|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
35-361 |
0e+00 |
|
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: 658.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 35 GNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLDTYR 114
Cdd:cd07123 197 GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYR 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 115 TFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPvEDFST 194
Cdd:cd07123 277 TYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDP-DDFSN 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 195 FFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYPEKHYKEV 274
Cdd:cd07123 356 FMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEET 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 275 LQLIDNTSPYALTGAVFAQDKEVIAEAAEALRNAAGNYYVNDKSTGSVVAQQPFGGARASGTNDKPGGPHYVLRWTSPQV 354
Cdd:cd07123 436 LELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRT 515
|
....*..
gi 2108526399 355 VKQTHVP 361
Cdd:cd07123 516 IKETFVP 522
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
34-370 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 583.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 34 VGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLDTY 113
Cdd:TIGR01236 195 MGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRY 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 114 RTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPvEDFS 193
Cdd:TIGR01236 275 HNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDP-DDFR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 194 TFFSAVIDEKSFVRIKTWLDRAKSS-SNLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYPEKHYK 272
Cdd:TIGR01236 354 GFMGAVIDEQSFDKIVKYIEDAKKDpEALTILYGGKYDDSQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYK 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 273 EVLQLIDNTSPYALTGAVFAQDKEVIAEAAEALRNAAGNYYVNDKSTGSVVAQQPFGGARASGTNDKPGGPHYVLRWTSP 352
Cdd:TIGR01236 434 EILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYINDKCTGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSP 513
|
330
....*....|....*...
gi 2108526399 353 QVVKQTHVPLTDWKYPYM 370
Cdd:TIGR01236 514 RSIKETFVPLTDWSYPYM 531
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
32-359 |
4.99e-160 |
|
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: 458.20 E-value: 4.99e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLD 111
Cdd:cd07083 179 VAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAP 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 TYRTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:cd07083 259 GQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEN 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fSTFFSAVIDEKSFVRIKTWLDRAKSSsnLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYPEKHY 271
Cdd:cd07083 339 -GTDLGPVIDAEQEAKVLSYIEHGKNE--GQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDF 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 272 KEVLQLIDNTSPYALTGAVFAQdKEVIAEAAEALrnAAGNYYVNDKSTGSVVAQQPFGGARASGTNDKPGGPHYVLRWTS 351
Cdd:cd07083 416 AEALEVANSTPYGLTGGVYSRK-REHLEEARREF--HVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRRFLE 492
|
....*...
gi 2108526399 352 PQVVKQTH 359
Cdd:cd07083 493 MKAVAERF 500
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
32-355 |
3.11e-102 |
|
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: 308.37 E-value: 3.11e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLd 111
Cdd:cd07078 121 LAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtfPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVeD 191
Cdd:cd07078 200 -----KRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPL-D 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 FSTFFSAVIDEKSFVRIKTWLDRAKSSSnLNVIAGGNCDD-KTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpeKH 270
Cdd:cd07078 274 PDTDMGPLISAAQLDRVLAYIEDAKAEG-AKLLCGGKRLEgGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPF--KD 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 271 YKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGsVVAQQPFGGARASGTNdKPGGPHYVLRWT 350
Cdd:cd07078 351 EEEAIELA-NDTEYGLAAGVFTRDLERALRVAERLE--AGTVWINDYSVG-AEPSAPFGGVKQSGIG-REGGPYGLEEYT 425
|
....*
gi 2108526399 351 SPQVV 355
Cdd:cd07078 426 EPKTV 430
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
32-359 |
3.59e-102 |
|
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: 309.75 E-value: 3.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLd 111
Cdd:COG1012 166 LAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtfPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPvED 191
Cdd:COG1012 245 -----KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDP-LD 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 FSTFFSAVIDEKSFVRIKTWLDRAKsSSNLNVIAGGNC-DDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpeKH 270
Cdd:COG1012 319 PGTDMGPLISEAQLERVLAYIEDAV-AEGAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPF--DD 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 271 YKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGsVVAQQPFGGARASGTNDKpGGPHYVLRWT 350
Cdd:COG1012 396 EEEAIALA-NDTEYGLAASVFTRDLARARRVARRLE--AGMVWINDGTTG-AVPQAPFGGVKQSGIGRE-GGREGLEEYT 470
|
....*....
gi 2108526399 351 SPQVVKQTH 359
Cdd:COG1012 471 ETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
32-355 |
8.08e-93 |
|
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: 285.19 E-value: 8.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSAsYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:pfam00171 151 LAAGNTVVLKPSElTPLTA-LLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 dtyrtfPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPvE 190
Cdd:pfam00171 230 ------KRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDP-L 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DFSTFFSAVIDEKSFVRIKTWLDRAKsSSNLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpeKH 270
Cdd:pfam00171 303 DPDTDMGPLISKAQLERVLKYVEDAK-EEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRF--KD 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 271 YKEVLQlIDNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAqQPFGGARASGTNDKpGGPHYVLRWT 350
Cdd:pfam00171 380 EEEAIE-IANDTEYGLAAGVFTSDLERALRVARRLE--AGMVWINDYTTGDADG-LPFGGFKQSGFGRE-GGPYGLEEYT 454
|
....*
gi 2108526399 351 SPQVV 355
Cdd:pfam00171 455 EVKTV 459
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
32-355 |
1.68e-90 |
|
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: 281.03 E-value: 1.68e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLD 111
Cdd:cd07124 191 LVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQP 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 TYRTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPvED 191
Cdd:cd07124 271 GQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDP-ED 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 FSTFFSAVIDEKSFVRIKTWLDRAKSSSNLnvIAGGNCDDKT--GYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpeK 269
Cdd:cd07124 350 PEVYMGPVIDKGARDRIRRYIEIGKSEGRL--LLGGEVLELAaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKA--K 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 270 HYKEVLQlIDNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAQQPFGGARASGTNDKPGGPHYVLRW 349
Cdd:cd07124 426 DFDEALE-IANDTEYGLTGGVFSRSPEHLERARREFE--VGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQF 502
|
....*.
gi 2108526399 350 TSPQVV 355
Cdd:cd07124 503 MQPKTV 508
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
32-358 |
3.77e-84 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 264.49 E-value: 3.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLD 111
Cdd:PRK03137 196 IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQP 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 TYRTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:PRK03137 276 GQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fsTFFSAVIDEKSFVRIKTWLDRAKSSSNLnvIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAvyVYPEKHY 271
Cdd:PRK03137 356 --AYMGPVINQASFDKIMSYIEIGKEEGRL--VLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVA--FIKAKDF 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 272 KEVLQlIDNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAQQPFGGARASGTNDKPGGPHYVLRWTS 351
Cdd:PRK03137 430 DHALE-IANNTEYGLTGAVISNNREHLEKARREFH--VGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQ 506
|
....*..
gi 2108526399 352 PQVVKQT 358
Cdd:PRK03137 507 AKTVSEM 513
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
32-357 |
8.21e-74 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 237.84 E-value: 8.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLD 111
Cdd:TIGR01237 192 IVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQP 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 TYRTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPvED 191
Cdd:TIGR01237 272 GQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPP-DS 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 FSTFFSAVIDEKSFVRIKTWLDRAKSSSNLnvIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAvyVYPEKHY 271
Cdd:TIGR01237 351 ADVYVGPVIDQKSFNKIMEYIEIGKAEGRL--VSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVA--FIRASDF 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 272 KEVLQLIDNTSpYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAQQPFGGARASGTNDKPGGPHYVLRWTS 351
Cdd:TIGR01237 427 DEALEIANNTE-YGLTGGVISNNRDHINRAKAEFE--VGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQ 503
|
....*.
gi 2108526399 352 PQVVKQ 357
Cdd:TIGR01237 504 AKTVTE 509
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
32-355 |
2.02e-72 |
|
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: 229.81 E-value: 2.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLd 111
Cdd:cd06534 117 LAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtfPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLdihsnirvgdpved 191
Cdd:cd06534 196 -----KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDEFVEKLV-------------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fstffsavideksfvriktwldraksssnlnviaggncddktgyfvepTIIETTDPQDAIMNEEIFGPVLAVYVYpeKHY 271
Cdd:cd06534 257 ------------------------------------------------TVLVDVDPDMPIAQEEIFGPVLPVIRF--KDE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 272 KEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGsVVAQQPFGGARASGTNDKpGGPHYVLRWTS 351
Cdd:cd06534 287 EEAIALA-NDTEYGLTAGVFTRDLNRALRVAERLR--AGTVYINDSSIG-VGPEAPFGGVKNSGIGRE-GGPYGLEEYTR 361
|
....
gi 2108526399 352 PQVV 355
Cdd:cd06534 362 TKTV 365
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
32-348 |
8.05e-69 |
|
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: 224.77 E-value: 8.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPS-DTAMSASYAVyKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNl 110
Cdd:cd07125 192 LAAGNTVIAKPAeQTPLIAARAV-ELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAER- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 dtYRTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPvE 190
Cdd:cd07125 270 --DGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDP-W 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DFSTFFSAVIDEKSFVRIKTWLDRAKSSSNLnvIAGGNCDDKTGYFVEPTIIEttDPQDAIMNEEIFGPVLAVYVYPEKH 270
Cdd:cd07125 347 DLSTDVGPLIDKPAGKLLRAHTELMRGEAWL--IAPAPLDDGNGYFVAPGIIE--IVGIFDLTTEVFGPILHVIRFKAED 422
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526399 271 YKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAQQPFGGARASGTNDKPGGPHYVLR 348
Cdd:cd07125 423 LDEAIEDI-NATGYGLTLGIHSRDEREIEYWRERVE--AGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLR 497
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
32-355 |
1.00e-57 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 202.35 E-value: 1.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYAVyKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQnl 110
Cdd:PRK11904 709 LAAGNTVIAKPAEqTPLIAAEAV-KLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAA-- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 dtyRTFP--RLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDP 188
Cdd:PRK11904 786 ---RDGPivPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDP 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 189 vEDFSTFFSAVIDEKSFVRIKTWLDRAKSSSNLnvIAGGNCDDKT--GYFVEPTIIETTDPQDaiMNEEIFGPVLAVYVY 266
Cdd:PRK11904 863 -RLLSTDVGPVIDAEAKANLDAHIERMKREARL--LAQLPLPAGTenGHFVAPTAFEIDSISQ--LEREVFGPILHVIRY 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 267 PEKHYKEVLQLIDNTSpYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAQQPFGGARASGTNDKPGGPHYV 346
Cdd:PRK11904 938 KASDLDKVIDAINATG-YGLTLGIHSRIEETADRIADRVR--VGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYL 1014
|
....*....
