 244 RAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQG 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 201 GTVVYGGKvmdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLg 280
Cdd:cd07146 324 ARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLV- 399
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 194380572 281 pKGSDCGIVNVN------IPTSgaeiggAFGGEKHTG-GGRESGSDAWKQYMRRSTCTI 332
Cdd:cd07146 400 -ERLDVGTVNVNevpgfrSELS------PFGGVKDSGlGGKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
42-277 |
3.68e-62 |
|
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: 205.19 E-value: 3.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 42 IAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLS 120
Cdd:cd07088 179 FAELVDEAGLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLD 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 121 LVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEG 200
Cdd:cd07088 259 LAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAVEAG 338
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194380572 201 GTVVYGGKVMD-RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR 277
Cdd:cd07088 339 ATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMR 416
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
42-316 |
1.50e-61 |
|
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: 203.35 E-value: 1.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 42 IAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLS 120
Cdd:cd07145 169 LAKILEEAGLPpGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 121 LVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEG 200
Cdd:cd07145 249 RAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKG 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 201 GTVVYGGKVMDrpGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlg 280
Cdd:cd07145 329 GKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKV-- 404
|
250 260 270
....*....|....*....|....*....|....*.
gi 194380572 281 PKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES 316
Cdd:cd07145 405 ARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREG 440
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
1-324 |
4.59e-61 |
|
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: 202.28 E-value: 4.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 1 MWRLPRAL---CVHAAKTSKLsgpwsrpaafmsTSLISVAVTKIIAKVlednKLPGAICSLTCG-GADIGTAMAKDERVN 76
Cdd:cd07115 135 AWKVAPALaagNTVVLKPAEL------------TPLSALRIAELMAEA----GFPAGVLNVVTGfGEVAGAALVEHPDVD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 77 LLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVN 156
Cdd:cd07115 199 KITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 157 RLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTET 236
Cdd:cd07115 279 RFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEI 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 237 FAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNipTSGA-EIGGAFGGEKHTGGGRE 315
Cdd:cd07115 359 FGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRV--AAALKAGTVWIN--TYNRfDPGSPFGGYKQSGFGRE 434
|
....*....
gi 194380572 316 SGSDAWKQY 324
Cdd:cd07115 435 MGREALDEY 443
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
42-315 |
4.64e-61 |
|
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: 201.53 E-value: 4.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 42 IAKVLEDNKLP-GAICSLTCGGADIGTAMAkDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLS 120
Cdd:cd07100 142 IEELFREAGFPeGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLD 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 121 LVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEG 200
Cdd:cd07100 221 KAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 201 GTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLG---RIFR 277
Cdd:cd07100 301 ATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLEraeRVAR 380
|
250 260 270
....*....|....*....|....*....|....*....
gi 194380572 278 WLgpkgsDCGIVNVNIPT-SGAEIggAFGGEKHTGGGRE 315
Cdd:cd07100 381 RL-----EAGMVFINGMVkSDPRL--PFGGVKRSGYGRE 412
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
21-334 |
1.58e-60 |
|
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: 202.07 E-value: 1.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 21 PWSRPAAFMSTSLISVAV------------TKIIA----KVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGS 83
Cdd:cd07124 175 PWNFPLAILAGMTTAALVtgntvvlkpaedTPVIAaklvEILEEAGLPpGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 84 tqvgKQVGLMVQERFG----------RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDE 153
Cdd:cd07124 255 ----REVGLRIYERAAkvqpgqkwlkRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 154 VVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMDRP--GNYVEPTIVTGLGHDASI 231
Cdd:cd07124 331 FLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSE-GRLLLGGEVLELAaeGYFVQPTIFADVPPDHRL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 232 AHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRI--FRwlgpKGSDCGIVNVNIPTSGAEIG-GAFGGEK 308
Cdd:cd07124 410 AQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLerAR----REFEVGNLYANRKITGALVGrQPFGGFK 485
|
330 340
....*....|....*....|....*..
gi 194380572 309 HTG-GGRESGSDAWKQYMRRSTCTINY 334
Cdd:cd07124 486 MSGtGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
52-325 |
6.58e-60 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 200.30 E-value: 6.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 52 PGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvgLMVQ--ERFGRSLLELGGNNAIIAFEDADLSLVVPSALFA 129
Cdd:PLN02278 217 PGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKK--LMAGaaATVKRVSLELGGNAPFIVFDDADLDVAVKGALAS 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 130 AVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKV 209
Cdd:PLN02278 295 KFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKR 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 210 MDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIV 289
Cdd:PLN02278 375 HSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRV--SEALEYGIV 452
|
250 260 270
....*....|....*....|....*....|....*....
gi 194380572 290 NVN---IPTSGAeiggAFGGEKHTGGGRESGSDAWKQYM 325
Cdd:PLN02278 453 GVNeglISTEVA----PFGGVKQSGLGREGSKYGIDEYL 487
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
25-329 |
3.13e-59 |
|
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: 196.98 E-value: 3.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 25 PAAFmsTSLISVAVTKIIAKVLEdnklPGAICSLTcGGADIGTAMAKDERVNLLSFTGSTQVGKQVglMVQ--ERFGRSL 102
Cdd:cd07106 149 PSPF--TPLCTLKLGELAQEVLP----PGVLNVVS-GGDELGPALTSHPDIRKISFTGSTATGKKV--MASaaKTLKRVT 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 103 LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHT 182
Cdd:cd07106 220 LELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQN 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 183 KQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQG 262
Cdd:cd07106 300 KMQYDKVKELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYG 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194380572 263 LSSSIFTKDLGRIFRwLGPKgSDCGIVNVNiptSGAEIGGA--FGGEKHTGGGRESGSDAWKQYMRRST 329
Cdd:cd07106 380 LGASVWSSDLERAEA-VARR-LEAGTVWIN---THGALDPDapFGGHKQSGIGVEFGIEGLKEYTQTQV 443
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
24-332 |
5.64e-59 |
|
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: 196.79 E-value: 5.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 24 RPAAFMSTSlisvavTKIIAKVLEDNKLPGAICS-LTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSL 102
Cdd:cd07118 153 KPSEFTSGT------TLMLAELLIEAGLPAGVVNiVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVS 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 103 LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHT 182
Cdd:cd07118 227 LELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIIN 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 183 KQAVSMFLGAVEEAKKEGGTVVYGGKVMD-RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQ 261
Cdd:cd07118 307 EAQLAKITDYVDAGRAEGATLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVY 386
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194380572 262 GLSSSIFTKDLGRIFrwLGPKGSDCGIVNVN-IPTSGAEIggAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 332
Cdd:cd07118 387 GLSAGVWSKDIDTAL--TVARRIRAGTVWVNtFLDGSPEL--PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
20-326 |
1.65e-58 |
|
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: 195.52 E-value: 1.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 20 GPWSRPaafMSTSLISVA---------VTK----------IIAKVLEDNKLPGAICSLTCGGADIGTAMAkDERVNLLSF 80
Cdd:cd07099 127 SPWNYP---LLTPMGDIIpalaagnavVLKpsevtplvgeLLAEAWAAAGPPQGVLQVVTGDGATGAALI-DAGVDKVAF 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 81 TGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKK 160
Cdd:cd07099 203 TGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 161 AYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPI 240
Cdd:cd07099 283 KARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPV 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 241 LYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL---GRIFRWLgpkgsDCGIVNVNIPTSGAEIGGA-FGGEKHTGGGRES 316
Cdd:cd07099 363 LPVMPVADEDEAIALANDSRYGLSASVFSRDLaraEAIARRL-----EAGAVSINDVLLTAGIPALpFGGVKDSGGGRRH 437
|
330
....*....|
gi 194380572 317 GSDAWKQYMR 326
Cdd:cd07099 438 GAEGLREFCR 447
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
42-333 |
