|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
1-222 |
2.56e-168 |
|
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: 472.46 E-value: 2.56e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07130 254 MEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAI 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHnAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:cd07130 334 EEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSD-APIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLR 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701367271 161 RIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKLYMRRSTCTINYS 222
Cdd:cd07130 413 NAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
1-222 |
2.15e-156 |
|
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: 442.39 E-value: 2.15e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07086 255 MDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINR--PGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKD 158
Cdd:cd07086 335 EIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701367271 159 LGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKLYMRRSTCTINYS 222
Cdd:cd07086 415 LREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
2-233 |
1.15e-118 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 347.59 E-value: 1.15e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:PLN02315 277 DDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKVINRPGNYVEPTIVTgLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGR 161
Cdd:PLN02315 357 IIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPET 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701367271 162 IFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKLYMRRSTCTINYSKDLPLAQGIKF 233
Cdd:PLN02315 436 IFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTINYGNELPLAQGINF 507
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
1-219 |
8.51e-85 |
|
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: 258.29 E-value: 8.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07078 215 FDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYI 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVI-NRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDL 159
Cdd:cd07078 295 EDAKAEGAKLLCGGKRLeGGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDL 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 160 GRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKLYMRRSTCTI 219
Cdd:cd07078 375 ERALRVA--ERLEAGTVWINDYSVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-221 |
2.32e-82 |
|
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: 253.51 E-value: 2.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:COG1012 260 LDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYI 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINR-PGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDL 159
Cdd:COG1012 340 EDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701367271 160 GRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKLYMRRSTCTINY 221
Cdd:COG1012 420 ARARRVA--RRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
1-216 |
2.95e-82 |
|
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: 252.84 E-value: 2.95e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:pfam00171 245 LEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYV 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:pfam00171 325 EDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLE 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 701367271 161 RIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKLYMRRST 216
Cdd:pfam00171 405 RALRVA--RRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
1-213 |
6.05e-59 |
|
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: 192.38 E-value: 6.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRP----GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFT 156
Cdd:cd07114 318 ARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701367271 157 KDLGRIFRWlgPKGSDCGIVNVNI-----PTSgaeiggAFGGEKHTGGGRESGSDSWKLYMR 213
Cdd:cd07114 398 RDLARAHRV--ARAIEAGTVWVNTyralsPSS------PFGGFKDSGIGRENGIEAIREYTQ 451
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
2-222 |
3.39e-58 |
|
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: 191.02 E-value: 3.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07131 255 DDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKVINR----PGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTK 157
Cdd:cd07131 335 IGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTE 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701367271 158 DLGRIFRWLGpkgsDC--GIVNVNIPTSGAEIGGAFGGEKHTGGG-RESGSDSWKLYMRRSTCTINYS 222
Cdd:cd07131 415 DVNKAFRARR----DLeaGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYVDYS 478
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
1-205 |
1.83e-56 |
|
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: 185.71 E-value: 1.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07103 236 FDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALV 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:cd07103 316 EDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 701367271 161 RIFRwLGpKGSDCGIVNVNIPT-SGAEIggAFGGEKHTGGGRESGS 205
Cdd:cd07103 396 RAWR-VA-EALEAGMVGINTGLiSDAEA--PFGGVKESGLGREGGK 437
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
1-202 |
5.55e-50 |
|
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: 169.04 E-value: 5.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07092 236 FDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFV 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQqGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:cd07092 316 ERAPA-HARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 701367271 161 RIFRWLGPKGSDCGIVNVNIPTSgAEIggAFGGEKHTGGGRE 202
Cdd:cd07092 395 RAMRLSARLDFGTVWVNTHIPLA-AEM--PHGGFKQSGYGKD 433
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
2-208 |
1.03e-49 |
|
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: 167.71 E-value: 1.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07104 219 DDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKvinRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGR 161
Cdd:cd07104 299 DAVAAGARLLTGGT---YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLER 375
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 701367271 162 IFRwLGpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSW 208
Cdd:cd07104 376 AMA-FA-ERLETGMVHINDQTVNDEPHVPFGGVKASGGGRFGGPASL 420
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
1-212 |
1.12e-48 |
|
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: 165.43 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYV 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRP----GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFT 156
Cdd:cd07093 316 ELARAEGATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWT 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701367271 157 KDLGRIFRWlgPKGSDCGIVNVN------IPTsgaeiggAFGGEKHTGGGRESGSDSWKLYM 212
Cdd:cd07093 396 RDLGRAHRV--ARRLEAGTVWVNcwlvrdLRT-------PFGGVKASGIGREGGDYSLEFYT 448
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
1-206 |
1.74e-48 |
|
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: 165.30 E-value: 1.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:cd07115 316 DVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLG 395
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 701367271 161 RIFRWlgPKGSDCGIVNVNipTSGA-EIGGAFGGEKHTGGGRESGSD 206
Cdd:cd07115 396 RAHRV--AAALKAGTVWIN--TYNRfDPGSPFGGYKQSGFGREMGRE 438
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
1-219 |
7.98e-48 |
|
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: 161.24 E-value: 7.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAkayaqvrigdpwdpdtlygplhtkeavkmfldav 80
Cdd:cd06534 211 DEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDEFVEKLV---------------------------------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 dqakqqggsvvyggkvinrpgnyvepTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:cd06534 257 --------------------------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLN 310
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 701367271 161 RIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKLYMRRSTCTI 219
Cdd:cd06534 311 RALRVA--ERLRAGTVYINDSSIGVGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
2-202 |
4.34e-47 |
|