gi 2108526399 347 LRWTSPQVV 355
Cdd:PRK11904 1015 LRFATEKTV 1023
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
32-355 |
1.30e-54 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 193.62 E-value: 1.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYAVyKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:COG4230 705 LAAGNTVLAKPAEqTPLIAARAV-RLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARD 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DTYrtfPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIK---RGLLDihsNIRVGD 187
Cdd:COG4230 784 GPI---VPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLemlKGAMA---ELRVGD 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 188 PvEDFSTFFSAVIDEKSFVRIKTWLDRAKSSSNL--NVIAGGNCDDktGYFVEPTIIETTDPQDaiMNEEIFGPVLAVYV 265
Cdd:COG4230 858 P-ADLSTDVGPVIDAEARANLEAHIERMRAEGRLvhQLPLPEECAN--GTFVAPTLIEIDSISD--LEREVFGPVLHVVR 932
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 266 YPEKHYKEVLQLIDNTSpYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAQQPFGGARASGTNDKPGGPHY 345
Cdd:COG4230 933 YKADELDKVIDAINATG-YGLTLGVHSRIDETIDRVAARAR--VGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHY 1009
|
330
....*....|
gi 2108526399 346 VLRWTSPQVV 355
Cdd:COG4230 1010 LLRFATERTV 1019
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
32-344 |
4.72e-53 |
|
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: 182.45 E-value: 4.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNld 111
Cdd:cd07097 160 LAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR-- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:cd07097 238 ----GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fSTFFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGNCDDKT-GYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpeKH 270
Cdd:cd07097 314 -GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRV--RD 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526399 271 YKEVLQlIDNTSPYALTGAVFAQDkevIAEAAEALRNA-AGNYYVNDKSTGsVVAQQPFGGARASGTNDKPGGPH 344
Cdd:cd07097 391 YDEALA-IANDTEFGLSAGIVTTS---LKHATHFKRRVeAGVVMVNLPTAG-VDYHVPFGGRKGSSYGPREQGEA 460
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
32-363 |
1.30e-52 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 187.76 E-value: 1.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYAVyKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:PRK11905 701 LVAGNTVLAKPAEqTPLIAARAV-RLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRS 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DtyRTFPrLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDglwpqikrgllDIHSNI------- 183
Cdd:PRK11905 780 G--PPVP-LIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQE-----------DVADRVltmlkga 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 184 ----RVGDPvEDFSTFFSAVIDEKSFVRIKTWLDRAKSSSNL--NVIAGGNCDDktGYFVEPTIIETTDPQDaiMNEEIF 257
Cdd:PRK11905 846 mdelRIGDP-WRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLvhQLPLPAETEK--GTFVAPTLIEIDSISD--LEREVF 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 258 GPVLAVYVYpekHYKEVLQLID--NTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAQQPFGGARASG 335
Cdd:PRK11905 921 GPVLHVVRF---KADELDRVIDdiNATGYGLTFGLHSRIDETIAHVTSRIR--AGNIYVNRNIIGAVVGVQPFGGEGLSG 995
|
330 340 350
....*....|....*....|....*....|....
gi 2108526399 336 TNDKPGGPHYVLR------WTSPQVVKQTHVPLT 363
Cdd:PRK11905 996 TGPKAGGPLYLGRlvreapTPIPPAHESVDTDAA 1029
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
32-353 |
3.64e-52 |
|
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: 180.49 E-value: 3.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYAVyKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:TIGR01238 185 LAAGNTVIAKPAEqTSLIAYRAV-ELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DTYRTFprlTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSA----CSRMYVPDGLWPQIKRGLldihSNIRVG 186
Cdd:TIGR01238 264 DAPVPL---IAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSAlrvlCVQEDVADRVLTMIQGAM----QELKVG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 187 DPVEdFSTFFSAVIDEKSFVRIKTWLD--RAKSSSNLNVIAGGNCDDKTGYFVEPTIIETTDPQDaiMNEEIFGPVLAVY 264
Cdd:TIGR01238 337 VPHL-LTTDVGPVIDAEAKQNLLAHIEhmSQTQKKIAQLTLDDSRACQHGTFVAPTLFELDDIAE--LSEEVFGPVLHVV 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 265 VYpekHYKEVLQLID--NTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAQQPFGGARASGTNDKPGG 342
Cdd:TIGR01238 414 RY---KARELDQIVDqiNQTGYGLTMGVHSRIETTYRWIEKHAR--VGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGG 488
|
330
....*....|.
gi 2108526399 343 PHYVLRWTSPQ 353
Cdd:TIGR01238 489 PHYLYRLTQVQ 499
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
32-355 |
8.08e-51 |
|
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: 176.48 E-value: 8.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVfGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLD 111
Cdd:cd07113 167 LATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQAASDLT 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:cd07113 246 ------RVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fSTFFSAVIDEKSFVRIKTWLDRAKSSSNlNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYPEKhy 271
Cdd:cd07113 320 -SVMFGPLANQPHFDKVCSYLDDARAEGD-EIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDE-- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 272 KEVLQLIdNTSPYALTGAVFAQDkeviaeAAEALRNA----AGNYYVNDKSTgsVVAQQPFGGARASGTNdKPGGPHYVL 347
Cdd:cd07113 396 EELIQLI-NDTPFGLTASVWTNN------LSKALRYIprieAGTVWVNMHTF--LDPAVPFGGMKQSGIG-REFGSAFID 465
|
....*...
gi 2108526399 348 RWTSPQVV 355
Cdd:cd07113 466 DYTELKSV 473
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
32-348 |
8.51e-51 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 182.48 E-value: 8.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYAVyKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:PRK11809 793 LAAGNSVLAKPAEqTPLIAAQAV-RILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRL 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DTY-RTFPrLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSA----CSRMYVPDGLWPQIKRGLldihSNIRV 185
Cdd:PRK11809 872 DPQgRPIP-LIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSAlrvlCLQDDVADRTLKMLRGAM----AECRM 946
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 186 GDPvEDFSTFFSAVIDEKSFVRIKTWLD--RAKSSSNLNVIAGGNCDDKTGYFVEPTIIETTDPQDaiMNEEIFGPVLAV 263
Cdd:PRK11809 947 GNP-DRLSTDIGPVIDAEAKANIERHIQamRAKGRPVFQAARENSEDWQSGTFVPPTLIELDSFDE--LKREVFGPVLHV 1023
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 264 YVYPEKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEalRNAAGNYYVNDKSTGSVVAQQPFGGARASGTNDKPGGP 343
Cdd:PRK11809 1024 VRYNRNQLDELIEQI-NASGYGLTLGVHTRIDETIAQVTG--SAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGP 1100
|
....*
gi 2108526399 344 HYVLR 348
Cdd:PRK11809 1101 LYLYR 1105
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
32-335 |
1.83e-50 |
|
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: 175.44 E-value: 1.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYK----VLRECGLPPNIIQFLPADGPVfGDAVTSSEHLAGINFTGSVPTFKRLWKQVA 107
Cdd:cd07086 158 LVCGNTVVWKPSETTPLTAIAVTKilaeVLEKNGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 108 qnldtyRTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGD 187
Cdd:cd07086 237 ------RRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGD 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 188 PVEDfSTFFSAVIDEKSFVRIKTWLDRAKsSSNLNVIAGGNC--DDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLavYV 265
Cdd:cd07086 311 PLDE-GTLVGPLINQAAVEKYLNAIEIAK-SQGGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPIL--YV 386
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2108526399 266 YPEKHYKEVLQlIDNTSPYALTGAVFAQDkevIAEAAEALRNA---AGNYYVNDKSTGSVVaQQPFGGARASG 335
Cdd:cd07086 387 IKFDSLEEAIA-INNDVPQGLSSSIFTED---LREAFRWLGPKgsdCGIVNVNIPTSGAEI-GGAFGGEKETG 454
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
32-355 |
2.14e-49 |
|
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: 172.01 E-value: 2.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSAsYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAqnl 110
Cdd:cd07149 148 IAAGNAVVLKPASqTPLSA-LKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 dtyrtFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVE 190
Cdd:cd07149 224 -----LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLD 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DfSTFFSAVIDEKSFVRIKTWLDRAKSSSNlNVIAGGNCDdktGYFVEPTIIETTDPQDAIMNEEIFGPVlaVYVYPEKH 270
Cdd:cd07149 299 E-DTDVGPMISEAEAERIEEWVEEAVEGGA-RLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPV--VSLNPFDT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 271 YKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSvVAQQPFGGARASGTNDKpgGPHYVLR-W 349
Cdd:cd07149 372 LDEAIAMA-NDSPYGLQAGVFTNDLQKALKAARELE--VGGVMINDSSTFR-VDHMPYGGVKESGTGRE--GPRYAIEeM 445
|
....*.
gi 2108526399 350 TSPQVV 355
Cdd:cd07149 446 TEIKLV 451
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
32-351 |
2.48e-48 |
|
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: 169.84 E-value: 2.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAqnld 111
Cdd:cd07131 160 LVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA---- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyRTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:cd07131 236 --RPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fSTFFSAVIDEKSFVRIKTWLDRAKS-----SSNLNVIAGGNCDDktGYFVEPTIIETTDPQDAIMNEEIFGPVLAvyVY 266
Cdd:cd07131 314 -ETDMGPLINEAQLEKVLNYNEIGKEegatlLLGGERLTGGGYEK--GYFVEPTVFTDVTPDMRIAQEEIFGPVVA--LI 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 267 PEKHYKEVLQlIDNTSPYALTGAVFAQDkevIAEAAEALRNA-AGNYYVNDKSTGSVVaQQPFGGARASGTNDKPGGP-- 343
Cdd:cd07131 389 EVSSLEEAIE-IANDTEYGLSSAIYTED---VNKAFRARRDLeAGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGTta 463
|
....*....