1.70e-58 |
|
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: 195.87 E-value: 1.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 42 IAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvgLMVQERFGRSLLELGGNNAIIAFEDADLS 120
Cdd:cd07082 187 LAEAFHDAGFPkGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNR--LKKQHPMKRLVLELGGKDPAIVLPDADLE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 121 LVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEG 200
Cdd:cd07082 265 LAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKG 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 201 GTVVYGGKvmDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIF---R 277
Cdd:cd07082 345 ATVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARklaD 422
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 194380572 278 WLgpkgsDCGIVNVNIPTS-GAEIgGAFGGEKHTGGGRESGSDAWKQYMRRSTCTIN 333
Cdd:cd07082 423 AL-----EVGTVNINSKCQrGPDH-FPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
43-334 |
6.49e-58 |
|
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: 194.13 E-value: 6.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 43 AKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLV 122
Cdd:cd07107 163 AELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 123 VPSALFAA-VGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGG 201
Cdd:cd07107 243 ADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREGA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 202 TVVYGGKVMDRP----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR 277
Cdd:cd07107 323 RLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHR 402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 194380572 278 wlGPKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 334
Cdd:cd07107 403 --TARRVEAGYVWIN-GSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
24-316 |
8.49e-58 |
|
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: 194.21 E-value: 8.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 24 RPAAFMSTSLISVAvtKIIAKVLEDnklpGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLL 103
Cdd:cd07117 170 KPSSTTSLSLLELA--KIIQDVLPK----GVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 104 ELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTK 183
Cdd:cd07117 244 ELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 184 QAVSMFLGAVEEAKKEGGTVVYGGKVMDRP----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEV 259
Cdd:cd07117 324 DQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDS 403
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194380572 260 KQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRES 316
Cdd:cd07117 404 EYGLGGGVFTKDINRALRV--ARAVETGRVWVNtynqIPA-----GAPFGGYKKSGIGRET 457
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
21-325 |
3.60e-57 |
|
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: 191.79 E-value: 3.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 21 PWSRPAAFM--------------------STSLISVAVTKIIAKVLEdnkLP-GAICSLTCGGADIGTAMAKDERVNLLS 79
Cdd:cd07120 126 PWNSPVVLLvrslapalaagctvvvkpagQTAQINAAIIRILAEIPS---LPaGVVNLFTESGSEGAAHLVASPDVDVIS 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 80 FTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLK 159
Cdd:cd07120 203 FTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 160 KAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVY-GGKVMDR--PGNYVEPTIVTGLGHDASIAHTET 236
Cdd:cd07120 283 ARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLrGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEI 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 237 FAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNipTSGAEIGGA-FGGEKHTGGGRE 315
Cdd:cd07120 363 FGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRV--ARAIRAGTVWIN--DWNKLFAEAeEGGYRQSGLGRL 438
|
330
....*....|
gi 194380572 316 SGSDAWKQYM 325
Cdd:cd07120 439 HGVAALEDFI 448
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
42-332 |
5.38e-57 |
|
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: 191.29 E-value: 5.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 42 IAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLS 120
Cdd:cd07109 163 LAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 121 LVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPW-DPNVlyGPLHTKQAVSMFLGAVEEAKKE 199
Cdd:cd07109 243 AALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLeDPDL--GPLISAKQLDRVEGFVARARAR 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 200 GGTVVYGG-KVMDRP--GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIF 276
Cdd:cd07109 321 GARIVAGGrIAEGAPagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRAL 400
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 194380572 277 RWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 332
Cdd:cd07109 401 RV--ARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
41-315 |
6.72e-57 |
|
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: 191.30 E-value: 6.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLP-GAICSLTCGgADIGTAMAKDERVNLLSFTGStqvgKQVGLMVQERFGRS--LLELGGNNAIIAFEDA 117
Cdd:cd07147 168 ILGEVLAETGLPkGAFSVLPCS-RDDADLLVTDERIKLLSFTGS----PAVGWDLKARAGKKkvVLELGGNAAVIVDSDA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 118 DLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAK 197
Cdd:cd07147 243 DLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAV 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 198 KEGGTVVYGGKvmdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR 277
Cdd:cd07147 323 DAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALR 399
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 194380572 278 -WlgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKHTGGGRE 315
Cdd:cd07147 400 aW---DELEVGGVVINdVPTFRVD-HMPYGGVKDSGIGRE 435
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
31-325 |
1.94e-56 |
|
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: 190.60 E-value: 1.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 31 TSLISVAVTKIIAKVlednKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNN 109
Cdd:cd07119 173 TPLTTIALFELIEEA----GLPAGVVNLVTGsGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKN 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 110 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMF 189
Cdd:cd07119 249 PNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKV 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 190 LGAVEEAKKEGGTVVYGGKVMDRP----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSS 265
Cdd:cd07119 329 LSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAG 408
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194380572 266 SIFTKDLGRIFRWLgpKGSDCGIVNVN---IPTSGAEiggaFGGEKHTGGGRESGSDAWKQYM 325
Cdd:cd07119 409 AVWTKDIARANRVA--RRLRAGTVWINdyhPYFAEAP----WGGYKQSGIGRELGPTGLEEYQ 465
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
31-277 |
2.83e-56 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 190.12 E-value: 2.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 31 TSLISVAVTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNA 110
Cdd:PRK13473 177 TPLTALKLAELAADILP----PGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAP 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 111 IIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFL 190
Cdd:PRK13473 253 VIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 191 GAVEEAKKEG-GTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT 269
Cdd:PRK13473 333 GFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWT 412
|
....*...
gi 194380572 270 KDLGRIFR 277
Cdd:PRK13473 413 RDVGRAHR 420
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
41-326 |
2.91e-56 |
|
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: 189.82 E-value: 2.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLS 120
Cdd:cd07090 161 LLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 121 LVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEG 200
Cdd:cd07090 241 NAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEG 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 201 GTVVYGGKVMD-----RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRI 275
Cdd:cd07090 321 AKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRA 400
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 194380572 276 FRWLGP-KGSDCGIVNVNIptSGAEIggAFGGEKHTGGGRESGSDAWKQYMR 326
Cdd:cd07090 401 HRVIAQlQAGTCWINTYNI--SPVEV--PFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
2-315 |
5.54e-56 |
|
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: 189.48 E-value: 5.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 2 WRLPRALCvhAAKTSKLsgpwsRPAAFMSTSLISVAvtKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFT 81
Cdd:cd07559 155 WKLAPALA--AGNTVVL-----KPASQTPLSILVLM--ELIGDLLP----KGVVNVVTGFGSEAGKPLASHPRIAKLAFT 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 82 GSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSL--VVPSALFAAVGTA---GQRCTTARRLFIHESIHDEVVN 156
Cdd:cd07559 222 GSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAMDADddFDDKAEEGQLGFAfnqGEVCTCPSRALVQESIYDEFIE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 157 RLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRP----GNYVEPTIVTGLGHDASIA 232
Cdd:cd07559 302 RAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIF 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 233 HTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEK 308
Cdd:cd07559 382 QEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRV--ARGIQTGRVWVNcyhqYPA-----HAPFGGYK 454
|
....*..