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: 160.70 E-value: 4.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07100 215 DDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG- 160
Cdd:cd07100 295 EAVAAGATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLEr 374
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 701367271 161 --RIFRWLgpkgsDCGIVNVNIPT-SGAEIggAFGGEKHTGGGRE 202
Cdd:cd07100 375 aeRVARRL-----EAGMVFINGMVkSDPRL--PFGGVKRSGYGRE 412
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
2-206 |
5.99e-47 |
|
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: 161.26 E-value: 5.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07097 255 DDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKVINRP--GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDL 159
Cdd:cd07097 335 IARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSL 414
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 701367271 160 GRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTG-GGRESGSD 206
Cdd:cd07097 415 KHATHFK--RRVEAGVVMVNLPTAGVDYHVPFGGRKGSSyGPREQGEA 460
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
2-204 |
2.76e-46 |
|
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: 159.23 E-value: 2.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTK---EAVKMFld 78
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKmqyDKVKEL-- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 79 aVDQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKD 158
Cdd:cd07106 310 -VEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSD 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 701367271 159 LGRIFRwLGPKgSDCGIVNVNiptSGAEIGGA--FGGEKHTGGGRESG 204
Cdd:cd07106 389 LERAEA-VARR-LEAGTVWIN---THGALDPDapFGGHKQSGIGVEFG 431
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
1-212 |
2.88e-46 |
|
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: 159.33 E-value: 2.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07089 242 LDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYI 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKvinRP-----GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIF 155
Cdd:cd07089 322 ARGRDEGARLVTGGG---RPagldkGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 156 TKDLGR---IFRWLgpkgsDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDSWKLYM 212
Cdd:cd07089 399 SADVDRayrVARRI-----RTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
1-164 |
4.85e-46 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 158.92 E-value: 4.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:PRK13473 256 FDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQG-GSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDL 159
Cdd:PRK13473 336 ERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDV 415
|
....*
gi 701367271 160 GRIFR 164
Cdd:PRK13473 416 GRAHR 420
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
2-207 |
1.56e-45 |
|
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: 157.11 E-value: 1.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07150 239 ADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKvinRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGR 161
Cdd:cd07150 319 DAVAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQR 395
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 701367271 162 IFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDS 207
Cdd:cd07150 396 AFKL--AERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWS 439
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
1-213 |
5.42e-45 |
|
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: 155.93 E-value: 5.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07090 234 FDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYI 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVIN-----RPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIF 155
Cdd:cd07090 314 ESAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVF 393
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 701367271 156 TKDLGRIFRWLGP-KGSDCGIVNVNIptSGAEIggAFGGEKHTGGGRESGSDSWKLYMR 213
Cdd:cd07090 394 TRDLQRAHRVIAQlQAGTCWINTYNI--SPVEV--PFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
1-164 |
6.67e-45 |
|
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: 155.89 E-value: 6.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07088 252 MKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMV 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVIN-RPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDL 159
Cdd:cd07088 332 ERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENL 411
|
....*
gi 701367271 160 GRIFR 164
Cdd:cd07088 412 NTAMR 416
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
2-204 |
2.90e-44 |
|
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: 154.38 E-value: 2.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07151 251 EDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKVinrPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGR 161
Cdd:cd07151 331 QAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLER 407
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 701367271 162 IFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESG 204
Cdd:cd07151 408 GVQF--ARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNG 448
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
2-219 |
3.34e-44 |
|
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: 153.67 E-value: 3.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07146 238 DDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKvinRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGR 161
Cdd:cd07146 318 EAIAQGARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDT 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701367271 162 IFRWLgpKGSDCGIVNVN------IPTSgaeiggAFGGEKHTG-GGRESGSDSWKLYMRRSTCTI 219
Cdd:cd07146 395 IKRLV--ERLDVGTVNVNevpgfrSELS------PFGGVKDSGlGGKEGVREAMKEMTNVKTYSL 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
1-212 |
5.58e-44 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 154.08 E-value: 5.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:PLN02278 279 FDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:PLN02278 359 QDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQ 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701367271 161 RIFRWlgPKGSDCGIVNVN---IPTSGAeiggAFGGEKHTGGGRESGSDSWKLYM 212
Cdd:PLN02278 439 RAWRV--SEALEYGIVGVNeglISTEVA----PFGGVKQSGLGREGSKYGIDEYL 487
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
2-202 |
6.20e-44 |
|
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: 153.14 E-value: 6.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07149 241 ADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKvinRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGR 161
Cdd:cd07149 321 EAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQK 397
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 701367271 162 IFRWLgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKHTGGGRE 202
Cdd:cd07149 398 ALKAA--RELEVGGVMINdSSTFRVD-HMPYGGVKESGTGRE 436
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
1-213 |
6.35e-44 |
|
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: 153.15 E-value: 6.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07099 236 LADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHV 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDL- 159
Cdd:cd07099 316 DDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLa 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 701367271 160 --GRIFRWLgpkgsDCGIVNVNIPTSGAEIGGA-FGGEKHTGGGRESGSDSWKLYMR 213
Cdd:cd07099 396 raEAIARRL-----EAGAVSINDVLLTAGIPALpFGGVKDSGGGRRHGAEGLREFCR 447
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
2-202 |
2.35e-43 |
|
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: 151.63 E-value: 2.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07147 240 SDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVN 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKvinRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGR 161
Cdd:cd07147 320 EAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEK 396
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 701367271 162 IFR-WlgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKHTGGGRE 202
Cdd:cd07147 397 ALRaW---DELEVGGVVINdVPTFRVD-HMPYGGVKDSGIGRE 435
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
1-201 |
3.23e-42 |
|