gi 2108526399 344 -HYVLRWTS 351
Cdd:cd07131 464 lDAFTEWKA 472
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
32-335 |
2.80e-48 |
|
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: 169.27 E-value: 2.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNld 111
Cdd:cd07114 144 LAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN-- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPvED 191
Cdd:cd07114 222 ----LAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDP-LD 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 FSTFFSAVIDEKSFVRIKTWLDRAKsSSNLNVIAGGN----CDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAvyVYP 267
Cdd:cd07114 297 PETQMGPLATERQLEKVERYVARAR-EEGARVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLS--VIP 373
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2108526399 268 EKHYKEVLQlIDNTSPYALTGAVFAQDkevIAEA---AEALRnaAGNYYVNDKSTGSVVAqqPFGGARASG 335
Cdd:cd07114 374 FDDEEEAIA-LANDSEYGLAAGIWTRD---LARAhrvARAIE--AGTVWVNTYRALSPSS--PFGGFKDSG 436
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
32-336 |
1.95e-47 |
|
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: 166.97 E-value: 1.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYAVyKVLRECGLPP---NIIQflpADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVA 107
Cdd:cd07093 142 LAFGNTVVLKPSEwTPLTAWLLA-ELANEAGLPPgvvNVVH---GFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 108 QNLDtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGD 187
Cdd:cd07093 218 PNLK------PVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGD 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 188 PvEDFSTFFSAVIDEKSFVRIKTWLDRAKSSsNLNVIAGGNCDD----KTGYFVEPTIIETTDPQDAIMNEEIFGPVLAv 263
Cdd:cd07093 292 P-LDPDTEVGPLISKEHLEKVLGYVELARAE-GATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVT- 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526399 264 yVYPEKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVN-----DKSTgsvvaqqPFGGARASGT 336
Cdd:cd07093 369 -VIPFDDEEEAIELA-NDTPYGLAAYVWTRDLGRAHRVARRLE--AGTVWVNcwlvrDLRT-------PFGGVKASGI 435
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
32-335 |
7.04e-47 |
|
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: 165.30 E-value: 7.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPS-DTAMSAsYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:cd07103 142 LAAGCTVVLKPAeETPLSA-LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVE 190
Cdd:cd07103 221 K------RVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLD 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DfSTFFSAVIDEKSFVRIKTWLDRAKSSSnLNVIAGGNCDDKTGYFVEPTIIetTD-PQDA-IMNEEIFGPVLAVYVYPE 268
Cdd:cd07103 295 E-GTDMGPLINERAVEKVEALVEDAVAKG-AKVLTGGKRLGLGGYFYEPTVL--TDvTDDMlIMNEETFGPVAPIIPFDT 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108526399 269 khYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDksTGSVVAQQPFGGARASG 335
Cdd:cd07103 371 --EDEVIARA-NDTPYGLAAYVFTRDLARAWRVAEALE--AGMVGINT--GLISDAEAPFGGVKESG 430
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
32-335 |
1.33e-46 |
|
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: 164.91 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAqnld 111
Cdd:cd07094 148 IATGCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:cd07094 224 ----GKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fSTFFSAVIDEKSFVRIKTWLDRA-KSSSNLnvIAGGNCDDKTgyfVEPTIIEtTDPQDAIM-NEEIFGPVLAVYVYpeK 269
Cdd:cd07094 300 -DTDVGPLISEEAAERVERWVEEAvEAGARL--LCGGERDGAL---FKPTVLE-DVPRDTKLsTEETFGPVVPIIRY--D 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526399 270 HYKEVLQLIDNTsPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDkSTGSVVAQQPFGGARASG 335
Cdd:cd07094 371 DFEEAIRIANST-DYGLQAGIFTRDLNVAFKAAEKLE--VGGVMVND-SSAFRTDWMPFGGVKESG 432
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
32-335 |
1.96e-46 |
|
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: 164.15 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLD 111
Cdd:cd07115 142 LAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVeD 191
Cdd:cd07115 222 ------RVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPL-D 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 FSTFFSAVIDEKSFVRIKTWLDRAKSSSNlNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpeKHY 271
Cdd:cd07115 295 PKTQMGPLVSQAQFDRVLDYVDVGREEGA-RLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRF--RDE 371
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108526399 272 KEVLQlIDNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNdkSTGSVVAQQPFGGARASG 335
Cdd:cd07115 372 EEALR-IANGTEYGLAAGVWTRDLGRAHRVAAALK--AGTVWIN--TYNRFDPGSPFGGYKQSG 430
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
32-335 |
2.43e-45 |
|
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: 161.52 E-value: 2.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSAsYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVptfkRLWKQVAQNl 110
Cdd:cd07138 155 LAAGCTVVLKPSEvAPLSA-IILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGST----RAGKRVAEA- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 dTYRTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPvE 190
Cdd:cd07138 229 -AADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDP-R 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DFSTFFSAVIDEKSFVRIKTWLDR-----AKsssnlnVIAGG-----NCDdkTGYFVEPTIIETTDPQDAIMNEEIFGPV 260
Cdd:cd07138 307 DPATTLGPLASAAQFDRVQGYIQKgieegAR------LVAGGpgrpeGLE--RGYFVKPTVFADVTPDMTIAREEIFGPV 378
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526399 261 LAVYVYpeKHYKEVLQlIDNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDkstGSVVAQQPFGGARASG 335
Cdd:cd07138 379 LSIIPY--DDEDEAIA-IANDTPYGLAGYVWSADPERARAVARRLR--AGQVHING---AAFNPGAPFGGYKQSG 445
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
32-336 |
2.76e-45 |
|
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: 161.39 E-value: 2.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECgLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQnld 111
Cdd:cd07107 141 LAAGNTVVVKPPEQAPLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAE--- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSA-FEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVE 190
Cdd:cd07107 217 ---GIKHVTLELGGKNALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTD 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DfSTFFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGNCDDKT---GYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYP 267
Cdd:cd07107 294 P-ATTMGPLVSRQQYDRVMHYIDSAKREGARLVTGGGRPEGPAlegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWR 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 268 EKhyKEVLQLIdNTSPYALTGAVFAQDkevIAEAAE-ALRNAAGNYYVNDKSTGSVVAqqPFGGARASGT 336
Cdd:cd07107 373 DE--AEMVAQA-NGVEYGLTAAIWTND---ISQAHRtARRVEAGYVWINGSSRHFLGA--PFGGVKNSGI 434
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
32-335 |
6.98e-45 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 160.77 E-value: 6.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYAVyKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNl 110
Cdd:cd07143 169 LAAGNTIVLKPSElTPLSALYMT-KLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 dtyrTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVE 190
Cdd:cd07143 247 ----NLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DfSTFFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGNCDDKtGYFVEPTIIETTDPQDAIMNEEIFGPVLAvyVYPEKH 270
Cdd:cd07143 323 E-DTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNE-GYFIEPTIFTDVTEDMKIVKEEIFGPVVA--VIKFKT 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526399 271 YKEVLQlIDNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTgsVVAQQPFGGARASG 335
Cdd:cd07143 399 EEEAIK-RANDSTYGLAAAVFTNNINNAIRVANALK--AGTVWVNCYNL--LHHQVPFGGYKQSG 458
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
24-351 |
7.39e-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: 160.19 E-value: 7.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 24 SWEQYTLHLAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLW 103
Cdd:cd07150 136 ATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 104 KQVAQNLDTYrtfprlTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNI 183
Cdd:cd07150 216 EKAGRHLKKI------TLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 184 RVGDPvEDFSTFFSAVIDEKSFVRIKTWLDRAKSSSNlNVIAGGNCDdktGYFVEPTIIETTDPQDAIMNEEIFGPVlaV 263
Cdd:cd07150 290 KVGDP-RDPDTVIGPLISPRQVERIKRQVEDAVAKGA-KLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPV--T 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 264 YVYPEKHYKEVLQLiDNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDkSTGSVVAQQPFGGARASGTNdKPGGP 343
Cdd:cd07150 363 SVIPAKDAEEALEL-ANDTEYGLSAAILTNDLQRAFKLAERLE--SGMVHIND-PTILDEAHVPFGGVKASGFG-REGGE 437
|
330
....*....|...
gi 2108526399 344 HYV-----LRWTS 351
Cdd:cd07150 438 WSMeefteLKWIT 450
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
32-355 |
1.37e-44 |
|
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: 1.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECgLPPNIIQFLPADGPVfGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLD 111
Cdd:cd07106 139 LLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKTLK 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:cd07106 217 ------RVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDP 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fSTFFSAVIDEKSFVRIKTWLDRAKSSsNLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYPEKHy 271
Cdd:cd07106 291 -GTTLGPVQNKMQYDKVKELVEDAKAK-GAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDED- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 272 kEVLQLIdNTSPYALTGAVFAQDkeviAEAAEAL--RNAAGNYYVNdkSTGSVVAQQPFGGARASGTndkpG---GPHYV 346
Cdd:cd07106 368 -EVIARA-NDSEYGLGASVWSSD----LERAEAVarRLEAGTVWIN--THGALDPDAPFGGHKQSGI----GvefGIEGL 435
|
....*....