gi 194380572 309 HTGGGRE 315
Cdd:cd07559 455 KSGIGRE 461
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
62-332 |
1.13e-55 |
|
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: 188.57 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 62 GADIGTAMAKDERVNLLSFTGSTQVGKQVglMV---QERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRC 138
Cdd:cd07091 208 GPTAGAAISSHMDVDKIAFTGSTAVGRTI--MEaaaKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCC 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 139 TTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVE 218
Cdd:cd07091 286 CAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQ 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 219 PTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR----------WLgpkgsDC-G 287
Cdd:cd07091 366 PTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRvsralkagtvWV-----NTyN 440
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 194380572 288 IVNVNIPtsgaeiggaFGGEKHTGGGRESGSDAWKQYMRRSTCTI 332
Cdd:cd07091 441 VFDAAVP---------FGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
52-325 |
2.20e-55 |
|
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: 187.42 E-value: 2.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 52 PGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvgLMvqERFGRS-----LLELGGNNAIIAFEDA-DLSLVVPS 125
Cdd:cd07112 181 AGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRR--FL--EYSGQSnlkrvWLECGGKSPNIVFADApDLDAAAEA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 126 ALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVY 205
Cdd:cd07112 257 AAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 206 GGKV--MDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRwlGPKG 283
Cdd:cd07112 337 GGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHR--VARR 414
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 194380572 284 SDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYM 325
Cdd:cd07112 415 LRAGTVWVNC-FDEGDITTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
41-317 |
5.75e-55 |
|
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: 186.63 E-value: 5.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLS 120
Cdd:cd07139 182 LLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLD 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 121 LVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEG 200
Cdd:cd07139 262 AAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEG 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 201 GTVVYGGKvmdRP-----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGR- 274
Cdd:cd07139 342 ARLVTGGG---RPagldrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERg 418
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 194380572 275 --IFRWLgpkgsDCGIVNVNIPTSgaEIGGAFGGEKHTGGGRESG 317
Cdd:cd07139 419 laVARRI-----RTGTVGVNGFRL--DFGAPFGGFKQSGIGREGG 456
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
1-334 |
8.87e-55 |
|
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: 186.11 E-value: 8.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 1 MWRLPRALCVHAAKTSKlsgpwsrPAAFMSTSLISVAVTKIIAKVlednklPGAICSLTCGGADIGTAMAKDERVNLLSF 80
Cdd:cd07113 160 VWKIGAALATGCTIVIK-------PSEFTPLTLLRVAELAKEAGI------PDGVLNVVNGKGAVGAQLISHPDVAKVSF 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 81 TGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKK 160
Cdd:cd07113 227 TGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 161 AYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPI 240
Cdd:cd07113 307 ALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPV 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 241 LYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgPKgSDCGIVNVNIPTSgAEIGGAFGGEKHTGGGRESGSDA 320
Cdd:cd07113 387 VSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYI-PR-IEAGTVWVNMHTF-LDPAVPFGGMKQSGIGREFGSAF 463
|
330
....*....|....
gi 194380572 321 WKQYMRRSTCTINY 334
Cdd:cd07113 464 IDDYTELKSVMIRY 477
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
52-334 |
7.17e-54 |
|
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: 184.24 E-value: 7.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 52 PGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVglM---VQERFGRSLLELGGNNAIIAFEDADLSLVVPSALF 128
Cdd:cd07140 204 KGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHI--MkscAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMS 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 129 AAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGK 208
Cdd:cd07140 282 SVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGK 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 209 VMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNE--EEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDC 286
Cdd:cd07140 362 QVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDTEYGLASGVFTKDINKALYV--SDKLEA 439
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 194380572 287 GIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 334
Cdd:cd07140 440 GTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIEY 486
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
41-326 |
1.22e-53 |
|
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: 183.08 E-value: 1.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQV-GLMVQERFGRSLLELGGNNAIIAFEDAD 118
Cdd:cd07142 186 LAAKLAAEAGLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIImQLAAKSNLKPVTLELGGKSPFIVCEDAD 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 119 LSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKK 198
Cdd:cd07142 266 VDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 199 EGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRW 278
Cdd:cd07142 346 EGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTL 425
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 194380572 279 LgpKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMR 326
Cdd:cd07142 426 S--RALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
21-315 |
2.90e-53 |
|
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: 181.79 E-value: 2.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 21 PWSRPAAFMSTSLIS--VAVTKIIAKVLED-------------NKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGST 84
Cdd:cd07108 126 PWNAPLMLAALKIAPalVAGNTVVLKAAEDaplavlllaeilaQVLPAGVLNVITGyGEECGAALVDHPDVDKVTFTGST 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 85 QVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGT-AGQRCTTARRLFIHESIHDEVVNRLKKAYA 163
Cdd:cd07108 206 EVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLS 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 164 QIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKE-GGTVVYGGK----VMDRPGNYVEPTIVTGLGHDASIAHTETFA 238
Cdd:cd07108 286 KLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLSTsGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFG 365
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194380572 239 PILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRwlGPKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRE 315
Cdd:cd07108 366 PVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALR--AAHALEAGWVQVN-QGGGQQPGQSYGGFKQSGLGRE 439
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
21-325 |
9.50e-53 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 180.87 E-value: 9.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 21 PWSRPAAFMSTSL---ISVAVTKII-------------AKVLEDNKLPGAICSLTCGGA-DIGTAMAKDERVNLLSFTGS 83
Cdd:PRK11241 155 PWNFPAAMITRKAgpaLAAGCTMVLkpasqtpfsalalAELAIRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGS 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 84 TQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYA 163
Cdd:PRK11241 235 TEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 164 QIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYV 243
Cdd:PRK11241 315 KLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 244 FKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIgGAFGGEKHTGGGRESGSDAWKQ 323
Cdd:PRK11241 395 FRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRV--GEALEYGIVGINTGIISNEV-APFGGIKASGLGREGSKYGIED 471
|
..
gi 194380572 324 YM 325
Cdd:PRK11241 472 YL 473
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
24-315 |
1.23e-52 |
|
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: 179.94 E-value: 1.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 24 RPAAfmSTSLISVAVTKIIakvLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvgLMVQERFGRSLL 103
Cdd:cd07094 157 KPAS--KTPLSALELAKIL---VEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEA--LRANAGGKRIAL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 104 ELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTK 183
Cdd:cd07094 230 ELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 184 QAVSMFLGAVEEAKKEGGTVVYGGKvmdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGL 263
Cdd:cd07094 310 EAAERVERWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGL 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 194380572 264 SSSIFTKDLGRIFRwlGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRE 315
Cdd:cd07094 387 QAGIFTRDLNVAFK--AAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGRE 436
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
2-317 |
1.92e-52 |
|
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: 179.47 E-value: 1.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 2 WRLPRAL---CVHAAKTSKLsgpwsrpaafmsTSLISVAVTKIIAKVlednKLP-GAICSLTCGGADIGTAMAKDERVNL 77
Cdd:cd07110 139 WKVAPALaagCTVVLKPSEL------------TSLTELELAEIAAEA----GLPpGVLNVVTGTGDEAGAPLAAHPGIDK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 78 LSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNR 157
Cdd:cd07110 203 ISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLER 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 158 LKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMD--RPGNYVEPTIVTGLGHDASIAHTE 235
Cdd:cd07110 283 LATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 236 TFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSgAEIGGAFGGEKHTGGGRE 315
Cdd:cd07110 363 IFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRV--AEALEAGIVWINCSQP-CFPQAPWGGYKRSGIGRE 439
|
..
gi 194380572 316 SG 317
Cdd:cd07110 440 LG 441
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
41-325 |
4.00e-52 |
|
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: 178.26 E-value: 4.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGlmvqERFGRSL----LELGGNNAIIAFED 116
Cdd:cd07152 156 VIARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVG----EAAGRHLkkvsLELGGKNALIVLDD 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 117 ADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEA 196
Cdd:cd07152 232 ADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDS 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 197 KKEGGTVVYGGKvmdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIF 276
Cdd:cd07152 312 VAAGARLEAGGT---YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAM 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 194380572 277 RwLGPKgSDCGIVNVNIPTSGAEIGGAFGGEKHTG-GGRESGSDAWKQYM 325
Cdd:cd07152 389 A-LADR-LRTGMLHINDQTVNDEPHNPFGGMGASGnGSRFGGPANWEEFT 436
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
52-332 |
2.49e-51 |
|
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: 177.15 E-value: 2.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 52 PGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKqvglMVQERFGRS-----LLELGGNNAIIAFEDADLSLVVPSA 126
Cdd:cd07141 202 PGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGK----LIQQAAGKSnlkrvTLELGGKSPNIVFADADLDYAVEQA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 127 LFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYG 206
Cdd:cd07141 278 HEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECG 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 207 GKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDC 286
Cdd:cd07141 358 GKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITF--SNALRA 435
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 194380572 287 GIVNVNIPTSGAeIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 332
Cdd:cd07141 436 GTVWVNCYNVVS-PQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
61-326 |
3.29e-50 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 174.30 E-value: 3.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 61 GGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTT 140
Cdd:PRK13252 207 GDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTN 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 141 ARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDR----PGNY 216
Cdd:PRK13252 287 GTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAF 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 217 VEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGpkGSDCGIVNVNipTS 296
Cdd:PRK13252 367 VAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIH--QLEAGICWIN--TW 442
|
250 260 270
....*....|....*....|....*....|...