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: 148.52 E-value: 3.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDA-DLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDA 79
Cdd:cd07112 244 FADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGY 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 80 VDQAKQQGGSVVYGGKVINR--PGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTK 157
Cdd:cd07112 324 IESGKAEGARLVAGGKRVLTetGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTS 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 701367271 158 DLGRIFRwlGPKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGR 201
Cdd:cd07112 404 DLSRAHR--VARRLRAGTVWVNC-FDEGDITTPFGGFKQSGNGR 444
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
1-221 |
7.84e-42 |
|
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: 147.52 E-value: 7.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAA-VGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDA 79
Cdd:cd07107 234 FPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHY 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 80 VDQAKQQGGSVVYGGKvinRP-------GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSS 152
Cdd:cd07107 314 IDSAKREGARLVTGGG---RPegpalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTA 390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701367271 153 SIFTKDLGRIFRwlGPKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDSWKLYMRRSTCTINY 221
Cdd:cd07107 391 AIWTNDISQAHR--TARRVEAGYVWIN-GSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
1-203 |
8.07e-42 |
|
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: 147.49 E-value: 8.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07145 242 LKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLV 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVInrPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:cd07145 322 NDAVEKGGKILYGGKRD--EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDIN 399
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 701367271 161 RIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES 203
Cdd:cd07145 400 RALKV--ARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREG 440
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
1-213 |
8.20e-42 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 148.10 E-value: 8.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:PRK13252 260 FDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYI 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINR----PGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFT 156
Cdd:PRK13252 340 EKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFT 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 157 KDLGRIFRWLGpkGSDCGIVNVNipTSG---AEIggAFGGEKHTGGGRESGSDSWKLYMR 213
Cdd:PRK13252 420 ADLSRAHRVIH--QLEAGICWIN--TWGespAEM--PVGGYKQSGIGRENGIATLEHYTQ 473
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
2-221 |
8.25e-42 |
|
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: 148.52 E-value: 8.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07124 292 EDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKqQGGSVVYGGKVINRP--GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDL 159
Cdd:cd07124 372 IGK-SEGRLLLGGEVLELAaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701367271 160 GRI--FRwlgpKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTG-GGRESGSDSWKLYMRRSTCTINY 221
Cdd:cd07124 451 EHLerAR----REFEVGNLYANRKITGALVGrQPFGGFKMSGtGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
1-204 |
1.40e-41 |
|
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: 147.00 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPW-DPDtlYGPL---HTKEAVKMF 76
Cdd:cd07109 236 FADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLeDPD--LGPLisaKQLDRVEGF 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 77 ldaVDQAKQQGGSVVYGGKVINRP---GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSS 153
Cdd:cd07109 314 ---VARARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAG 390
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 701367271 154 IFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESG 204
Cdd:cd07109 391 VWTRDGDRALRV--ARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKG 439
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
2-221 |
5.72e-41 |
|
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: 145.66 E-value: 5.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07113 261 KDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLD 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGR 161
Cdd:cd07113 341 DARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSK 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 162 IFRWLgPKgSDCGIVNVNIPTSgAEIGGAFGGEKHTGGGRESGSDSWKLYMRRSTCTINY 221
Cdd:cd07113 421 ALRYI-PR-IEAGTVWVNMHTF-LDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIRY 477
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
1-219 |
3.17e-40 |
|
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: 143.50 E-value: 3.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07091 261 FDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYI 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:cd07091 341 ESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDIN 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 161 RIFR----------WLgpkgsDC-GIVNVNIPtsgaeiggaFGGEKHTGGGRESGSDSWKLYMRRSTCTI 219
Cdd:cd07091 421 KALRvsralkagtvWV-----NTyNVFDAAVP---------FGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
1-221 |
1.11e-38 |
|
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: 139.55 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07140 267 FADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYC 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEE--EEVFAWNNEVKQGLSSSIFTKD 158
Cdd:cd07140 347 ERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDTEYGLASGVFTKD 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701367271 159 LGRIFRWlgPKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDSWKLYMRRSTCTINY 221
Cdd:cd07140 427 INKALYV--SDKLEAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIEY 486
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
1-202 |
1.86e-38 |
|
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: 138.65 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGT-AGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDA 79
Cdd:cd07108 235 FPDADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGY 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 80 VDQAKQ-QGGSVVYGGK----VINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSI 154
Cdd:cd07108 315 IDLGLStSGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 701367271 155 FTKDLGRIFRwlGPKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRE 202
Cdd:cd07108 395 WTRDLGRALR--AAHALEAGWVQVN-QGGGQQPGQSYGGFKQSGLGRE 439
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
2-204 |
2.43e-38 |
|
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: 138.48 E-value: 2.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07139 256 DDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKvinRP-----GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFT 156
Cdd:cd07139 336 KGRAEGARLVTGGG---RPagldrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWT 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 701367271 157 KDLGR---IFRWLgpkgsDCGIVNVNIPTSgaEIGGAFGGEKHTGGGRESG 204
Cdd:cd07139 413 ADVERglaVARRI-----RTGTVGVNGFRL--DFGAPFGGFKQSGIGREGG 456
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
1-203 |
6.12e-38 |
|
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: 137.59 E-value: 6.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07117 254 FDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYV 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRP----GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFT 156
Cdd:cd07117 334 DIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFT 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 701367271 157 KDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRES 203
Cdd:cd07117 414 KDINRALRV--ARAVETGRVWVNtynqIPA-----GAPFGGYKKSGIGRET 457
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
2-164 |
1.17e-37 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 135.63 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTL-YGPLHTKEAVKMFLDAV 80
Cdd:PRK10090 191 DDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAERNDIaMGPLINAAALERVEQKV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:PRK10090 271 ARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLN 350
|
....