gi 2108526399 347 LRWTSPQVV 355
Cdd:cd07106 436 KEYTQTQVI 444
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
32-336 |
2.83e-44 |
|
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: 158.67 E-value: 2.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAqnld 111
Cdd:cd07145 148 IAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG---- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyRTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:cd07145 224 --GTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fSTFFSAVIDEKSFVRIKTWLDRAKSSSNlNVIAGGNCDDktGYFVEPTIIETTDPQDAIMNEEIFGPVLAvyVYPEKHY 271
Cdd:cd07145 302 -STDLGPLISPEAVERMENLVNDAVEKGG-KILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLP--IAKVKDD 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526399 272 KEVLQlIDNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKST---GSVvaqqPFGGARASGT 336
Cdd:cd07145 376 EEAVE-IANSTEYGLQASVFTNDINRALKVARELE--AGGVVINDSTRfrwDNL----PFGGFKKSGI 436
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
32-335 |
7.25e-44 |
|
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: 157.76 E-value: 7.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPS-DTAMSAsYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQ-N 109
Cdd:cd07112 149 LAAGNSVVLKPAeQSPLTA-LRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsN 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 110 LDtyrtfpRLTGECGGKNFYFV-HKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDP 188
Cdd:cd07112 228 LK------RVWLECGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDP 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 189 VeDFSTFFSAVIDEKSFVRIKTWLDRAKSSsNLNVIAGGNCD--DKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAvyVY 266
Cdd:cd07112 302 L-DPATRMGALVSEAHFDKVLGYIESGKAE-GARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLS--VI 377
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526399 267 PEKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVvaQQPFGGARASG 335
Cdd:cd07112 378 TFDSEEEAVALA-NDSVYGLAASVWTSDLSRAHRVARRLR--AGTVWVNCFDEGDI--TTPFGGFKQSG 441
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
32-335 |
8.39e-44 |
|
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: 157.40 E-value: 8.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPS-DTAMSAsYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:cd07089 148 LAAGNTVVLKPApDTPLSA-LLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVe 190
Cdd:cd07089 227 K------RVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPA- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DFSTFFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGNCDD-KTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpeK 269
Cdd:cd07089 300 DPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGRPAGlDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPY--D 377
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526399 270 HYKEVLQlIDNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSvvAQQPFGGARASG 335
Cdd:cd07089 378 DDDEAVR-IANDSDYGLSGGVWSADVDRAYRVARRIR--TGSVGINGGGGYG--PDAPFGGYKQSG 438
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
16-355 |
1.10e-43 |
|
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: 157.09 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 16 KQKVFSLSSWeQYTLHLAV---------GNVVLWKP-SDTAMSASYAVyKVLRECGLPPNIIQFLPADGPVFGDAVTssE 85
Cdd:cd07101 119 KGVVGVISPW-NYPLTLAVsdaipallaGNAVVLKPdSQTALTALWAV-ELLIEAGLPRDLWQVVTGPGSEVGGAIV--D 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 86 HLAGINFTGSVPTFKRLWKQVAQnldtyrtfpRLTG---ECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRM 162
Cdd:cd07101 195 NADYVMFTGSTATGRVVAERAGR---------RLIGcslELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 163 YVPDGLWPQIKRGLLDIHSNIRVGdPVEDFSTFFSAVIDEKSFVRIKTWLDRAKSSSnLNVIAGGNCDDKTG-YFVEPTI 241
Cdd:cd07101 266 YVHESVYDEFVRRFVARTRALRLG-AALDYGPDMGSLISQAQLDRVTAHVDDAVAKG-ATVLAGGRARPDLGpYFYEPTV 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 242 IETTDPQDAIMNEEIFGPVlaVYVYPekhYKEVLQLID--NTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVND--- 316
Cdd:cd07101 344 LTGVTEDMELFAEETFGPV--VSIYR---VADDDEAIElaNDTDYGLNASVWTRDGARGRRIAARLR--AGTVNVNEgya 416
|
330 340 350
....*....|....*....|....*....|....*....
gi 2108526399 317 KSTGSVVAqqPFGGARASGTNDKpGGPHYVLRWTSPQVV 355
Cdd:cd07101 417 AAWASIDA--PMGGMKDSGLGRR-HGAEGLLKYTETQTV 452
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
32-355 |
2.86e-43 |
|
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: 156.27 E-value: 2.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLd 111
Cdd:cd07088 158 LVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrTFPRLtgECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:cd07088 237 ---TKVSL--ELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fSTFFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYPEkhY 271
Cdd:cd07088 312 -ATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSS--L 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 272 KEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNdksTGSVVAQQPF-GGARASGTNDKpGGPHYVLRWT 350
Cdd:cd07088 389 DEAIELA-NDSEYGLTSYIYTENLNTAMRATNELE--FGETYIN---RENFEAMQGFhAGWKKSGLGGA-DGKHGLEEYL 461
|
....*
gi 2108526399 351 SPQVV 355
Cdd:cd07088 462 QTKVV 466
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
32-335 |
4.00e-43 |
|
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: 155.93 E-value: 4.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNld 111
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN-- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVeD 191
Cdd:cd07119 237 ----VKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGL-D 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 FSTFFSAVIDEKSFVRIKTWLDRAKSSSnLNVIAGGNCDD----KTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYp 267
Cdd:cd07119 312 ADTEMGPLVSAEHREKVLSYIQLGKEEG-ARLVCGGKRPTgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERF- 389
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526399 268 eKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDksTGSVVAQQPFGGARASG 335
Cdd:cd07119 390 -DTEEEAIRLA-NDTPYGLAGAVWTKDIARANRVARRLR--AGTVWIND--YHPYFAEAPWGGYKQSG 451
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
32-335 |
7.93e-43 |
|
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: 154.83 E-value: 7.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKpsdTAMSASYAVYKVLRECG--LPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQn 109
Cdd:cd07108 142 LVAGNTVVLK---AAEDAPLAVLLLAEILAqvLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 110 ldtyRTFPrLTGECGGKNFYFVHKSADVESVVKGTIRSA-FEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDP 188
Cdd:cd07108 218 ----RLIP-VSLELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDP 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 189 VeDFSTFFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGN----CDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAvy 264
Cdd:cd07108 293 L-DEATDIGAIISEKQFAKVCGYIDLGLSTSGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLC-- 369
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2108526399 265 VYPEKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNdkSTGSVVAQQPFGGARASG 335
Cdd:cd07108 370 AIPWKDEDEVIAMA-NDSHYGLAAYVWTRDLGRALRAAHALE--AGWVQVN--QGGGQQPGQSYGGFKQSG 435
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
32-335 |
1.78e-42 |
|
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: 154.29 E-value: 1.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYaVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQ-N 109
Cdd:cd07091 166 LAAGNTVVLKPAEqTPLSALY-LAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsN 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 110 LDtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPv 189
Cdd:cd07091 245 LK------KVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDP- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 190 EDFSTFFSAVIDEKSFVRIKTWLDRAKSSSnLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpeK 269
Cdd:cd07091 318 FDPDTFQGPQVSKAQFDKILSYIESGKKEG-ATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKF--K 394
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526399 270 HYKEVLQLIDNTSpYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNdkSTGSVVAQQPFGGARASG 335
Cdd:cd07091 395 TEDEVIERANDTE-YGLAAGVFTKDINKALRVSRALK--AGTVWVN--TYNVFDAAVPFGGFKQSG 455
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
32-335 |
1.89e-42 |
|
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: 153.07 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPS-DTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAqnl 110
Cdd:cd07104 123 LALGNAVVLKPDsRTPVTGGLLIAEIFEEAGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAG--- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 dtyRTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVE 190
Cdd:cd07104 200 ---RHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DfSTFFSAVIDEKSFVRIKTWLDRAKSSSnLNVIAGGNCDdktGYFVEPTIIETTDPQDAIMNEEIFGPVlaVYVYPEKH 270
Cdd:cd07104 277 P-DTVIGPLINERQVDRVHAIVEDAVAAG-ARLLTGGTYE---GLFYQPTVLSDVTPDMPIFREEIFGPV--APVIPFDD 349
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526399 271 YKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDkSTGSVVAQQPFGGARASG 335
Cdd:cd07104 350 DEEAVELA-NDTEYGLSAAVFTRDLERAMAFAERLE--TGMVHIND-QTVNDEPHVPFGGVKASG 410
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
32-335 |
3.75e-42 |
|
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: 152.84 E-value: 3.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSAsYAVYKVLRECGLPPNIIQFLPADGPVfGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:cd07090 141 LACGNAMVYKPSPfTPLTA-LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVe 190
Cdd:cd07090 219 K------HVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPL- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DFSTFFSAVIDEKSFVRIKTWLDRAKSSSNlNVIAGGN-----CDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYV 265
Cdd:cd07090 292 DEDTQMGALISEEHLEKVLGYIESAKQEGA-KVLCGGErvvpeDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILP 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 266 YPEKhyKEVLQLIDNTsPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVvaQQPFGGARASG 335
Cdd:cd07090 371 FDTE--EEVIRRANDT-TYGLAAGVFTRDLQRAHRVIAQLQ--AGTCWINTYNISPV--EVPFGGYKQSG 433
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
32-335 |
4.94e-42 |
|
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: 152.39 E-value: 4.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNld 111
Cdd:cd07109 142 LAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEN-- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:cd07109 220 ----VVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLED 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 FStfFSAVIDEKSFVRIKTWLDRAKSSSnLNVIAGG---NCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYPE 268
Cdd:cd07109 296 PD--LGPLISAKQLDRVEGFVARARARG-ARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDD 372
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108526399 269 KhyKEVLQLIDNTSpYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVaQQPFGGARASG 335
Cdd:cd07109 373 E--AEAIALANGTD-YGLVAGVWTRDGDRALRVARRLR--AGQVFVNNYGAGGGI-ELPFGGVKKSG 433
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
32-335 |
2.17e-41 |
|
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: 150.95 E-value: 2.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLD 111
Cdd:cd07118 144 LAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:cd07118 224 ------KVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDP 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fSTFFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpeKHY 271
Cdd:cd07118 298 -ETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTF--DTV 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108526399 272 KEVLQLIDNTsPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSvvAQQPFGGARASG 335
Cdd:cd07118 375 DEAIALANDT-VYGLSAGVWSKDIDTALTVARRIR--AGTVWVNTFLDGS--PELPFGGFKQSG 433
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
23-363 |
2.20e-41 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 151.95 E-value: 2.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 23 SSWeQYTLHLAV---------GNVVLWKP-SDTAMSASYAVyKVLRECGLPPNIIQFLPADGPVFGDAVTssEHLAGINF 92
Cdd:PRK09407 162 SPW-NYPLTLAVsdaipallaGNAVVLKPdSQTPLTALAAV-ELLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMF 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 93 TGSVPTFKRLWKQVAQnldtyrtfpRLTG---ECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLW 169
Cdd:PRK09407 238 TGSTATGRVLAEQAGR---------RLIGfslELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIY 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 170 PQIKRGLLDIHSNIRVGdPVEDFSTFFSAVIDEKSFVRIKTWLD--RAKSSSnlnVIAGGNCDDKTG-YFVEPTIIETTD 246
Cdd:PRK09407 309 DEFVRAFVAAVRAMRLG-AGYDYSADMGSLISEAQLETVSAHVDdaVAKGAT---VLAGGKARPDLGpLFYEPTVLTGVT 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 247 PQDAIMNEEIFGPVlaVYVYPEKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKST---GSVV 323
Cdd:PRK09407 385 PDMELAREETFGPV--VSVYPVADVDEAVERA-NDTPYGLNASVWTGDTARGRAIAARIR--AGTVNVNEGYAaawGSVD 459
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2108526399 324 AqqPFGGARASGTNDKpGGPHYVLRWTSPQ-VVKQTHVPLT 363
Cdd:PRK09407 460 A--PMGGMKDSGLGRR-HGAEGLLKYTESQtIATQRVLPLA 497
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
32-335 |
9.46e-41 |
|
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: 149.48 E-value: 9.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYaVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:cd07144 169 LAAGNTVVIKPAEnTPLSLLY-FANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DTyrtfprLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLD-IHSNIRVGDPV 189
Cdd:cd07144 248 KA------VTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEhVKQNYKVGSPF 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 190 EDfSTFFSAVIDEKSFVRIKTWLDRAKsSSNLNVIAGGN---CDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVY 266
Cdd:cd07144 322 DD-DTVVGPQVSKTQYDRVLSYIEKGK-KEGAKLVYGGEkapEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKF 399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526399 267 peKHYKEVLQLIDNTsPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNdkSTGSVVAQQPFGGARASG 335
Cdd:cd07144 400 --KTYEEAIKKANDT-TYGLAAAVFTKDIRRAHRVARELE--AGMVWIN--SSNDSDVGVPFGGFKMSG 461
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
32-335 |
6.31e-40 |
|
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: 146.73 E-value: 6.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLD 111
Cdd:cd07110 145 LAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:cd07110 225 ------PVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fSTFFSAVIDEKSFVRIKTWLDRAKSSSnLNVIAGGNCDD--KTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYPEK 269
Cdd:cd07110 299 -GVRLGPLVSQAQYEKVLSFIARGKEEG-ARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATE 376
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526399 270 hyKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNdkSTGSVVAQQPFGGARASG 335
Cdd:cd07110 377 --DEAIALA-NDSEYGLAAAVISRDAERCDRVAEALE--AGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
32-355 |
7.59e-40 |
|
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: 146.60 E-value: 7.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYAVyKVLRECGLPPNIIQFLPADGPVfGDAVTSSEHlAGINFTGSVPTFKRLWKQVAQnl 110
Cdd:cd07099 144 LAAGNAVVLKPSEvTPLVGELLA-EAWAAAGPPQGVLQVVTGDGAT-GAALIDAGV-DKVAFTGSVATGRKVMAAAAE-- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 dtyrtfpRLTG---ECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGD 187
Cdd:cd07099 219 -------RLIPvvlELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 188 PvEDFSTFFSAVIDEKSFVRIKTWLDRAKSSSNLnVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYP 267
Cdd:cd07099 292 D-DIGDADIGPMTTARQLDIVRRHVDDAVAKGAK-ALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 268 EKhyKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAQQPFGGARASGTNDKpGGPHYVL 347
Cdd:cd07099 370 DE--DEAIALA-NDSRYGLSASVFSRDLARAEAIARRLE--AGAVSINDVLLTAGIPALPFGGVKDSGGGRR-HGAEGLR 443
|
....*...