gi 194380572 297 G---AEIggAFGGEKHTGGGRESGSDAWKQYMR 326
Cdd:PRK13252 443 GespAEM--PVGGYKQSGIGRENGIATLEHYTQ 473
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
41-325 |
1.48e-49 |
|
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: 171.72 E-value: 1.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLPGAICSLTCG-GADIGTAMAkdERVNLLSFTGSTQVGKQVGlmvqERFGRSL----LELGGNNAIIAFE 115
Cdd:cd07101 163 WAVELLIEAGLPRDLWQVVTGpGSEVGGAIV--DNADYVMFTGSTATGRVVA----ERAGRRLigcsLELGGKNPMIVLE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 116 DADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEE 195
Cdd:cd07101 237 DADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDD 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 196 AKKEGGTVVYGGKVmdRP--GNYV-EPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL 272
Cdd:cd07101 317 AVAKGATVLAGGRA--RPdlGPYFyEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDG 394
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 194380572 273 GRIfRWLGPKgSDCGIVNVN--IPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYM 325
Cdd:cd07101 395 ARG-RRIAAR-LRAGTVNVNegYAAAWASIDAPMGGMKDSGLGRRHGAEGLLKYT 447
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
41-277 |
2.15e-49 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 170.30 E-value: 2.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADL 119
Cdd:PRK10090 116 AFAKIVDEIGLPKGVFNLVLGrGETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 120 SLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWD-PNVLYGPLHTKQAVSMFLGAVEEAKK 198
Cdd:PRK10090 196 DLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVE 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194380572 199 EGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR 277
Cdd:PRK10090 276 EGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMK 354
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
52-325 |
2.35e-49 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 172.61 E-value: 2.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 52 PGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAV 131
Cdd:PLN02467 208 PGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCF 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 132 GTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKvmd 211
Cdd:PLN02467 288 WTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGK--- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 212 RP-----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDC 286
Cdd:PLN02467 365 RPehlkkGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERV--SEAFQA 442
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 194380572 287 GIVNVN--------IPtsgaeiggaFGGEKHTGGGRESGSDAWKQYM 325
Cdd:PLN02467 443 GIVWINcsqpcfcqAP---------WGGIKRSGFGRELGEWGLENYL 480
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
42-332 |
7.52e-49 |
|
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: 169.29 E-value: 7.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 42 IAKVLEDNKLP-GAICSLTCGGAD---IGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDA 117
Cdd:cd07105 144 IGRVFHEAGLPkGVLNVVTHSPEDapeVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 118 DLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIrvgnPWDPNVLyGPLHTKQAVSMFLGAVEEAK 197
Cdd:cd07105 224 DLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKL----FAGPVVL-GSLVSAAAADRVKELVDDAL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 198 KEGGTVVYGGKVMDRP-GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIF 276
Cdd:cd07105 299 SKGAKLVVGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARAL 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 194380572 277 RwLGpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 332
Cdd:cd07105 379 A-VA-KRIESGAVHINGMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
41-317 |
6.65e-48 |
|
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: 167.68 E-value: 6.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADL 119
Cdd:cd07138 175 ILAEILDEAGLPAGVFNLVNGdGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 120 SLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKE 199
Cdd:cd07138 255 EKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 200 GGTVVYGGkvMDRP-----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGR 274
Cdd:cd07138 335 GARLVAGG--PGRPeglerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPER 412
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 194380572 275 ---IFRWLgpkgsDCGIVNVNipTSGAEIGGAFGGEKHTGGGRESG 317
Cdd:cd07138 413 araVARRL-----RAGQVHIN--GAAFNPGAPFGGYKQSGNGREWG 451
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
46-319 |
6.93e-47 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 166.21 E-value: 6.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 46 LEDNKLPGAICSLTCG-GADIGTAMAkdERVNLLSFTGSTQVGKQVGlmvqERFGRSL----LELGGNNAIIAFEDADLS 120
Cdd:PRK09407 204 LYEAGLPRDLWQVVTGpGPVVGTALV--DNADYLMFTGSTATGRVLA----EQAGRRLigfsLELGGKNPMIVLDDADLD 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 121 LVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQ---AVSMFlgaVEEAK 197
Cdd:PRK09407 278 KAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAqleTVSAH---VDDAV 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 198 KEGGTVVYGGKVmdRP--GNYV-EPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGR 274
Cdd:PRK09407 355 AKGATVLAGGKA--RPdlGPLFyEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTAR 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 194380572 275 ---IFRWLgpkgsDCGIVNVN---IPTSGAeIGGAFGGEKHTGGGRESGSD 319
Cdd:PRK09407 433 graIAARI-----RAGTVNVNegyAAAWGS-VDAPMGGMKDSGLGRRHGAE 477
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
53-326 |
1.08e-45 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 162.68 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 53 GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKqvglMVQERFGRS-----LLELGGNNAIIAFEDADLSLVVPSAL 127
Cdd:PLN02766 216 GVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGR----KIMQAAATSnlkqvSLELGGKSPLLIFDDADVDMAVDLAL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 128 FAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGG 207
Cdd:PLN02766 292 LGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGG 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 208 KVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL---GRIFRWLgpkgs 284
Cdd:PLN02766 372 KPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLdvaNTVSRSI----- 446
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 194380572 285 DCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMR 326
Cdd:PLN02766 447 RAGTIWVNC-YFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
24-333 |
2.35e-45 |
|
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: 161.16 E-value: 2.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 24 RPAAFmsTSLISVAVTKIIAkvlEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKqvglMVQERFGRS-- 101
Cdd:cd07143 178 KPSEL--TPLSALYMTKLIP---EAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGR----KVMEAAAKSnl 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 102 ---LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYG 178
Cdd:cd07143 249 kkvTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQG 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 179 PLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNE 258
Cdd:cd07143 329 PQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRAND 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194380572 259 VKQGLSSSIFTKDLGRIFRWLGP-KGSDCGIVNVNIPTSGAeiggAFGGEKHTGGGRESGSDAWKQYMRRSTCTIN 333
Cdd:cd07143 409 STYGLAAAVFTNNINNAIRVANAlKAGTVWVNCYNLLHHQV----PFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
37-320 |
3.37e-45 |
|
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: 159.74 E-value: 3.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 37 AVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSL-LELGGNNAIIAFE 115
Cdd:cd07095 138 AVAELMVELWEEAGLPPGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWD 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 116 DADLSLVVPSALFAAVGTAGQRCTTARRLFIHES-IHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVE 194
Cdd:cd07095 218 VADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 195 EAKKEGGTVVYGGKVMDRPGNYVEPTI--VTGLghdASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDl 272
Cdd:cd07095 298 DLLALGGEPLLAMERLVAGTAFLSPGIidVTDA---ADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDD- 373
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 194380572 273 GRIFRWLGPKgSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDA 320
Cdd:cd07095 374 EALFERFLAR-IRAGIVNWNRPTTGASSTAPFGGVGLSGNHRPSAYYA 420
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
52-333 |
3.67e-45 |
|
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: 161.04 E-value: 3.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 52 PGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAV 131
Cdd:cd07144 201 PGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIM 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 132 GTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQI-RVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGG--- 207
Cdd:cd07144 281 YNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGeka 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 208 KVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCG 287
Cdd:cd07144 361 PEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVA--RELEAG 438
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 194380572 288 IVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTIN 333
Cdd:cd07144 439 MVWIN-SSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHIN 483
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
41-317 |
6.76e-44 |
|
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: 157.08 E-value: 6.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLS 120
Cdd:cd07098 169 IIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 121 LVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEG 200
Cdd:cd07098 249 QIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKG 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 201 GTVVYGGKVMDRP----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIF 276
Cdd:cd07098 329 ARLLAGGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRAR 408
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 194380572 277 RWLgpKGSDCGIVNVNiptsgaEIGGA-------FGGEKHTGGGRESG 317
Cdd:cd07098 409 RIA--SQLETGMVAIN------DFGVNyyvqqlpFGGVKGSGFGRFAG 448
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
21-277 |
1.06e-39 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 146.62 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 21 PWSRPAAFMS-TSLISVAV-----------TKIIA----KVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGS 83
Cdd:PRK03137 180 PWNFPFAIMAgMTLAAIVAgntvllkpasdTPVIAakfvEVLEEAGLPaGVVNFVPGSGSEVGDYLVDHPKTRFITFTGS 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 84 tqvgKQVGLMVQER----------FGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDE 153
Cdd:PRK03137 260 ----REVGLRIYERaakvqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 154 VVNRLKKAYAQIRVGNPWDPNVLyGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAH 233
Cdd:PRK03137 336 VLEKVVELTKELTVGNPEDNAYM-GPVINQASFDKIMSYIEIGKEE-GRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQ 413
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 194380572 234 TETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR 277
Cdd:PRK03137 414 EEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEK 457
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
43-326 |
1.09e-39 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 146.88 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 43 AKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQV-GLMVQERFGRSLLELGGNNAIIAFEDADLS 120
Cdd:PLN02466 242 AKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVlELAAKSNLKPVTLELGGKSPFIVCEDADVD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 121 LVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEG 200
Cdd:PLN02466 322 KAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 201 GTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL---GRIFR 277
Cdd:PLN02466 402 ATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLdtaNTLSR 481
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 194380572 278 WLgpkgsDCGIVNVN--------IPtsgaeiggaFGGEKHTGGGRESGSDAWKQYMR 326
Cdd:PLN02466 482 AL-----RVGTVWVNcfdvfdaaIP---------FGGYKMSGIGREKGIYSLNNYLQ 524
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
1-328 |
2.83e-39 |
|
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: 144.85 E-value: 2.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 1 MWRLPRALCVHAAKTSKLSgPWSRPAAFMstslisvavtkiIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSF 80
Cdd:cd07111 165 AWKICPALAMGNTVVLKPA-EYTPLTALL------------FAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAF 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 81 TGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKK 160
Cdd:cd07111 232 TGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 161 AYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPI 240
Cdd:cd07111 312 RMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPV 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 241 LYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRwLGPkGSDCGIVNVNI-----PTSGaeiggaFGGEKHTGGGRE 315
Cdd:cd07111 392 LVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALE-VAL-SLKAGVVWINGhnlfdAAAG------FGGYRESGFGRE 463
|
330
....*....|...