gi 701367271 161 RIFR 164
Cdd:PRK10090 351 VAMK 354
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
1-202 |
2.02e-37 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 136.19 E-value: 2.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:PRK11241 265 FDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHI 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:PRK11241 345 ADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLS 424
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 701367271 161 RIFRWlgPKGSDCGIVNVNIPTSGAEIgGAFGGEKHTGGGRE 202
Cdd:PRK11241 425 RVFRV--GEALEYGIVGINTGIISNEV-APFGGIKASGLGRE 463
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
2-220 |
4.09e-37 |
|
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: 135.39 E-value: 4.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07082 259 PDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLID 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKviNRPGNYVEPTIvtgLPHNAP---IVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKD 158
Cdd:cd07082 339 DAVAKGATVLNGGG--REGGNLIYPTL---LDPVTPdmrLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKD 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701367271 159 LGRIF---RWLgpkgsDCGIVNVNIPTS-GAEIgGAFGGEKHTGGGRESGSDSWKLYMRRSTCTIN 220
Cdd:cd07082 414 INKARklaDAL-----EVGTVNINSKCQrGPDH-FPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
1-207 |
4.34e-37 |
|
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: 134.78 E-value: 4.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07120 237 FDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVY-GGKVINR--PGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTK 157
Cdd:cd07120 317 ERAIAAGAEVVLrGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 701367271 158 DLGRIFRWlgPKGSDCGIVNVNipTSGAEIGGA-FGGEKHTGGGRESGSDS 207
Cdd:cd07120 397 DLARAMRV--ARAIRAGTVWIN--DWNKLFAEAeEGGYRQSGLGRLHGVAA 443
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
1-205 |
7.65e-37 |
|
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: 134.75 E-value: 7.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07119 253 FADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKvinRP-------GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSS 153
Cdd:cd07119 333 QLGKEEGARLVCGGK---RPtgdelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGA 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701367271 154 IFTKDLGRIFRWLgpKGSDCGIVNVN---IPTSGAEiggaFGGEKHTGGGRESGS 205
Cdd:cd07119 410 VWTKDIARANRVA--RRLRAGTVWINdyhPYFAEAP----WGGYKQSGIGRELGP 458
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
1-219 |
5.02e-36 |
|
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: 132.47 E-value: 5.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07141 265 FADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELI 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:cd07141 345 ESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDID 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 701367271 161 RIFRWlgPKGSDCGIVNVNIPTSGAeIGGAFGGEKHTGGGRESGSDSWKLYMRRSTCTI 219
Cdd:cd07141 425 KAITF--SNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
22-202 |
6.83e-36 |
|
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: 132.08 E-value: 6.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 22 GQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVDQAKQQGGSVVYGGKVINRP- 100
Cdd:cd07559 280 GEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 101 ---GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVN 177
Cdd:cd07559 360 ldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRV--ARGIQTGRVW 437
|
170 180
....*....|....*....|....*....
gi 701367271 178 VN----IPTsgaeiGGAFGGEKHTGGGRE 202
Cdd:cd07559 438 VNcyhqYPA-----HAPFGGYKKSGIGRE 461
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
1-204 |
1.67e-35 |
|
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: 130.54 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07118 238 FADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVIN-RPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDL 159
Cdd:cd07118 318 DAGRAEGATLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDI 397
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 701367271 160 GRIFrwLGPKGSDCGIVNVN-IPTSGAEIggAFGGEKHTGGGRESG 204
Cdd:cd07118 398 DTAL--TVARRIRAGTVWVNtFLDGSPEL--PFGGFKQSGIGRELG 439
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
1-201 |
1.78e-35 |
|
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: 130.00 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRigdpWDPDTLyGPLHTKEAVKMFLDAV 80
Cdd:cd07105 220 LEDADLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLF----AGPVVL-GSLVSAAAADRVKELV 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGK-VINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDL 159
Cdd:cd07105 295 DDALSKGAKLVVGGLaDESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDL 374
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 701367271 160 GRIFRwLGpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGR 201
Cdd:cd07105 375 ARALA-VA-KRIESGAVHINGMTVHDEPTLPHGGVKSSGYGR 414
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
2-202 |
1.02e-34 |
|
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: 128.32 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07094 241 RDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKvinRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGR 161
Cdd:cd07094 321 EAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNV 397
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 701367271 162 IFRwlGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRE 202
Cdd:cd07094 398 AFK--AAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGRE 436
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
1-213 |
3.40e-34 |
|
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: 127.61 E-value: 3.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07142 261 CEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYI 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:cd07142 341 EHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNID 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 701367271 161 RIFRWLgpKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDSWKLYMR 213
Cdd:cd07142 421 TANTLS--RALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
1-204 |
4.57e-34 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 127.54 E-value: 4.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:PLN02467 270 FDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKvinRP-----GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIF 155
Cdd:PLN02467 350 STAKSEGATILCGGK---RPehlkkGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 701367271 156 TKDLGRIFRWlgPKGSDCGIVNVN--------IPtsgaeiggaFGGEKHTGGGRESG 204
Cdd:PLN02467 427 SNDLERCERV--SEAFQAGIVWINcsqpcfcqAP---------WGGIKRSGFGRELG 472
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
1-204 |
5.64e-34 |
|
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: 126.70 E-value: 5.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07110 239 FDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVIN--RPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKD 158
Cdd:cd07110 319 ARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRD 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 701367271 159 LGRIFRWlgPKGSDCGIVNVNIPTSgAEIGGAFGGEKHTGGGRESG 204
Cdd:cd07110 399 AERCDRV--AEALEAGIVWINCSQP-CFPQAPWGGYKRSGIGRELG 441
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
1-206 |
4.19e-32 |
|
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: 121.26 E-value: 4.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07101 235 LEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHV 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVinRP--GNYV-EPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTK 157
Cdd:cd07101 315 DDAVAKGATVLAGGRA--RPdlGPYFyEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 701367271 158 DLGRIfRWLGPKgSDCGIVNVN--IPTSGAEIGGAFGGEKHTGGGRESGSD 206
Cdd:cd07101 393 DGARG-RRIAAR-LRAGTVNVNegYAAAWASIDAPMGGMKDSGLGRRHGAE 441
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
1-220 |
4.62e-32 |
|
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: 121.75 E-value: 4.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQV-RIGDPWDPDTLYGPLHTKEAVKMFLDA 79
Cdd:cd07144 263 FEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDTVVGPQVSKTQYDRVLSY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 80 VDQAKQQGGSVVYGG---KVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFT 156