gi 2108526399 348 RWTSPQVV 355
Cdd:cd07099 444 EFCRPKAI 451
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
32-336 |
6.86e-39 |
|
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: 144.01 E-value: 6.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLREcGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLD 111
Cdd:cd07092 143 LAAGNTVVLKPSETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPvED 191
Cdd:cd07092 222 ------RVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDP-DD 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 FSTFFSAVIDEKSFVRIKTWLDRAKSssNLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYPEKhy 271
Cdd:cd07092 295 EDTEMGPLNSAAQRERVAGFVERAPA--HARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDE-- 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526399 272 KEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKstGSVVAQQPFGGARASGT 336
Cdd:cd07092 371 DEAIELA-NDVEYGLASSVWTRDVGRAMRLSARLD--FGTVWVNTH--IPLAAEMPHGGFKQSGY 430
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
32-335 |
1.56e-38 |
|
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: 143.15 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSAsYAVYKVLRECGLPPNIIQFLPADGPVfGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNl 110
Cdd:cd07147 148 IAAGCPFVLKPASrTPLSA-LILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKARAGKK- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 dtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVE 190
Cdd:cd07147 225 -------KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKD 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DfSTFFSAVIDEKSFVRIKTWLDRAKSSSNlNVIAGGNCDdktGYFVEPTIIETTDPQDAIMNEEIFGPVlaVYVYPEKH 270
Cdd:cd07147 298 D-ATDVGPMISESEAERVEGWVNEAVDAGA-KLLTGGKRD---GALLEPTILEDVPPDMEVNCEEVFGPV--VTVEPYDD 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526399 271 YKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSvVAQQPFGGARASG 335
Cdd:cd07147 371 FDEALAAV-NDSKFGLQAGVFTRDLEKALRAWDELE--VGGVVINDVPTFR-VDHMPYGGVKDSG 431
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
32-335 |
2.15e-38 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 143.13 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECgLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRlwkqVAQNld 111
Cdd:PRK13473 163 LAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKH----VLSA-- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 TYRTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPvED 191
Cdd:PRK13473 236 AADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDP-DD 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 FSTFFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYPEKhy 271
Cdd:PRK13473 315 EDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE-- 392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526399 272 KEVLQLIdNTSPYALTGAVFAQDkeviaeAAEALRNAA----GNYYVNDKstGSVVAQQPFGGARASG 335
Cdd:PRK13473 393 DQAVRWA-NDSDYGLASSVWTRD------VGRAHRVSArlqyGCTWVNTH--FMLVSEMPHGGQKQSG 451
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
32-335 |
4.94e-38 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 142.56 E-value: 4.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLD 111
Cdd:PLN02467 176 LAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 TyrtfprLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:PLN02467 256 P------VSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fSTFFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGNCDD-KTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYPEKh 270
Cdd:PLN02467 330 -GCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTE- 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526399 271 yKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNdkSTGSVVAQQPFGGARASG 335
Cdd:PLN02467 408 -DEAIELA-NDSHYGLAGAVISNDLERCERVSEAFQ--AGIVWIN--CSQPCFCQAPWGGIKRSG 466
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
32-342 |
5.06e-38 |
|
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: 141.25 E-value: 5.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYAVyKVLRECGLPPNIIQFLPADGPVfGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:cd07095 122 LLAGNTVVFKPSElTPAVAELMV-ELWEEAGLPPGVLNLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRP 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DTYrtfprLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQ--IKRgLLDIHSNIRVGDP 188
Cdd:cd07095 200 GKI-----LALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDGAVGDafLER-LVEAAKRLRIGAP 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 189 VEDfSTFFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGNCDDKTGyFVEPTIIETTDPQDaIMNEEIFGPVLAVYVYpe 268
Cdd:cd07095 274 DAE-PPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTA-FLSPGIIDVTDAAD-VPDEEIFGPLLQVYRY-- 348
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108526399 269 KHYKEVLQLIDNTsPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAqQPFGGARASGtNDKPGG 342
Cdd:cd07095 349 DDFDEAIALANAT-RFGLSAGLLSDDEALFERFLARIR--AGIVNWNRPTTGASST-APFGGVGLSG-NHRPSA 417
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
32-335 |
1.19e-37 |
|
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: 140.79 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPS-DTAMSAsYAVYKVLRECGLPPNIIQFLPADGPVfGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:cd07139 162 LAAGCTVVLKPSpETPLDA-YLLAEAAEEAGLPPGVVNVVPADREV-GEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 dtyrtfPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVE 190
Cdd:cd07139 240 ------ARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLD 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DfSTFFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGNCDD-KTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpek 269
Cdd:cd07139 314 P-ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGlDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPY--- 389
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526399 270 HYKEVLQLIDNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNdksTGSVVAQQPFGGARASG 335
Cdd:cd07139 390 DDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIR--TGTVGVN---GFRLDFGAPFGGFKQSG 450
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
32-336 |
1.61e-37 |
|
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: 140.95 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYaVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTfKRLWKQVA--Q 108
Cdd:cd07141 170 LACGNTVVLKPAEqTPLTALY-LASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV-GKLIQQAAgkS 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 109 NLDtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDP 188
Cdd:cd07141 248 NLK------RVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNP 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 189 VEDfSTFFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGNCDDKtGYFVEPTIIetTDPQD--AIMNEEIFGPVLAVYVY 266
Cdd:cd07141 322 FDP-KTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDK-GYFIQPTVF--SDVTDdmRIAKEEIFGPVQQIFKF 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 267 peKHYKEVLQLIDNTsPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNdkSTGSVVAQQPFGGARASGT 336
Cdd:cd07141 398 --KTIDEVIERANNT-TYGLAAAVFTKDIDKAITFSNALR--AGTVWVN--CYNVVSPQAPFGGYKMSGN 460
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
19-343 |
4.35e-37 |
|
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: 139.36 E-value: 4.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 19 VFSLSSWeQYTLH---------LAVGNVVLWKPSD-TAMSASY---AVYKVLRECGLPPNIIQFLPADGPVfGDAVTSSE 85
Cdd:cd07098 124 VGAIVSW-NYPFHnllgpiiaaLFAGNAIVVKVSEqVAWSSGFflsIIRECLAACGHDPDLVQLVTCLPET-AEALTSHP 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 86 HLAGINFTGSVPTFKRLWKQVAQNLDtyrtfPrLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVP 165
Cdd:cd07098 202 VIDHITFIGSPPVGKKVMAAAAESLT-----P-VVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVH 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 166 DGLWPQIKRGLLDIHSNIRVGdPVEDFSTFFSAVIDEKSFVRIKTWL-DRAKSSSNLnvIAGG----NCDDKTGYFVEPT 240
Cdd:cd07098 276 EKIYDKLLEILTDRVQALRQG-PPLDGDVDVGAMISPARFDRLEELVaDAVEKGARL--LAGGkrypHPEYPQGHYFPPT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 241 IIETTDPQDAIMNEEIFGPVLAVYVYPEKHykEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTG 320
Cdd:cd07098 353 LLVDVTPDMKIAQEEVFGPVMVVMKASDDE--EAVEIA-NSTEYGLGASVFGKDIKRARRIASQLE--TGMVAINDFGVN 427
|
330 340
....*....|....*....|...