gi 194380572 316 SGSDAWKQYMRRS 328
Cdd:cd07111 464 GGKEGLYEYLRPS 476
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
62-315 |
1.28e-38 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 142.57 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 62 GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTA 141
Cdd:PRK09406 189 GSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 142 RRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTI 221
Cdd:PRK09406 269 KRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTV 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 222 VTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN-IPTSGAEI 300
Cdd:PRK09406 349 ITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFI--DDLEAGQVFINgMTVSYPEL 426
|
250
....*....|....*
gi 194380572 301 GgaFGGEKHTGGGRE 315
Cdd:PRK09406 427 P--FGGVKRSGYGRE 439
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
42-274 |
2.20e-38 |
|
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: 142.00 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 42 IAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSL 121
Cdd:cd07102 162 FAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 122 VVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGG 201
Cdd:cd07102 242 AAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGA 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194380572 202 TVVYGGK---VMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGR 274
Cdd:cd07102 322 RALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIAR 397
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
25-317 |
1.06e-36 |
|
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: 138.48 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 25 PAafMSTSLISVAVTKIiakvLEDNKLPGAICSLT-CGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLL 103
Cdd:cd07125 202 PA--EQTPLIAARAVEL----LHEAGVPRDVLQLVpGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPILP 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 104 ---ELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPL 180
Cdd:cd07125 276 liaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 181 HTKQAVSMFLGAVEEAKKEgGTVVYGGKVMDRPGNYVEPTIVTGlghDASIAH-TETFAPILYVFKFKNE--EEVFAWNN 257
Cdd:cd07125 356 IDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEI---VGIFDLtTEVFGPILHVIRFKAEdlDEAIEDIN 431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194380572 258 EVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAeIGGA--FGGEKHTGGGRESG 317
Cdd:cd07125 432 ATGYGLTLGIHSRDEREIEYWR--ERVEAGNLYINRNITGA-IVGRqpFGGWGLSGTGPKAG 490
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
21-327 |
1.97e-36 |
|
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: 137.33 E-value: 1.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 21 PWSRPAAfMSTSLISVAV---TKIIAKVLEDNKL---------------PGAICSLTCGGADIGTAMAKDERVNLLSFTG 82
Cdd:cd07083 163 PWNFPVA-IFTGMIVAPVavgNTVIAKPAEDAVVvgykvfeifheagfpPGVVQFLPGVGEEVGAYLTEHERIRGINFTG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 83 STQVGKQVGLMVQER------FGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVN 156
Cdd:cd07083 242 SLETGKKIYEAAARLapgqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 157 RLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTET 236
Cdd:cd07083 322 RLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNE-GQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 237 FAPILYVFKFKNEE--EVFAWNNEVKQGLSSSIFTKDLGRIfRWLGPKgSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGG 313
Cdd:cd07083 401 FGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHL-EEARRE-FHVGNLYINRKITGALVGvQPFGGFKLSGTN 478
|
330
....*....|....
gi 194380572 314 RESGSdawKQYMRR 327
Cdd:cd07083 479 AKTGG---PHYLRR 489
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
52-316 |
1.99e-33 |
|
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: 128.72 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 52 PGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFED---ADLSLVVPS--- 125
Cdd:cd07116 192 PGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFADvmdADDAFFDKAleg 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 126 -ALFAAvgTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVV 204
Cdd:cd07116 272 fVMFAL--NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 205 YGGKVMDRPGN----YVEPTIVTGlGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlg 280
Cdd:cd07116 350 TGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRM-- 426
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 194380572 281 PKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRES 316
Cdd:cd07116 427 GRGIQAGRVWTNcyhlYPA-----HAAFGGYKQSGIGREN 461
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
41-294 |
3.28e-33 |
|
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: 128.40 E-value: 3.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVglmvQER---FGRSLLELGG-NNAIIAFED 116
Cdd:cd07085 181 RLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYI----YERaaaNGKRVQALGGaKNHAVVMPD 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 117 ADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEA 196
Cdd:cd07085 257 ADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 197 KKEGGTVVYGG---KVMDRP-GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD- 271
Cdd:cd07085 337 VEEGAKLVLDGrgvKVPGYEnGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSg 416
|
250 260
....*....|....*....|....
gi 194380572 272 -LGRIFRwlgpKGSDCGIVNVNIP 294
Cdd:cd07085 417 aAARKFQ----REVDAGMVGINVP 436
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
24-313 |
1.05e-32 |
|
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: 126.38 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 24 RPAAfmSTSLISVAVTKIiakvLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGkqvgLMVQERFG---R 100
Cdd:cd07148 158 KPAL--ATPLSCLAFVDL----LHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVG----WMLRSKLApgtR 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 101 SLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPL 180
Cdd:cd07148 228 CALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 181 HTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRpgNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 260
Cdd:cd07148 308 IRPREVDRVEEWVNEAVAAGARLLCGGKRLSD--TTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLP 385
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 194380572 261 QGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGG 313
Cdd:cd07148 386 VAFQAAVFTKDLDVALKAV--RRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
42-332 |
2.46e-32 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 126.16 E-value: 2.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 42 IAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQvgLMV---QERFGRSLLELGGNNAIIAFEDA 117
Cdd:PRK09847 203 LAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQ--LLKdagDSNMKRVWLEAGGKSANIVFADC 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 118 -DLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEA 196
Cdd:PRK09847 281 pDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREG 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 197 KKEGgTVVYGGKVMDRPGnYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIF 276
Cdd:PRK09847 361 ESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAH 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 194380572 277 RWlgPKGSDCGIVNVNIPTSGaEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 332
Cdd:PRK09847 439 RM--SRRLKAGSVFVNNYNDG-DMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
40-315 |
2.48e-32 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 125.74 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 40 KIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADL 119
Cdd:PRK13968 170 QLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 120 SLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKE 199
Cdd:PRK13968 250 ELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 200 GGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWl 279
Cdd:PRK13968 330 GARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQM- 408
|
250 260 270
....*....|....*....|....*....|....*..