Cdd:cd07144 343 IEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFT 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701367271 157 KDLGRIFRWLgpKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDSWKLYMRRSTCTIN 220
Cdd:cd07144 423 KDIRRAHRVA--RELEAGMVWIN-SSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHIN 483
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
1-213 |
1.88e-31 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 120.31 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:PLN02766 278 FDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYI 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDL- 159
Cdd:PLN02766 358 EHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLd 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 701367271 160 --GRIFRWLgpkgsDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDSWKLYMR 213
Cdd:PLN02766 438 vaNTVSRSI-----RAGTIWVNC-YFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
1-220 |
2.73e-31 |
|
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: 119.56 E-value: 2.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07143 264 FDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:cd07143 344 ESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNIN 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701367271 161 RIFRWLGP-KGSDCGIVNVNIPTSGAeiggAFGGEKHTGGGRESGSDSWKLYMRRSTCTIN 220
Cdd:cd07143 424 NAIRVANAlKAGTVWVNCYNLLHHQV----PFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
8-202 |
5.77e-30 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 115.61 E-value: 5.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 8 LVIPSA-LFAAVGTA--------GQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLD 78
Cdd:PRK09406 239 IVMPSAdLDRAAETAvtarvqnnGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEK 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 79 AVDQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKD 158
Cdd:PRK09406 319 QVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRD 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 701367271 159 LGRIFRWLgpKGSDCGIVNVN-IPTSGAEIGgaFGGEKHTGGGRE 202
Cdd:PRK09406 399 EAEQERFI--DDLEAGQVFINgMTVSYPELP--FGGVKRSGYGRE 439
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
1-204 |
2.92e-29 |
|
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: 113.93 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07098 242 LDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELV 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRP----GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFT 156
Cdd:cd07098 322 ADAVEKGARLLAGGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFG 401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701367271 157 KDLGRIFRWLgpKGSDCGIVNVNiptsgaEIGGA-------FGGEKHTGGGRESG 204
Cdd:cd07098 402 KDIKRARRIA--SQLETGMVAIN------DFGVNyyvqqlpFGGVKGSGFGRFAG 448
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
2-206 |
7.69e-29 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 113.05 E-value: 7.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:PRK09407 272 DDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKVinRP--GNYV-EPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKD 158
Cdd:PRK09407 352 DAVAKGATVLAGGKA--RPdlGPLFyEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGD 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 701367271 159 LGR---IFRWLgpkgsDCGIVNVN---IPTSGAeIGGAFGGEKHTGGGRESGSD 206
Cdd:PRK09407 430 TARgraIAARI-----RAGTVNVNegyAAAWGS-VDAPMGGMKDSGLGRRHGAE 477
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
2-212 |
4.26e-28 |
|
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: 110.46 E-value: 4.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07152 230 DDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVD 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKvinRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGR 161
Cdd:cd07152 310 DSVAAGARLEAGGT---YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGR 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 701367271 162 IFRwLGPKgSDCGIVNVNIPTSGAEIGGAFGGEKHTG-GGRESGSDSWKLYM 212
Cdd:cd07152 387 AMA-LADR-LRTGMLHINDQTVNDEPHNPFGGMGASGnGSRFGGPANWEEFT 436
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
1-204 |
9.95e-28 |
|
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: 109.51 E-value: 9.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07138 249 LDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYI 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGkvINRP-----GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIF 155
Cdd:cd07138 329 QKGIEEGARLVAGG--PGRPeglerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVW 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 701367271 156 TKDLGR---IFRWLgpkgsDCGIVNVNipTSGAEIGGAFGGEKHTGGGRESG 204
Cdd:cd07138 407 SADPERaraVARRL-----RAGQVHIN--GAAFNPGAPFGGYKQSGNGREWG 451
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
1-161 |
2.04e-26 |
|
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: 105.79 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRP---GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTK 157
Cdd:cd07102 314 ADAIAKGARALIDGALFPEDkagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTK 393
|
....
gi 701367271 158 DLGR 161
Cdd:cd07102 394 DIAR 397
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
1-215 |
2.58e-26 |
|
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: 105.94 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07111 265 FDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELV 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:cd07111 345 EEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLS 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 161 RIFRwLGPkGSDCGIVNVNI-----PTSGaeiggaFGGEKHTGGGRESGSDSWKLYMRRS 215
Cdd:cd07111 425 LALE-VAL-SLKAGVVWINGhnlfdAAAG------FGGYRESGFGREGGKEGLYEYLRPS 476
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
2-204 |
6.23e-26 |
|
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: 104.28 E-value: 6.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLH-KSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAV 80
Cdd:cd07095 217 DVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPdGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQ 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTI--VTGLphnAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKD 158
Cdd:cd07095 297 QDLLALGGEPLLAMERLVAGTAFLSPGIidVTDA---ADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDD 373
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 701367271 159 lGRIFRWLGPKgSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESG 204
Cdd:cd07095 374 -EALFERFLAR-IRAGIVNWNRPTTGASSTAPFGGVGLSGNHRPSA 417
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
3-181 |
7.93e-26 |
|
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: 104.52 E-value: 7.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 3 DADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVDQ 82
Cdd:cd07085 256 DADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIES 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 83 AKQQGGSVVYGGKVINRP----GNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKD 158
Cdd:cd07085 336 GVEEGAKLVLDGRGVKVPgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRS 415
|
170 180
....*....|....*....|....*
gi 701367271 159 --LGRIFRwlgpKGSDCGIVNVNIP 181
Cdd:cd07085 416 gaAARKFQ----REVDAGMVGINVP 436
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
1-213 |
1.51e-25 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 104.12 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKlAKAYAQVR-IGDPWDPDTLYGPLHTKEAVKMFLDA 79
Cdd:PLN02466 315 CEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK-AKARALKRvVGDPFKKGVEQGPQIDSEQFEKILRY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 80 VDQAKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDL 159
Cdd:PLN02466 394 IKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701367271 160 ---GRIFRWLgpkgsDCGIVNVN--------IPtsgaeiggaFGGEKHTGGGRESGSDSWKLYMR 213
Cdd:PLN02466 474 dtaNTLSRAL-----RVGTVWVNcfdvfdaaIP---------FGGYKMSGIGREKGIYSLNNYLQ 524
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
2-200 |
7.51e-25 |
|
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: 101.34 E-value: 7.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07148 242 RSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQGGSVVYGGKVINRpgNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGR 161
Cdd:cd07148 322 EAVAAGARLLCGGKRLSD--TTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDV 399
|
170 180 190
....*....|....*....|....*....|....*....