gi 2108526399 321 SVVAQQPFGGARASGTnDKPGGP 343
Cdd:cd07098 428 YYVQQLPFGGVKGSGF-GRFAGE 449
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
32-344 |
4.87e-37 |
|
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: 139.45 E-value: 4.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPvFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQnld 111
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAG--- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVeD 191
Cdd:cd07111 248 ---TGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPL-D 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 FSTFFSAVIDEKSFVRIKTWLDRAKSSSnLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAvyVYPEKHY 271
Cdd:cd07111 324 KAIDMGAIVDPAQLKRIRELVEEGRAEG-ADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLV--VLTFRTA 400
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2108526399 272 KEVLQLIDNTsPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNdkSTGSVVAQQPFGGARASGTNdKPGGPH 344
Cdd:cd07111 401 KEAVALANNT-PYGLAASVWSENLSLALEVALSLK--AGVVWIN--GHNLFDAAAGFGGYRESGFG-REGGKE 467
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
32-341 |
8.46e-37 |
|
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: 138.26 E-value: 8.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYAVyKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAqnl 110
Cdd:cd07146 145 IAANNRIVLKPSEkTPLSAIYLA-DLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 dtYRtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVE 190
Cdd:cd07146 221 --YK---RQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMD 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DfSTFFSAVIDEKSFVRIKTWLDRAKSSSnLNVIAGGncdDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAvyVYPEKH 270
Cdd:cd07146 296 P-ATDMGTVIDEEAAIQIENRVEEAIAQG-ARVLLGN---QRQGALYAPTVLDHVPPDAELVTEETFGPVAP--VIRVKD 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2108526399 271 YKEVLQLIDNTSpYALTGAVFAQDKEVIAEAAEALRNAAGNyyVNDkSTGSVVAQQPFGGARASGTNDKPG 341
Cdd:cd07146 369 LDEAIAISNSTA-YGLSSGVCTNDLDTIKRLVERLDVGTVN--VNE-VPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
29-294 |
1.18e-36 |
|
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: 138.11 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 29 TLHLAVGNVVLWKPSDTAMSASYAVYK----VLRECGLPPNIIQFLPADGPVfGDAVTSSEHLAGINFTGSVPTFKRLWK 104
Cdd:cd07130 154 AIALVCGNVVVWKPSPTTPLTAIAVTKivarVLEKNGLPGAIASLVCGGADV-GEALVKDPRVPLVSFTGSTAVGRQVGQ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 105 QVAqnldtyRTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIR 184
Cdd:cd07130 233 AVA------ARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 185 VGDPVEDfSTFFSAVIDEKSFVRIKTWLDRAKSSSNlNVIAGGNCDDKTGYFVEPTIIEtTDPQDAIMNEEIFGPVLavY 264
Cdd:cd07130 307 IGDPLDD-GTLVGPLHTKAAVDNYLAAIEEAKSQGG-TVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPIL--Y 381
|
250 260 270
....*....|....*....|....*....|
gi 2108526399 265 VYPEKHYKEVLQlIDNTSPYALTGAVFAQD 294
Cdd:cd07130 382 VLKFDTLEEAIA-WNNEVPQGLSSSIFTTD 410
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
32-335 |
1.33e-36 |
|
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: 137.86 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKP-SDTAMSASyAVYKVLREC-GLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQN 109
Cdd:cd07120 142 LAAGCTVVVKPaGQTAQINA-AIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPT 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 110 LDtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGdPV 189
Cdd:cd07120 221 LK------RLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVG-PG 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 190 EDFSTFFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGNCDDKT--GYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYp 267
Cdd:cd07120 294 LDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGGPVTEGLakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETF- 372
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526399 268 eKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKstGSVVAQQPFGGARASG 335
Cdd:cd07120 373 -DDEAEAVALA-NDTDYGLAASVWTRDLARAMRVARAIR--AGTVWINDW--NKLFAEAEEGGYRQSG 434
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
32-335 |
6.28e-35 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 132.55 E-value: 6.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLd 111
Cdd:PRK10090 96 LLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNI- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtfPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:PRK10090 175 -----TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAER 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 FSTFFSAVIDEKSFVRIKTWLDRAKSSSnLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpeKHY 271
Cdd:PRK10090 250 NDIAMGPLINAAALERVEQKVARAVEEG-ARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAF--DTL 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526399 272 KEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKstgSVVAQQPF-GGARASG 335
Cdd:PRK10090 327 EEAIAMA-NDSDYGLTSSIYTQNLNVAMKAIKGLK--FGETYINRE---NFEAMQGFhAGWRKSG 385
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
32-343 |
1.22e-34 |
|
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: 132.42 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPS-DTAMSASYAVYKVLRECGLPPNIIQFLPADGPVfGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:cd07152 135 LALGNAVVLKPDpRTPVSGGVVIARLFEEAGLPAGVLHVLPGGADA-GEALVEDPNVAMISFTGSTAVGRKVGEAAGRHL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVE 190
Cdd:cd07152 214 K------KVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPAT 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DfSTFFSAVIDEKSFVRIktwlDRAKSSS---NLNVIAGGNCDdktGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYp 267
Cdd:cd07152 288 G-QVALGPLINARQLDRV----HAIVDDSvaaGARLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVF- 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526399 268 eKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKsTGSVVAQQPFGGARASGTNDKPGGP 343
Cdd:cd07152 359 -DSDEEAVALA-NDTEYGLSAGIISRDVGRAMALADRLR--TGMLHINDQ-TVNDEPHNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
32-335 |
1.35e-34 |
|
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: 132.43 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKP-SDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:cd07151 155 LALGNAVVLKPaSDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVE 190
Cdd:cd07151 235 K------KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DfSTFFSAVIDEKSFVRIKTWLDRAKSSSnLNVIAGGncdDKTGYFVEPTIIETTDPQDAIMNEEIFGPVlaVYVYPEKH 270
Cdd:cd07151 309 P-DTVVGPLINESQVDGLLDKIEQAVEEG-ATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPV--APIIKADD 381
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526399 271 YKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKStgsvVAQQP---FGGARASG 335
Cdd:cd07151 382 EEEALELA-NDTEYGLSGAVFTSDLERGVQFARRID--AGMTHINDQP----VNDEPhvpFGGEKNSG 442
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
32-335 |
1.70e-34 |
|
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: 132.31 E-value: 1.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKP-SDTAMSASYAVyKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNl 110
Cdd:cd07082 166 LIMGNTVVFKPaTQGVLLGIPLA-EAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMK- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 dtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVE 190
Cdd:cd07082 244 -------RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWD 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DfSTFFSAVIDEKSFVRIKTWLDRAKSSSNlNVIAGGNCDDKTgyFVEPTIIETTDPQDAIMNEEIFGPVLavyvyPEKH 270
Cdd:cd07082 317 N-GVDITPLIDPKSADFVEGLIDDAVAKGA-TVLNGGGREGGN--LIYPTLLDPVTPDMRLAWEEPFGPVL-----PIIR 387
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108526399 271 YKEVLQLID--NTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKStgsvvaQQ-----PFGGARASG 335
Cdd:cd07082 388 VNDIEEAIElaNKSNYGLQASIFTKDINKARKLADALE--VGTVNINSKC------QRgpdhfPFLGRKDSG 451
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
32-315 |
6.13e-34 |
|
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: 130.44 E-value: 6.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVfGDAVTSSEHLAGINFTGSVPTFKRLWKQVAqnld 111
Cdd:cd07102 141 LLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAA---- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyRTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:cd07102 216 --GRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDP 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fSTFFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGG--NCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAvyVYPEK 269
Cdd:cd07102 294 -STTLGPVVSARAADFVRAQIADAIAKGARALIDGAlfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVG--IMKVK 370
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2108526399 270 HYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALrnAAGNYYVN 315
Cdd:cd07102 371 SDAEAIALM-NDSEYGLTASVWTKDIARAEALGEQL--ETGTVFMN 413
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
32-344 |
1.10e-33 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 130.58 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSAsYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQnl 110
Cdd:PLN02278 185 LAAGCTVVVKPSElTPLTA-LAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAA-- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 dtyrTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVE 190
Cdd:PLN02278 262 ----TVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DFSTfFSAVIDEKSFVRIKTWLDRAkSSSNLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpeKH 270
Cdd:PLN02278 338 EGVT-QGPLINEAAVQKVESHVQDA-VSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRF--KT 413
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108526399 271 YKEVLqLIDNTSPYALTGAVFAQDKEVIAEAAEALRNaaGNYYVNDKSTGSVVAqqPFGGARASGTNdKPGGPH 344
Cdd:PLN02278 414 EEEAI-AIANDTEAGLAAYIFTRDLQRAWRVSEALEY--GIVGVNEGLISTEVA--PFGGVKQSGLG-REGSKY 481
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
32-335 |
6.35e-32 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 125.38 E-value: 6.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSAsYAVYKVLRECGLPPNIIQFLPADGPVfGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:PRK13252 167 LAAGNAMIFKPSEvTPLTA-LKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPvE 190
Cdd:PRK13252 245 K------EVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDP-M 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DFSTFFSAVIDEKSFVRIKTWLDRAKSSSnLNVIAGG----NCDDKTGYFVEPTIIetTDPQD--AIMNEEIFGPVLAVY 264
Cdd:PRK13252 318 DPATNFGPLVSFAHRDKVLGYIEKGKAEG-ARLLCGGerltEGGFANGAFVAPTVF--TDCTDdmTIVREEIFGPVMSVL 394
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526399 265 VYPEKhyKEVLQLIDNTsPYALTGAVFAQD----KEVIAeaaealRNAAGNYYVNdkSTGSVVAQQPFGGARASG 335
Cdd:PRK13252 395 TFDDE--DEVIARANDT-EYGLAAGVFTADlsraHRVIH------QLEAGICWIN--TWGESPAEMPVGGYKQSG 458
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
32-348 |
7.61e-32 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 124.84 E-value: 7.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKP-SDTAMSASyAVYKVLRECGLPPNIIQFLPADGPVfGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNl 110
Cdd:cd07148 149 IAAGCPVIVKPaLATPLSCL-AFVDLLHEAGLPEGWCQAVPCENAV-AEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 dtyrtfPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVe 190
Cdd:cd07148 226 ------TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPT- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DFSTFFSAVIDEKSFVRIKTWLDRAKSSSNlNVIAGGNCDDKTGYfvEPTIIeTTDPQDAIMN-EEIFGPVLAVYvypek 269
Cdd:cd07148 299 DPDTEVGPLIRPREVDRVEEWVNEAVAAGA-RLLCGGKRLSDTTY--APTVL-LDPPRDAKVStQEIFGPVVCVY----- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 270 HYKEVLQLID--NTSPYALTGAVFAQDKEVIAEAAEALrnAAGNYYVNDKsTGSVVAQQPFGGARASGTNdkPGGPHYVL 347
Cdd:cd07148 370 SYDDLDEAIAqaNSLPVAFQAAVFTKDLDVALKAVRRL--DATAVMVNDH-TAFRVDWMPFAGRRQSGYG--TGGIPYTM 444
|
.