gi 194380572 280 gPKGSDCGIVNVN-IPTSGAEIggAFGGEKHTGGGRE 315
Cdd:PRK13968 409 -AARLECGGVFINgYCASDARV--AFGGVKKSGFGRE 442
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
20-313 |
2.12e-28 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 115.13 E-value: 2.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 20 GPWSRPA----------------AFMSTSLISVAVTKIIAKVLeDNKLPGAICSLTCGGADIGTAMAKdERVNLLSFTGS 83
Cdd:PTZ00381 117 GAWNYPLnltliplagaiaagntVVLKPSELSPHTSKLMAKLL-TKYLDPSYVRVIEGGVEVTTELLK-EPFDHIFFTGS 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 84 TQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYA 163
Cdd:PTZ00381 195 PRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 164 QIRVGNPW---DPNVLYGPLHTKQAVSMFlgaveeaKKEGGTVVYGGKVmDRPGNYVEPTIVTGLGHDASIAHTETFAPI 240
Cdd:PTZ00381 275 EFFGEDPKkseDYSRIVNEFHTKRLAELI-------KDHGGKVVYGGEV-DIENKYVAPTIIVNPDLDSPLMQEEIFGPI 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 241 LYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDlGRIFRWLGPKGSDCGIV---------NVNIPtsgaeiggaFGGEKHTG 311
Cdd:PTZ00381 347 LPILTYENIDEVLEFINSRPKPLALYYFGED-KRHKELVLENTSSGAVVindcvfhllNPNLP---------FGGVGNSG 416
|
..
gi 194380572 312 GG 313
Cdd:PTZ00381 417 MG 418
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
37-316 |
2.73e-28 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 114.67 E-value: 2.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 37 AVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSL-LELGGNNAIIAFE 115
Cdd:PRK09457 175 WVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKILaLEMGGNNPLVIDE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 116 DADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIH-DEVVNRLKKAYAQIRVGNPW-DPNVLYGPLHTKQAVSMFLGAV 193
Cdd:PRK09457 255 VADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDaEPQPFMGAVISEQAAQGLVAAQ 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 194 EEAKKEGGTVVYGGKVMDRPGNYVEPTI--VTGLghdASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 271
Cdd:PRK09457 335 AQLLALGGKSLLEMTQLQAGTGLLTPGIidVTGV---AELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDD 411
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 194380572 272 LGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES 316
Cdd:PRK09457 412 REDYDQFL--LEIRAGIVNWNKPLTGASSAAPFGGVGASGNHRPS 454
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
52-274 |
9.03e-28 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 113.31 E-value: 9.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 52 PGAICSLTCGGADIGTAMAKDERVNLLSFTGStqvgkQVGLMVQERFGRSLL--ELGGNNAIIAFEDADLSLVVPSALFA 129
Cdd:PLN00412 215 KGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-----DTGIAISKKAGMVPLqmELGGKDACIVLEDADLDLAAANIIKG 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 130 AVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDpNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKv 209
Cdd:PLN00412 290 GFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWK- 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194380572 210 mdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGR 274
Cdd:PLN00412 368 --REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINK 430
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
41-271 |
8.77e-27 |
|
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: 110.75 E-value: 8.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQER------FGRSLLELGGNNAIIA 113
Cdd:cd07123 214 LVYKILEEAGLPpGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENldryrtYPRIVGETGGKNFHLV 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 114 FEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAV 193
Cdd:cd07123 294 HPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYI 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 194 EEAKKEGG-TVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPIL--YVFKFKNEEEVFAWNNEV-KQGLSSSIFT 269
Cdd:cd07123 374 DHAKSDPEaEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLtvYVYPDSDFEETLELVDTTsPYALTGAIFA 453
|
..
gi 194380572 270 KD 271
Cdd:cd07123 454 QD 455
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
21-328 |
1.58e-26 |
|
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: 109.61 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 21 PWSRPAAFMSTSLIS--VAVTKIIAKVLEDNKL---------------PGAICSLTCGGADIGTAMAKDERVNLLSFTGS 83
Cdd:TIGR01238 169 PWNFPLAIFTGQISAalAAGNTVIAKPAEQTSLiayravelmqeagfpAGTIQLLPGRGADVGAALTSDPRIAGVAFTGS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 84 TQVGKQVGLMVQERF---GRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKK 160
Cdd:TIGR01238 249 TEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQG 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 161 AYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTV---VYGGKVMDRPGNYVEPTIVTGLGHDAsiAHTETF 237
Cdd:TIGR01238 329 AMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIaqlTLDDSRACQHGTFVAPTLFELDDIAE--LSEEVF 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 238 APILYVFKFKNEE--EVFAWNNEVKQGLSSSIFTKDLGRIfRWLgPKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGR 314
Cdd:TIGR01238 407 GPVLHVVRYKAREldQIVDQINQTGYGLTMGVHSRIETTY-RWI-EKHARVGNCYVNRNQVGAVVGvQPFGGQGLSGTGP 484
|
330
....*....|....
gi 194380572 315 ESGSDAWKQYMRRS 328
Cdd:TIGR01238 485 KAGGPHYLYRLTQV 498
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
35-271 |
2.41e-25 |
|
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: 105.66 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 35 SVAVTKIIAKVLEDNKLPGAICSLTcGGADIGTAMAkDERVNLLSFTGSTQVGKqvglMVQERFGRSL----LELGGNNA 110
Cdd:cd07136 139 TPNTSKVIAKIIEETFDEEYVAVVE-GGVEENQELL-DQKFDYIFFTGSVRVGK----IVMEAAAKHLtpvtLELGGKSP 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 111 IIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKayaQIRVGNPWDP--NVLYGPL----HTKQ 184
Cdd:cd07136 213 CIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELKE---EIKKFYGEDPleSPDYGRIinekHFDR 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 185 AVSMFlgaveeakkEGGTVVYGGKVmDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLS 264
Cdd:cd07136 290 LAGLL---------DNGKIVFGGNT-DRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLA 359
|
....*..
gi 194380572 265 SSIFTKD 271
Cdd:cd07136 360 LYLFSED 366
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
37-271 |
8.97e-25 |
|
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: 104.15 E-value: 8.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 37 AVTKIIAKVLEDnKLPGAICSLTCGGADIGTAMAKdERVNLLSFTGSTQVGKQVglMvqERFGRSL----LELGGNNAII 112
Cdd:cd07087 141 ATSALLAKLIPK-YFDPEAVAVVEGGVEVATALLA-EPFDHIFFTGSPAVGKIV--M--EAAAKHLtpvtLELGGKSPCI 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 113 AFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWD-PNvlYGPL----HTKQAVS 187
Cdd:cd07087 215 VDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKEsPD--YGRIinerHFDRLAS 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 188 MFlgaveeakkEGGTVVYGGKVmDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSI 267
Cdd:cd07087 293 LL---------DDGKVVIGGQV-DKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYL 362
|
....
gi 194380572 268 FTKD 271
Cdd:cd07087 363 FSED 366
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
51-250 |
2.80e-24 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 104.25 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 51 LPGAicsltcgGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLL---ELGGNNAIIAfedaDLS-L---VV 123
Cdd:COG4230 743 LPGD-------GETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVPliaETGGQNAMIV----DSSaLpeqVV 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 124 PSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEgGTV 203
Cdd:COG4230 812 DDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAE-GRL 890
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 194380572 204 VYGGKVMDRP--GNYVEPTIVTgLGHDASIAHtETFAPILYVFKFKNEE 250
Cdd:COG4230 891 VHQLPLPEECanGTFVAPTLIE-IDSISDLER-EVFGPVLHVVRYKADE 937
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
32-271 |
3.14e-24 |
|
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: 102.68 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 32 SLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMakDERVNLLSFTGSTQVGKqvglMVQERFGRSL----LELGG 107
Cdd:cd07135 144 SELTPHTAALLAELVPKYLDPDAFQVVQGGVPETTALL--EQKFDKIFYTGSGRVGR----IIAEAAAKHLtpvtLELGG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 108 NNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQiRVGNPWDPNVLYGPLHTKQAVS 187
Cdd:cd07135 218 KSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDE-FYPGGANASPDYTRIVNPRHFN 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 188 MFLGAVEEAKkegGTVVYGGKvMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSI 267
Cdd:cd07135 297 RLKSLLDTTK---GKVVIGGE-MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYI 372
|
....