gi 701367271 162 IFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGG 200
Cdd:cd07148 400 ALKAV--RRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
4-204 |
8.25e-25 |
|
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: 101.89 E-value: 8.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 4 ADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMfLDAVDQA 83
Cdd:cd07125 292 ALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKL-LRAHTEL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 84 KQQGGSVVYGGKVINRPGNYVEPTIVTGlpHNAPIVHTETFAPILYVLKFEEE--EEVFAWNNEVKQGLSSSIFTKDLGR 161
Cdd:cd07125 371 MRGEAWLIAPAPLDDGNGYFVAPGIIEI--VGIFDLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDERE 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 701367271 162 IFRWLgpKGSDCGIVNVNIPTSGAeIGGA--FGGEKHTGGGRESG 204
Cdd:cd07125 449 IEYWR--ERVEAGNLYINRNITGA-IVGRqpFGGWGLSGTGPKAG 490
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
2-214 |
3.16e-23 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 97.26 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVD 81
Cdd:cd07083 280 ETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQgGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEE--EVFAWNNEVKQGLSSSIFTKDL 159
Cdd:cd07083 360 HGKNE-GQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 701367271 160 GRIfRWLGPKgSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSDSwklYMRR 214
Cdd:cd07083 439 EHL-EEARRE-FHVGNLYINRKITGALVGvQPFGGFKLSGTNAKTGGPH---YLRR 489
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
13-203 |
4.72e-23 |
|
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: 96.75 E-value: 4.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 13 ALFAAvgTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVDQAKQQGGSVVY 92
Cdd:cd07116 273 VMFAL--NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLT 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 93 GGKVINRPGN-----YVEPTIVTGlpHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlg 167
Cdd:cd07116 351 GGERNELGGLlgggyYVPTTFKGG--NKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRM-- 426
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 701367271 168 PKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRES 203
Cdd:cd07116 427 GRGIQAGRVWTNcyhlYPA-----HAAFGGYKQSGIGREN 461
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
2-164 |
7.28e-23 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 96.16 E-value: 7.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLyGPLHTKEAVKMFLDAVD 81
Cdd:PRK03137 297 EDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYM-GPVINQASFDKIMSYIE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 82 QAKQQgGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGR 161
Cdd:PRK03137 376 IGKEE-GRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREH 454
|
...
gi 701367271 162 IFR 164
Cdd:PRK03137 455 LEK 457
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
22-202 |
2.74e-20 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 88.80 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 22 GQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVDQAKQQGgSVVYGGKVINRPG 101
Cdd:PRK09847 299 GQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 102 nYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIP 181
Cdd:PRK09847 378 -AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRM--SRRLKAGSVFVNNY 454
|
170 180
....*....|....*....|.
gi 701367271 182 TSGaEIGGAFGGEKHTGGGRE 202
Cdd:PRK09847 455 NDG-DMTVPFGGYKQSGNGRD 474
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
3-202 |
1.05e-19 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 86.84 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 3 DADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVDQ 82
Cdd:PRK13968 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 83 AKQQGGSVVYGGKVINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGRI 162
Cdd:PRK13968 326 TLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQA 405
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 701367271 163 FRWlgPKGSDCGIVNVN-IPTSGAEIggAFGGEKHTGGGRE 202
Cdd:PRK13968 406 RQM--AARLECGGVFINgYCASDARV--AFGGVKKSGFGRE 442
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
3-203 |
2.93e-17 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 80.00 E-value: 2.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 3 DADLNLVIPSALFaavgTAGQRCTTARRLFLHKSIH-DEVVAKLAKAYAQVRIGDPW-DPDTLYGPLHTKEAVKMFLDAV 80
Cdd:PRK09457 259 DAAVHLIIQSAFI----SAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDaEPQPFMGAVISEQAAQGLVAAQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKVINRPGNYVEPTI--VTGLphnAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKD 158
Cdd:PRK09457 335 AQLLALGGKSLLEMTQLQAGTGLLTPGIidVTGV---AELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDD 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 701367271 159 LGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES 203
Cdd:PRK09457 412 REDYDQFL--LEIRAGIVNWNKPLTGASSAAPFGGVGASGNHRPS 454
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
2-158 |
7.52e-17 |
|
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: 78.80 E-value: 7.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTL---YGPLHTKEAVKMfld 78
Cdd:cd07135 225 KNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYtriVNPRHFNRLKSL--- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 79 aVDQAKqqgGSVVYGGKViNRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKD 158
Cdd:cd07135 302 -LDTTK---GKVVIGGEM-DEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDD 376
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-223 |
8.61e-17 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 78.64 E-value: 8.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 1 FEDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDpDTLYGPLHTKEAVKMFLDAV 80
Cdd:PLN00412 274 LEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLV 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 81 DQAKQQGGSVVYGGKvinRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLG 160
Cdd:PLN00412 353 MDAKEKGATFCQEWK---REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDIN 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701367271 161 RIFRWlgpkgSDC---GIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKLYMRRSTCTINYSK 223
Cdd:PLN00412 430 KAILI-----SDAmetGTVQINSAPARGPDHFPFQGLKDSGIGSQGITNSINMMTKVKSTVINLPK 490
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
4-158 |
8.64e-17 |
|
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: 78.78 E-value: 8.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 4 ADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVDQA 83
Cdd:cd07123 297 ADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHA 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 84 KQQGG-SVVYGGKVINRPGNYVEPTIV-TGLPHNaPIVHTETFAPILYVLKFEEE--EEVFAWNNEV-KQGLSSSIFTKD 158
Cdd:cd07123 377 KSDPEaEIIAGGKCDDSVGYFVEPTVIeTTDPKH-KLMTEEIFGPVLTVYVYPDSdfEETLELVDTTsPYALTGAIFAQD 455
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
21-215 |
8.59e-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: 75.77 E-value: 8.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 21 AGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVDQAKqQGGSVVYGGKVINRP 100
Cdd:cd07128 288 AGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLL-AEAEVVFGGPDRFEV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 101 -------GNYVEPTIVTGL-PHNAPIVH-TETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKD---LGRIFRWLGP 168
Cdd:cd07128 367 vgadaekGAFFPPTLLLCDdPDAATAVHdVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDpafARELVLGAAP 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 701367271 169 KGsdcGIVNVNIPTSGAEIGG--------AFGGEKHTGGGRE-SGSDSWKLYMRRS 215
Cdd:cd07128 447 YH---GRLLVLNRDSAKESTGhgsplpqlVHGGPGRAGGGEElGGLRGVKHYMQRT 499
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
21-204 |
4.28e-15 |
|
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: 73.41 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 21 AGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTL-YGPLHTKEAVKMFLDAVDQAKQQGGSVVYGGKViNR 99
Cdd:cd07134 236 AGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPdLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQF-DA 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 100 PGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGS-DCGI--- 175
Cdd:cd07134 315 AQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSgGVVVndv 394
|
170 180 190
....*....|....*....|....*....|...