gi 2108526399 348 R 348
Cdd:cd07148 445 H 445
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
32-335 |
1.82e-31 |
|
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: 124.10 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECgLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLd 111
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtFPRlTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:cd07117 239 ----IPA-TLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDP 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fSTFFSAVIDEKSFVRIKTWLDRAKSSsNLNVIAGG------NCDdkTGYFVEPTIIETTDPQDAIMNEEIFGPVLAvyV 265
Cdd:cd07117 314 -DTQMGAQVNKDQLDKILSYVDIAKEE-GAKILTGGhrltenGLD--KGFFIEPTLIVNVTNDMRVAQEEIFGPVAT--V 387
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 266 YPEKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNdkSTGSVVAQQPFGGARASG 335
Cdd:cd07117 388 IKFKTEDEVIDMA-NDSEYGLGGGVFTKDINRALRVARAVE--TGRVWVN--TYNQIPAGAPFGGYKKSG 452
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
32-340 |
2.27e-31 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 123.92 E-value: 2.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPAdGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLD 111
Cdd:PRK09457 159 LLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 TYrtfprLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQ--IKRgLLDIHSNIRVGDPV 189
Cdd:PRK09457 238 KI-----LALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDafLAR-LVAVAKRLTVGRWD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 190 EDFSTFFSAVIDEKSFVRIktwldrAKSSSNLnVIAGGNC-------DDKTGyFVEPTIIETTDPQDaIMNEEIFGPVLA 262
Cdd:PRK09457 312 AEPQPFMGAVISEQAAQGL------VAAQAQL-LALGGKSllemtqlQAGTG-LLTPGIIDVTGVAE-LPDEEYFGPLLQ 382
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526399 263 VYVYPekHYKEVLQLIDNTSpYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAqQPFGGARASGtNDKP 340
Cdd:PRK09457 383 VVRYD--DFDEAIRLANNTR-FGLSAGLLSDDREDYDQFLLEIR--AGIVNWNKPLTGASSA-APFGGVGASG-NHRP 453
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
32-335 |
3.59e-31 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 122.25 E-value: 3.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECgLPPNIIQFlpadgpVFGDAVTSSEHLAG----INFTGSVPTFKRLWKQVA 107
Cdd:cd07087 125 IAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAV------VEGGVEVATALLAEpfdhIFFTGSPAVGKIVMEAAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 108 QNLdtyrTfPrLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPdglwPQIKRGLLDihsniRVGD 187
Cdd:cd07087 198 KHL----T-P-VTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVH----ESIKDELIE-----ELKK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 188 PVEDF-------STFFSAVIDEKSFVRIKTWLDRAKsssnlnVIAGGNCDDKTGYfVEPTIIETTDPQDAIMNEEIFGPV 260
Cdd:cd07087 263 AIKEFygedpkeSPDYGRIINERHFDRLASLLDDGK------VVIGGQVDKEERY-IAPTILDDVSPDSPLMQEEIFGPI 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 261 LAVYVYPEKHykEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDkstgsVVAQQ-----PFGGARASG 335
Cdd:cd07087 336 LPILTYDDLD--EAIEFI-NSRPKPLALYLFSEDKAVQERVLAETS--SGGVCVND-----VLLHAaipnlPFGGVGNSG 405
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
32-335 |
5.48e-31 |
|
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: 122.84 E-value: 5.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAmSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLd 111
Cdd:cd07559 161 LAAGNTVVLKPASQT-PLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtFPrLTGECGGK--NFYFvhksADVES--------VVKGTIRSAFEYGgQKCSACSRMYVPDGLWPQIKRGLLDIHS 181
Cdd:cd07559 239 ----IP-VTLELGGKspNIFF----DDAMDadddfddkAEEGQLGFAFNQG-EVCTCPSRALVQESIYDEFIERAVERFE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 182 NIRVGDPVEDfSTFFSAVIDEKSFVRIKTWLDRAKSSsNLNVIAGG-----NCDDKtGYFVEPTIIETTDPQDAIMNEEI 256
Cdd:cd07559 309 AIKVGNPLDP-ETMMGAQVSKDQLEKILSYVDIGKEE-GAEVLTGGerltlGGLDK-GYFYEPTLIKGGNNDMRIFQEEI 385
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526399 257 FGPVLAVYVYpeKHYKEVLQlIDNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNdkSTGSVVAQQPFGGARASG 335
Cdd:cd07559 386 FGPVLAVITF--KDEEEAIA-IANDTEYGLGGGVWTRDINRALRVARGIQ--TGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
32-341 |
6.06e-31 |
|
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: 122.60 E-value: 6.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYAVyKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQ-N 109
Cdd:cd07142 166 LACGNTIVLKPAEqTPLSALLAA-KLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsN 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 110 LDtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPv 189
Cdd:cd07142 245 LK------PVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDP- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 190 edfstFFSAV-----IDEKSFVRIKTWLDRAKsSSNLNVIAGGNCDDKTGYFVEPTIIetTDPQD--AIMNEEIFGPVLA 262
Cdd:cd07142 318 -----FRKGVeqgpqVDKEQFEKILSYIEHGK-EEGATLITGGDRIGSKGYYIQPTIF--SDVKDdmKIARDEIFGPVQS 389
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526399 263 VYVYpeKHYKEVLQLIDNTSpYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNdkSTGSVVAQQPFGGARASGTNDKPG 341
Cdd:cd07142 390 ILKF--KTVDEVIKRANNSK-YGLAAGVFSKNIDTANTLSRALK--AGTVWVN--CYDVFDASIPFGGYKMSGIGREKG 461
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
32-335 |
1.18e-30 |
|
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: 121.18 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECglppniiqFLPADGPVF-GDAVTSSEHLA----GINFTGSVPTFKRLWKQV 106
Cdd:cd07134 125 IAAGNTAILKPSELTPHTSAVIAKIIREA--------FDEDEVAVFeGDAEVAQALLElpfdHIFFTGSPAVGKIVMAAA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 107 AQNLDTyrtfprLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSAcsrmyvPDGLW--PQIKRGLLD-----I 179
Cdd:cd07134 197 AKHLAS------VTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIA------PDYVFvhESVKDAFVEhlkaeI 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 180 HSNIRVGDPVEDfSTFFSAVIDEKSFVRIKTWLDRAKSSsNLNVIAGGNcDDKTGYFVEPTIIETTDPQDAIMNEEIFGP 259
Cdd:cd07134 265 EKFYGKDAARKA-SPDLARIVNDRHFDRLKGLLDDAVAK-GAKVEFGGQ-FDAAQRYIAPTVLTNVTPDMKIMQEEIFGP 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 260 VLAVYVYpeKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEalRNAAGNYYVNDkstgsVVAQ-----QPFGGARAS 334
Cdd:cd07134 342 VLPIITY--EDLDEVIEYI-NAKPKPLALYVFSKDKANVNKVLA--RTSSGGVVVND-----VVLHflnpnLPFGGVNNS 411
|
.
gi 2108526399 335 G 335
Cdd:cd07134 412 G 412
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
32-335 |
3.49e-30 |
|
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: 119.87 E-value: 3.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFgDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLD 111
Cdd:cd07100 121 LMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLK 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:cd07100 200 ------KSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDE 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fSTFFSAVIDEKSFVRIKTWLDRAKSSSNlNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpeKHY 271
Cdd:cd07100 274 -DTDLGPLARKDLRDELHEQVEEAVAAGA-TLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKV--KDE 349
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526399 272 KEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVND--KSTgsvvAQQPFGGARASG 335
Cdd:cd07100 350 EEAIALA-NDSPFGLGGSVFTTDLERAERVARRLE--AGMVFINGmvKSD----PRLPFGGVKRSG 408
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
32-335 |
4.60e-30 |
|
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: 119.60 E-value: 4.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFL---PADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQ 108
Cdd:cd07105 123 LAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 109 NLDtyrtfPRLTgECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDP 188
Cdd:cd07105 203 HLK-----PVLL-ELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPV 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 189 VEdfstffSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpe 268
Cdd:cd07105 277 VL------GSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRV-- 348
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 269 KHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNdkstGSVV---AQQPFGGARASG 335
Cdd:cd07105 349 KDEEEAVRIA-NDSEYGLSAAVFTRDLARALAVAKRIE--SGAVHIN----GMTVhdePTLPHGGVKSSG 411
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
32-335 |
4.62e-30 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 120.13 E-value: 4.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECgLPPNIIQFLPADGPVfGDAVTSsEHLAGINFTGSVPTFKRLWKQVAQNLd 111
Cdd:PTZ00381 134 IAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEV-TTELLK-EPFDHIFFTGSPRVGKLVMQAAAENL- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtFPrLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVP----DGLWPQIKRGLLDIHSNirvgD 187
Cdd:PTZ00381 210 ----TP-CTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHrsikDKFIEALKEAIKEFFGE----D 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 188 PVEdfSTFFSAVIDEKSFVRIKTWLDRAKSssnlNVIAGGNCDDKTGYfVEPTIIETTDPQDAIMNEEIFGPVLAVYVYp 267
Cdd:PTZ00381 281 PKK--SEDYSRIVNEFHTKRLAELIKDHGG----KVVYGGEVDIENKY-VAPTIIVNPDLDSPLMQEEIFGPILPILTY- 352
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108526399 268 eKHYKEVLQLIdNTSPYALTGAVFAQDKEvIAEAAEAlRNAAGNYYVNDkstgSVV----AQQPFGGARASG 335
Cdd:PTZ00381 353 -ENIDEVLEFI-NSRPKPLALYYFGEDKR-HKELVLE-NTSSGAVVIND----CVFhllnPNLPFGGVGNSG 416
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
32-335 |
8.51e-30 |
|
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: 119.52 E-value: 8.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSA-SYAVYKVLreCGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVA-Q 108
Cdd:cd07140 172 LAAGNTVVLKPAQvTPLTAlKFAELTVK--AGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAvS 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 109 NLDtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDP 188
Cdd:cd07140 250 NLK------KVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDP 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 189 VeDFSTFFSAVIDEKSFVRIKTWLDRA-KSSSNLnvIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYP 267