gi 194380572 268 FTKD 271
Cdd:cd07135 373 FTDD 376
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
31-317 |
2.61e-23 |
|
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: 99.99 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 31 TSLISVAVTKIIAKVLEDNKLpgAICSltcGGADIGTAmakdervnLLS-------FTGSTQVGKqvglMVQERFGRSL- 102
Cdd:cd07134 139 TPHTSAVIAKIIREAFDEDEV--AVFE---GDAEVAQA--------LLElpfdhifFTGSPAVGK----IVMAAAAKHLa 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 103 ---LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIrvgnpwdpnvlYGP 179
Cdd:cd07134 202 svtLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKF-----------YGK 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 180 LHTKQAVSMF------------LGAVEEAKKEGGTVVYGGKVmDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFK 247
Cdd:cd07134 271 DAARKASPDLarivndrhfdrlKGLLDDAVAKGAKVEFGGQF-DAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYE 349
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194380572 248 NEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGS-DCGI-------VNVNIPtsgaeiggaFGGEKHTGGGRESG 317
Cdd:cd07134 350 DLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSgGVVVndvvlhfLNPNLP---------FGGVNNSGIGSYHG 418
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
31-327 |
9.46e-23 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 99.55 E-value: 9.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 31 TSLI-SVAVtkiiaKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLL---EL 105
Cdd:PRK11905 715 TPLIaARAV-----RLLHEAGVPKDALQLLPGdGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaET 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 106 GGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQA 185
Cdd:PRK11905 790 GGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEA 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 186 VSMFLGAVEEAKKEGGTVvyggKVMDRP-----GNYVEPTIVTgLGHDASIAHtETFAPILYVFKFKNEE--EVFAWNNE 258
Cdd:PRK11905 870 QANIEAHIEAMRAAGRLV----HQLPLPaetekGTFVAPTLIE-IDSISDLER-EVFGPVLHVVRFKADEldRVIDDINA 943
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 259 VKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSdawKQYMRR 327
Cdd:PRK11905 944 TGYGLTFGLHSRIDETIAHVT--SRIRAGNIYVNRNIIGAVVGvQPFGGEGLSGTGPKAGG---PLYLGR 1008
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
31-250 |
1.94e-22 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 98.73 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 31 TSLISVAVTKIiakvLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSL---LELG 106
Cdd:PRK11904 723 TPLIAAEAVKL----LHEAGIPKDVLQLLPGdGATVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVpliAETG 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 107 GNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAV 186
Cdd:PRK11904 799 GQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAK 878
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194380572 187 SMFLGAVEEAKKEgGTVVYGGKVMD--RPGNYVEPTIVTgLGhDASIAHTETFAPILYVFKFKNEE 250
Cdd:PRK11904 879 ANLDAHIERMKRE-ARLLAQLPLPAgtENGHFVAPTAFE-ID-SISQLEREVFGPILHVIRYKASD 941
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
41-339 |
1.14e-19 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 90.19 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 41 IIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLS 120
Cdd:PLN02419 294 ILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANID 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 121 LVVPSALFAAVGTAGQRCTT-ARRLFIHE--SIHDEVVNRLKKayaqIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAK 197
Cdd:PLN02419 374 ATLNALLAAGFGAAGQRCMAlSTVVFVGDakSWEDKLVERAKA----LKVTCGSEPDADLGPVISKQAKERICRLIQSGV 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 198 KEGGTVVYGGKVMDRP----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD-- 271
Cdd:PLN02419 450 DDGAKLLLDGRDIVVPgyekGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSga 529
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194380572 272 LGRIFRwlgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGR-----ESGSDAWKQYmrrSTCTINYsKDLP 339
Cdd:PLN02419 530 AARKFQ----MDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDlnfygKAGVDFFTQI---KLVTQKQ-KDIH 594
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
31-250 |
3.88e-18 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 85.80 E-value: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 31 TSLISVAVTKIIakvLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERF---GRS---LLE 104
Cdd:PRK11809 807 TPLIAAQAVRIL---LEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqGRPiplIAE 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 105 LGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQ 184
Cdd:PRK11809 884 TGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAE 963
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194380572 185 AVSMFLGAVEEAKKEGGTV---VYGGKVMDRPGNYVEPTIVTgLGHDASIAHtETFAPILYVFKFKNEE 250
Cdd:PRK11809 964 AKANIERHIQAMRAKGRPVfqaARENSEDWQSGTFVPPTLIE-LDSFDELKR-EVFGPVLHVVRYNRNQ 1030
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
24-328 |
1.33e-16 |
|
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: 80.78 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 24 RPAAfmSTSLISVAVTKIIakvLEDNKLP-GAIcSLTCGGAdiGTAMAKDERVNLLSFTGSTQVGKQVGLM--VQERFGR 100
Cdd:cd07128 178 KPAT--ATAYLTEAVVKDI---VESGLLPeGAL-QLICGSV--GDLLDHLGEQDVVAFTGSAATAAKLRAHpnIVARSIR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 101 SLLELGGNNAIIAFEDA-----DLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNV 175
Cdd:cd07128 250 FNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 176 LYGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMDRP-------GNYVEPTIVTGLG-HDASIAH-TETFAPILYVFKF 246
Cdd:cd07128 330 RMGPLVSREQREDVRAAVATLLAE-AEVVFGGPDRFEVvgadaekGAFFPPTLLLCDDpDAATAVHdVEAFGPVATLMPY 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 247 KNEEEVFAWNNEVKQGLSSSIFTKD---LGRIFRWLGPKGsdcGIVNVNIPTSGAEIGG--------AFGGEKHTGGGRE 315
Cdd:cd07128 409 DSLAEAIELAARGRGSLVASVVTNDpafARELVLGAAPYH---GRLLVLNRDSAKESTGhgsplpqlVHGGPGRAGGGEE 485
|
330
....*....|....
gi 194380572 316 -SGSDAWKQYMRRS 328
Cdd:cd07128 486 lGGLRGVKHYMQRT 499
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
20-271 |
7.75e-16 |
|
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: 78.03 E-value: 7.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 20 GPWSRP----------------AAFMSTSLISVAVTKIIAKVLE---DNKLPGAICsltcGGADIGTAMAKdERVNLLSF 80
Cdd:cd07132 108 GAWNYPlqltlvplvgaiaagnCVVIKPSEVSPATAKLLAELIPkylDKECYPVVL----GGVEETTELLK-QRFDYIFY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 81 TGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKK 160
Cdd:cd07132 183 TGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 161 AYAQIRVGNPWD-PNvlYGPL----HTKQAVSMFlgaveeakkEGGTVVYGGKVmDRPGNYVEPTIVTGLGHDASIAHTE 235
Cdd:cd07132 263 TLKEFYGEDPKEsPD--YGRIindrHFQRLKKLL---------SGGKVAIGGQT-DEKERYIAPTVLTDVKPSDPVMQEE 330
|
250 260 270
....*....|....*....|....*....|....*.
gi 194380572 236 TFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 271
Cdd:cd07132 331 IFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN 366
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
38-328 |
9.02e-16 |
|
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: 78.05 E-value: 9.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 38 VTKIIAKVLED-NKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvgLMVQERFGRSLLELGGNNAIIAFED 116
Cdd:cd07084 142 VMQIMVRLLHYaGLLPPEDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEK--LALDAKQARIYLELAGFNWKVLGPD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 117 AD-LSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDE-VVNRLKKAYAQIRVGnpwdpNVLYGPLHTKQAVSMflgaVE 194
Cdd:cd07084 220 AQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLE-----DLLLGPVQTFTTLAM----IA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 195 EAKKEGGTVV-YGGKVM---DRPGNY----VEPTIVTGLGHDAS-IAHT-ETFAPILYVFKFKNEEEVFAWN-NEVKQG- 262
Cdd:cd07084 291 HMENLLGSVLlFSGKELknhSIPSIYgacvASALFVPIDEILKTyELVTeEIFGPFAIVVEYKKDQLALVLElLERMHGs 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194380572 263 LSSSIFTKD---LGRifrwLGPKGSDCGIVNVNIPTSgaeiGGAFGGEKHTGGGRES-------GSDAWKQYMRRS 328
Cdd:cd07084 371 LTAAIYSNDpifLQE----LIGNLWVAGRTYAILRGR----TGVAPNQNHGGGPAADprgagigGPEAIKLVWRCH 438
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
40-328 |
4.37e-15 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 75.90 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 40 KIIAKVLEDNKLPGAICSLTCGGAdiGTAMAKDERVNLLSFTGSTQVGKQVGLM--VQERFGRSLLELGGNNAIIAFEDA 117
Cdd:PRK11903 193 RMVKDVVAAGILPAGALSVVCGSS--AGLLDHLQPFDVVSFTGSAETAAVLRSHpaVVQRSVRVNVEADSLNSALLGPDA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 118 DLSlvvpSALFAAVG---------TAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTK-QAVS 187
Cdd:PRK11903 271 APG----SEAFDLFVkevvremtvKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRaQLAA 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 188 MFLGAveEAKKEGGTVVYGGKV---MDRP---GNYVEPTI-VTGLGHDASIAH-TETFAPILYVFKFKNEEEVFAWNNEV 259
Cdd:PRK11903 347 VRAGL--AALRAQAEVLFDGGGfalVDADpavAACVGPTLlGASDPDAATAVHdVEVFGPVATLLPYRDAAHALALARRG 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 260 KQGLSSSIFTKD---LGRIFRWLGPKGsdcGIVNVNIPTSGAEIGG--------AFGGEKHTGGGRE-SGSDAWKQYMRR 327
Cdd:PRK11903 425 QGSLVASVYSDDaafLAAAALELADSH---GRVHVISPDVAALHTGhgnvmpqsLHGGPGRAGGGEElGGLRALAFYHRR 501
|
.