gi 701367271 176 ----VNVNIPtsgaeiggaFGGEKHTGGGRESG 204
Cdd:cd07134 395 vlhfLNPNLP---------FGGVNNSGIGSYHG 418
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
2-158 |
7.20e-15 |
|
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: 72.94 E-value: 7.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWD-PDtlYGPL----HTKEAVKMF 76
Cdd:cd07087 217 KDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKEsPD--YGRIinerHFDRLASLL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 77 ldavdqakqQGGSVVYGGKViNRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFT 156
Cdd:cd07087 295 ---------DDGKVVIGGQV-DKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFS 364
|
..
gi 701367271 157 KD 158
Cdd:cd07087 365 ED 366
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
3-200 |
7.36e-15 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 73.14 E-value: 7.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 3 DADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVrIGDpwDPDT------LYGPLHTKEAVKMF 76
Cdd:PTZ00381 227 SCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEF-FGE--DPKKsedysrIVNEFHTKRLAELI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 77 ldavdqaKQQGGSVVYGGKViNRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFT 156
Cdd:PTZ00381 304 -------KDHGGKVVYGGEV-DIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFG 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 701367271 157 KDlGRIFRWLGPKGSDCGIV---------NVNIPtsgaeiggaFGGEKHTGGG 200
Cdd:PTZ00381 376 ED-KRHKELVLENTSSGAVVindcvfhllNPNLP---------FGGVGNSGMG 418
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
2-158 |
3.95e-14 |
|
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: 70.61 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLaKAYAQVRIGDpwdpdtlyGPLHTKEAVKM------ 75
Cdd:cd07136 217 EDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKEL-KEEIKKFYGE--------DPLESPDYGRIinekhf 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 76 -----FLDavdqakqqGGSVVYGGKvINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGL 150
Cdd:cd07136 288 drlagLLD--------NGKIVFGGN-TDRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPL 358
|
....*...
gi 701367271 151 SSSIFTKD 158
Cdd:cd07136 359 ALYLFSED 366
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
21-214 |
6.57e-14 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 70.66 E-value: 6.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 21 AGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVDQAKQQGGSVvyggKVINRP 100
Cdd:PRK11905 818 AGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLP 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 101 -----GNYVEPTI--VTGLPHnapiVHTETFAPILYVLKFEEEE--EVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGS 171
Cdd:PRK11905 894 aetekGTFVAPTLieIDSISD----LEREVFGPVLHVVRFKADEldRVIDDINATGYGLTFGLHSRIDETIAHVT--SRI 967
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 701367271 172 DCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSdswKLYMRR 214
Cdd:PRK11905 968 RAGNIYVNRNIIGAVVGvQPFGGEGLSGTGPKAGG---PLYLGR 1008
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
9-137 |
2.45e-13 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 68.81 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 9 VIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVDQAKQQgG 88
Cdd:COG4230 810 VVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAE-G 888
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 701367271 89 SVVYGGKVINRP--GNYVEPTIVTgLPHNAPIvHTETFAPILYVLKFEEEE 137
Cdd:COG4230 889 RLVHQLPLPEECanGTFVAPTLIE-IDSISDL-EREVFGPVLHVVRYKADE 937
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
9-137 |
2.97e-13 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 68.69 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 9 VIPSAlFaavGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVDQAKQQgg 88
Cdd:PRK11904 818 VVTSA-F---RSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-- 891
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 701367271 89 svvygGKVINRP--------GNYVEPTIVTgLPhNAPIVHTETFAPILYVLKFEEEE 137
Cdd:PRK11904 892 -----ARLLAQLplpagtenGHFVAPTAFE-ID-SISQLEREVFGPILHVIRYKASD 941
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
9-216 |
5.44e-13 |
|
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: 67.63 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 9 VIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVDQAKQQGG 88
Cdd:TIGR01238 290 VVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 89 SV---VYGGKVINRPGNYVEPTIVTGLPHNApiVHTETFAPILYVLKFEEEE--EVFAWNNEVKQGLSSSIFTKDLGRIf 163
Cdd:TIGR01238 370 KIaqlTLDDSRACQHGTFVAPTLFELDDIAE--LSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGVHSRIETTY- 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 701367271 164 RWLgPKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSdswKLYMRRST 216
Cdd:TIGR01238 447 RWI-EKHARVGNCYVNRNQVGAVVGvQPFGGQGLSGTGPKAGG---PHYLYRLT 496
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
21-215 |
1.42e-12 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 66.27 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 21 AGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAVKMFLDAVDQAKQQgGSVVYGGKV---I 97
Cdd:PRK11903 292 SGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQ-AEVLFDGGGfalV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 98 NRP---GNYVEPTI-VTGLPHNAPIVH-TETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKD---LGRIFRWLGPK 169
Cdd:PRK11903 371 DADpavAACVGPTLlGASDPDAATAVHdVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDaafLAAAALELADS 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 701367271 170 GsdcGIVNVNIPTSGAEIGG--------AFGGEKHTGGGRE-SGSDSWKLYMRRS 215