gi 194380572 328 S 328
Cdd:PRK11903 502 S 502
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
61-254 |
9.61e-14 |
|
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: 71.75 E-value: 9.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 61 GGADIGTAMAK---DervNLLsFTGSTQVGKQVglM---------VQerfgrslLELGGNN-AIIAfEDADLSLVVPSAL 127
Cdd:cd07133 165 GGADVAAAFSSlpfD---HLL-FTGSTAVGRHV--MraaaenltpVT-------LELGGKSpAIIA-PDADLAKAAERIA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 128 FAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQI---RVGNPwDpnvlYGPLHTKQAVSMFLGAVEEAKKEGGTVV 204
Cdd:cd07133 231 FGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNP-D----YTSIINERHYARLQGLLEDARAKGARVI 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 194380572 205 yggKVMDRPGNYVE-----PTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFA 254
Cdd:cd07133 306 ---ELNPAGEDFAAtrklpPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAID 357
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
26-317 |
2.34e-12 |
|
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: 67.44 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 26 AAFMSTSLISVAVTKIIAKVLEDNKLPGAIcSLTCGGADIGTAMAkDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLEL 105
Cdd:cd07137 131 AVVLKPSELAPATSALLAKLIPEYLDTKAI-KVIEGGVPETTALL-EQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLEL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 106 GGNNAIIAFEDADLSLVVPSALFAAVGT-AGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTK- 183
Cdd:cd07137 209 GGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHh 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 184 -QAVSMFLGAVEEAKKeggtVVYGGKVmDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQG 262
Cdd:cd07137 289 fQRLSRLLDDPSVADK----IVHGGER-DEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKP 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194380572 263 LSSSIFT--KDLGRIFRWLGPKGS----DCgIVNVNIPTSgaeiggAFGGEKHTGGGRESG 317
Cdd:cd07137 364 LAAYVFTknKELKRRIVAETSSGGvtfnDT-VVQYAIDTL------PFGGVGESGFGAYHG 417
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
26-317 |
1.80e-11 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 65.07 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 26 AAFMSTSLISVAVTKIIAKVLEDNKLPGAICSLTcgGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLEL 105
Cdd:PLN02174 142 AVVLKPSELAPASSALLAKLLEQYLDSSAVRVVE--GAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 106 GGNNAIIAFEDADLSLVVPSALFAAVG-TAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQ 184
Cdd:PLN02174 220 GGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTH 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 185 AVSmfLGAVEEAKKEGGTVVYGGKvMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLS 264
Cdd:PLN02174 300 FDR--LSKLLDEKEVSDKIVYGGE-KDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLA 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 194380572 265 SSIFTKDlGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESG 317
Cdd:PLN02174 377 AYLFTHN-KKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGESGMGAYHG 428
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
61-328 |
5.20e-10 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 60.51 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 61 GGADIGTAMAkDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNN-AIIAFEDA--DLSLVVPSALFAAVGT-AGQ 136
Cdd:PLN02203 172 GGPAVGEQLL-QHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCpCIVDSLSSsrDTKVAVNRIVGGKWGScAGQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 137 RCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTK--QAVSMFLgaveEAKKEGGTVVYGGKvMDRPG 214
Cdd:PLN02203 251 ACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKhfQRLSNLL----KDPRVAASIVHGGS-IDEKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 215 NYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIP 294
Cdd:PLN02203 326 LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAII 405
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 194380572 295 TSGAEiGGAFGGEKHTGGGRESGSDAW------KQYMRRS 328
Cdd:PLN02203 406 QYACD-SLPFGGVGESGFGRYHGKYSFdtfsheKAVLRRS 444
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
35-267 |
1.40e-04 |
|
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: 43.30 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 35 SVAVTKIIAKVLEDNKLPGAICSL-TCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQER------FGrsllELGG 107
Cdd:cd07129 150 SELVARAIRAALRATGLPAGVFSLlQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARpepipfYA----ELGS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 108 NNAIIafedadlslVVPSAL----------FAA--VGTAGQRCTTARRLFIHESIH-DEVVNRLKKAYAQirvgnpWDPn 174
Cdd:cd07129 226 VNPVF---------ILPGALaergeaiaqgFVGslTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAA------APA- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 175 vlyGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTI--VTG---LGHDAsiAHTETFAPILYVFKFKNE 249
Cdd:cd07129 290 ---QTMLTPGIAEAYRQGVEALAAAPGVRVLAGGAAAEGGNQAAPTLfkVDAaafLADPA--LQEEVFGPASLVVRYDDA 364
|
250
....*....|....*...
gi 194380572 250 EEVFAWNNEVKQGLSSSI 267
Cdd:cd07129 365 AELLAVAEALEGQLTATI 382
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
62-245 |
1.90e-03 |
|
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: 40.15 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 62 GADIGTAMAKDERVNLLSFTGSTQVGKQvgLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTA 141
Cdd:cd07127 265 EEPIAQTLATRPEVRIIDFTGSNAFGDW--LEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTP 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 142 RRLFI----------HESiHDEVVNRLKKAYAQIrVGNPWDPNVLYGPLHTkQAVsmfLGAVEEAKKEGGTVVYGGKVM- 210
Cdd:cd07127 343 QNIYVprdgiqtddgRKS-FDEVAADLAAAIDGL-LADPARAAALLGAIQS-PDT---LARIAEARQLGEVLLASEAVAh 416
|
170 180 190
....*....|....*....|....*....|....*..
gi 194380572 211 -DRPGNYVE-PTIVTGLGHDASIAHTETFAPILYVFK 245
Cdd:cd07127 417 pEFPDARVRtPLLLKLDASDEAAYAEERFGPIAFVVA 453
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
32-251 |
4.81e-03 |
|
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: 38.63 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 32 SLISVAVTKIIaKVLEDNKLPGAICSLT-CGGADIGTAMaKDERVNLLSFTGSTQVGKQVGLMVQerfGRSLLELGGNNA 110
Cdd:cd07126 179 SKVSVVMEQFL-RLLHLCGMPATDVDLIhSDGPTMNKIL-LEANPRMTLFTGSSKVAERLALELH---GKVKLEDAGFDW 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380572 111 IIAFED-ADLSLVVPSALFAAVGTAGQRCTTARRLFIHES-IHDEVVNRLKKAYAQIRVgnpwdPNVLYGPLHTKQAVSM 188
Cdd:cd07126 254 KILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKALAEQRKL-----EDLTIGPVLTWTTERI 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194380572 189 FLGAVEEAKKEGGTVVYGGKVM---DRPGNY--VEPTIV------TGLGHDASIAHTETFAPILYVFKFKNEEE 251
Cdd:cd07126 329 LDHVDKLLAIPGAKVLFGGKPLtnhSIPSIYgaYEPTAVfvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQL 402
|
|
| |