Cdd:PRK11903 451 H---GRVHVISPDVAALHTGhgnvmpqsLHGGPGRAGGGEElGGLRALAFYHRRS 502
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
3-226 |
1.94e-12 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 65.92 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 3 DADLNLVIPSALFAAVGTAGQRCTTARRLFL---HKSIHDEVVAKlAKAYaQVRIGDpwDPDTLYGPLHTKEAVKMFLDA 79
Cdd:PLN02419 369 DANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLVER-AKAL-KVTCGS--EPDADLGPVISKQAKERICRL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 80 VDQAKQQGGSVVYGGKVINRPG----NYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIF 155
Cdd:PLN02419 445 IQSGVDDGAKLLLDGRDIVVPGyekgNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIF 524
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701367271 156 TKD--LGRIFRwlgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES--GSDSWKLYMRRSTCTINYsKDLP 226
Cdd:PLN02419 525 TSSgaAARKFQ----MDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNfyGKAGVDFFTQIKLVTQKQ-KDIH 594
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
21-158 |
9.91e-08 |
|
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: 51.84 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 21 AGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWD-PDtlYGPL----HTKEAVKmFLDavdqakqqGGSVVYGGK 95
Cdd:cd07132 236 AGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKEsPD--YGRIindrHFQRLKK-LLS--------GGKVAIGGQ 304
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701367271 96 ViNRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKD 158
Cdd:cd07132 305 T-DEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN 366
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
9-214 |
6.33e-06 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 46.51 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 9 VIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDTLYGPLHTKEAvKMFLDAVDQAKQQGG 88
Cdd:PRK11809 901 VVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEA-KANIERHIQAMRAKG 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 89 SVVY----GGKVINRPGNYVEPTIVTgLPHNAPIvHTETFAPILYVLKFEEEE--EVFAWNNEVKQGLSSSIFTK----- 157
Cdd:PRK11809 980 RPVFqaarENSEDWQSGTFVPPTLIE-LDSFDEL-KREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTRideti 1057
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701367271 158 -------DLGRIFrwlgpkgsdcgiVNVNIptSGAEIG-GAFGGEKHTGGGRESGSdswKLYMRR 214
Cdd:PRK11809 1058 aqvtgsaHVGNLY------------VNRNM--VGAVVGvQPFGGEGLSGTGPKAGG---PLYLYR 1105
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
89-208 |
1.71e-05 |
|
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: 45.09 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 89 SVVYGGKvINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFT--KDLGRIFRWL 166
Cdd:cd07137 304 KIVHGGE-RDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTknKELKRRIVAE 382
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 701367271 167 GPKGS----DCgIVNVNIPTSgaeiggAFGGEKHTGGGRESGSDSW 208
Cdd:cd07137 383 TSSGGvtfnDT-VVQYAIDTL------PFGGVGESGFGAYHGKFSF 421
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
17-138 |
2.33e-05 |
|
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: 44.79 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 17 AVGTAGQRCTTARRLFLHKS-IHDEVVAKLAKAYAQVRIgdpwdPDTLYGPLHTKEAVKMfLDAVDQAKQ-QGGSVVYGG 94
Cdd:cd07126 274 AYACSGQKCSAQSILFAHENwVQAGILDKLKALAEQRKL-----EDLTIGPVLTWTTERI-LDHVDKLLAiPGAKVLFGG 347
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 701367271 95 KVI---NRPGNY--VEPTIV------TGLPHNAPIVHTETFAPILYVLKFEEEEE 138
Cdd:cd07126 348 KPLtnhSIPSIYgaYEPTAVfvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQL 402
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
21-215 |
3.39e-05 |
|
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: 44.15 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 21 AGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIgdpwDPDTLYGPLHTKEAVKMfldaVDQAKQQGGSVV-YGGKV--- 96
Cdd:cd07084 238 SGQKCTAQSMLFVPENWSKTPLVEKLKALLARRK----LEDLLLGPVQTFTTLAM----IAHMENLLGSVLlFSGKElkn 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 97 INRPGNY----VEPTIVTGLPHNA--PIVHTETFAPILYVLKFEEEEEVFAWN-NEVKQG-LSSSIFTKD---LGRifrw 165
Cdd:cd07084 310 HSIPSIYgacvASALFVPIDEILKtyELVTEEIFGPFAIVVEYKKDQLALVLElLERMHGsLTAAIYSNDpifLQE---- 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 701367271 166 LGPKGSDCGIVNVNIPTSgaeiGGAFGGEKHTGGGRES-------GSDSWKLYMRRS 215
Cdd:cd07084 386 LIGNLWVAGRTYAILRGR----TGVAPNQNHGGGPAADprgagigGPEAIKLVWRCH 438
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
89-215 |
7.87e-05 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 43.18 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 89 SVVYGGKvINRPGNYVEPTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGP 168
Cdd:PLN02203 314 SIVHGGS-IDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSE 392
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 701367271 169 KGSDCGIVNVNIPTSGAEiGGAFGGEKHTGGGRESGSDSWKLY------MRRS 215
Cdd:PLN02203 393 TSSGSVTFNDAIIQYACD-SLPFGGVGESGFGRYHGKYSFDTFshekavLRRS 444
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
2-141 |
4.48e-04 |
|
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: 40.55 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701367271 2 EDADLNLVIPSALFAAVGTAGQRCTTARRLFLHKSIHDEVVAKLAKAYAQVRIGDPWDPDtlYGPLHTKEAVKMFLDAVD 81
Cdd:cd07133 218 PDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNPD--YTSIINERHYARLQGLLE 295
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701367271 82 QAKQQGGSVVYggkvINRPGNYVE------PTIVTGLPHNAPIVHTETFAPILYVLKFEEEEEVFA 141
Cdd:cd07133 296 DARAKGARVIE----LNPAGEDFAatrklpPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAID 357
|
|
| |