Cdd:cd07140 324 L-DRSTDHGPQNHKAHLDKLVEYCERGvKEGATL--VYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFD 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526399 268 EKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAqqPFGGARASG 335
Cdd:cd07140 401 DGDVDGVLQRA-NDTEYGLASGVFTKDINKALYVSDKLE--AGTVFVNTYNKTDVAA--PFGGFKQSG 463
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
32-341 |
3.60e-29 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 117.99 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYAVyKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKrlwkqVAQNL 110
Cdd:PLN02466 220 LACGNTIVLKTAEqTPLSALYAA-KLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGK-----IVLEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DTYRTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQI-----KRGLLDIhsnirV 185
Cdd:PLN02466 294 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFvekakARALKRV-----V 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 186 GDPvedfstFFSAV-----IDEKSFVRIKTWLdRAKSSSNLNVIAGGNCDDKTGYFVEPTIIetTDPQDA--IMNEEIFG 258
Cdd:PLN02466 369 GDP------FKKGVeqgpqIDSEQFEKILRYI-KSGVESGATLECGGDRFGSKGYYIQPTVF--SNVQDDmlIAQDEIFG 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 259 PVLAVYVYpeKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVN--DKSTGSVvaqqPFGGARASGT 336
Cdd:PLN02466 440 PVQSILKF--KDLDEVIRRA-NNTRYGLAAGVFTQNLDTANTLSRALR--VGTVWVNcfDVFDAAI----PFGGYKMSGI 510
|
....*
gi 2108526399 337 NDKPG 341
Cdd:PLN02466 511 GREKG 515
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
32-335 |
4.52e-28 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 114.62 E-value: 4.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKP-SDTAMSAsYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:PRK11241 171 LAAGCTMVLKPaSQTPFSA-LALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVE 190
Cdd:PRK11241 250 K------KVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DFSTfFSAVIDEKSFVRIKTWLDRAkSSSNLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpeKH 270
Cdd:PRK11241 324 KGVT-IGPLIDEKAVAKVEEHIADA-LEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRF--KD 399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526399 271 YKEVLQLIDNTSpYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAqqPFGGARASG 335
Cdd:PRK11241 400 EADVIAQANDTE-FGLAAYFYARDLSRVFRVGEALE--YGIVGINTGIISNEVA--PFGGIKASG 459
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
32-335 |
6.22e-28 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 114.15 E-value: 6.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSD-TAMSASYAVYkVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQ-N 109
Cdd:PLN02766 183 LAAGCTMVVKPAEqTPLSALFYAH-LAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsN 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 110 LDtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPV 189
Cdd:PLN02766 262 LK------QVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 190 eDFSTFFSAVIDEKSFVRIKTWLDRAKSSSNLNVIAGGNCDDKtGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpeK 269
Cdd:PLN02766 336 -DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDK-GYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKF--K 411
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2108526399 270 HYKEVLQLIDNTSpYALTGAVFAQDKEVIAEAAEALRnaAGNYYVN-----DKSTgsvvaqqPFGGARASG 335
Cdd:PLN02766 412 TVEEAIKKANNTK-YGLAAGIVTKDLDVANTVSRSIR--AGTIWVNcyfafDPDC-------PFGGYKMSG 472
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
32-335 |
8.93e-28 |
|
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: 113.37 E-value: 8.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECgLPPNIIQFlpadgpVFGDAVTSSEHLAG----INFTGSVPTFKRLWKQVA 107
Cdd:cd07136 125 IAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAV------VEGGVEENQELLDQkfdyIFFTGSVRVGKIVMEAAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 108 QNLdtyrTfPrLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSAcsrmyvPDGLWpqikrglldIHSNIR--- 184
Cdd:cd07136 198 KHL----T-P-VTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVA------PDYVL---------VHESVKekf 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 185 ------------VGDPVEdfSTFFSAVIDEKSFVRIKTWLDRAKsssnlnVIAGGNCDDKTGYfVEPTIIETTDPQDAIM 252
Cdd:cd07136 257 ikelkeeikkfyGEDPLE--SPDYGRIINEKHFDRLAGLLDNGK------IVFGGNTDRETLY-IEPTILDNVTWDDPVM 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 253 NEEIFGPVLAVYVYpeKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRNAAGnyYVNDKSTGSVVAQQPFGGAR 332
Cdd:cd07136 328 QEEIFGPILPVLTY--DTLDEAIEII-KSRPKPLALYLFSEDKKVEKKVLENLSFGGG--CINDTIMHLANPYLPFGGVG 402
|
...
gi 2108526399 333 ASG 335
Cdd:cd07136 403 NSG 405
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
32-341 |
8.15e-27 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 111.08 E-value: 8.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYK----VLRECGLPPNIIQFLpADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVA 107
Cdd:PLN02315 179 LVCGNCVVWKGAPTTPLITIAMTKlvaeVLEKNNLPGAIFTSF-CGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 108 QNldtyrtFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGD 187
Cdd:PLN02315 258 AR------FGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGD 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 188 PVEDfSTFFSAVIDEKSFVRIKTWLDRAKSSSNlNVIAGGNCDDKTGYFVEPTIIETTdPQDAIMNEEIFGPVLavYVYP 267
Cdd:PLN02315 332 PLEK-GTLLGPLHTPESKKNFEKGIEIIKSQGG-KILTGGSAIESEGNFVQPTIVEIS-PDADVVKEELFGPVL--YVMK 406
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108526399 268 EKHYKEVLQlIDNTSPYALTGAVFAQDKEVIAEAAEALRNAAGNYYVNDKSTGSVVAqQPFGGARASGTNDKPG 341
Cdd:PLN02315 407 FKTLEEAIE-INNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAG 478
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
32-335 |
8.02e-25 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 105.36 E-value: 8.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNld 111
Cdd:PRK09847 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS-- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrTFPRLTGECGGK--NFYFVhKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPV 189
Cdd:PRK09847 260 ---NMKRVWLEAGGKsaNIVFA-DCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 190 eDFSTFFSAVIDEKSFVRIKTWLDRAKSSSNLnvIAGGNCDDKTGYfVEPTIIETTDPQDAIMNEEIFGPVLAVYVYpeK 269
Cdd:PRK09847 336 -DPATTMGTLIDCAHADSVHSFIREGESKGQL--LLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRF--T 409
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526399 270 HYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAqqPFGGARASG 335
Cdd:PRK09847 410 SEEQALQLA-NDSQYGLGAAVWTRDLSRAHRMSRRLK--AGSVFVNNYNDGDMTV--PFGGYKQSG 470
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
32-335 |
8.96e-24 |
|
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: 101.91 E-value: 8.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASyavyKVLREcglppNIIQFLPADG-PVF-GDAVTSSEHLAG----INFTGSVPTFKRLWKQ 105
Cdd:cd07132 125 IAAGNCVVIKPSEVSPATA----KLLAE-----LIPKYLDKECyPVVlGGVEETTELLKQrfdyIFYTGSTSVGKIVMQA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 106 VAQNLdtyrtfPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSA-----CSRmYVPDGLWPQIKRGLLDIH 180
Cdd:cd07132 196 AAKHL------TPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIApdyvlCTP-EVQEKFVEALKKTLKEFY 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 181 SNirvgDPVEdfSTFFSAVIDEKSFVRIKTWLdrakssSNLNVIAGGNCDDKTGYfVEPTIIETTDPQDAIMNEEIFGPV 260
Cdd:cd07132 269 GE----DPKE--SPDYGRIINDRHFQRLKKLL------SGGKVAIGGQTDEKERY-IAPTVLTDVKPSDPVMQEEIFGPI 335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526399 261 LAvyVYPEKHYKEVLQLIDN-TSPYALTgaVFAQDKEVIAEAAEalRNAAGNYYVNDKSTGSVVAQQPFGGARASG 335
Cdd:cd07132 336 LP--IVTVNNLDEAIEFINSrEKPLALY--VFSNNKKVINKILS--NTSSGGVCVNDTIMHYTLDSLPFGGVGNSG 405
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
32-336 |
1.25e-23 |
|
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: 101.14 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLREcGLPPNIIQFLPADGPVFGDAVTSS-EHlagINFTGSVPTFKRLWKQVAQNL 110
Cdd:cd07135 133 IAAGCTVVLKPSELTPHTAALLAELVPK-YLDPDAFQVVQGGVPETTALLEQKfDK---IFYTGSGRVGRIIAEAAAKHL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DtyrtfPrLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPdglwPQIKRGLLDihsniRVGDPVE 190
Cdd:cd07135 209 T-----P-VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVD----PSVYDEFVE-----ELKKVLD 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 191 DF-------STFFSAVIDEKSFVRIKTWLDRAKSssnlNVIAGGNCDDKTgYFVEPTIIETTDPQDAIMNEEIFGPVLAV 263
Cdd:cd07135 274 EFypgganaSPDYTRIVNPRHFNRLKSLLDTTKG----KVVIGGEMDEAT-RFIPPTIVSDVSWDDSLMSEELFGPVLPI 348
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2108526399 264 YVYpeKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSVVAQQPFGGARASGT 336
Cdd:cd07135 349 IKV--DDLDEAIKVI-NSRDTPLALYIFTDDKSEIDHILTRTR--SGGVVINDTLIHVGVDNAPFGGVGDSGY 416
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
32-334 |
1.72e-23 |
|
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: 101.44 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVfGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNld 111
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEA-VNALLDHPDIKAVSFVGSTPVGEYIYERAAAN-- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPVED 191
Cdd:cd07085 238 ----GKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDP 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 192 fSTFFSAVIDEKSFVRIKTWLDRAksssnlnVIAGGN--CDDKT--------GYFVEPTIIETTDPQDAIMNEEIFGPVL 261
Cdd:cd07085 314 -GADMGPVISPAAKERIEGLIESG-------VEEGAKlvLDGRGvkvpgyenGNFVGPTILDNVTPDMKIYKEEIFGPVL 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 262 A-VYVypeKHYKEVLQLIdNTSPYALTGAVFAQDkeviaeaaealrNAAGNYYVNDKSTGSV---------VAQQPFGGA 331
Cdd:cd07085 386 SiVRV---DTLDEAIAII-NANPYGNGAAIFTRS------------GAAARKFQREVDAGMVginvpipvpLAFFSFGGW 449
|
...
gi 2108526399 332 RAS 334
Cdd:cd07085 450 KGS 452
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
25-355 |
3.48e-21 |
|
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: 94.23 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 25 WEQYTLHLAVGNVVLWKPSDTAMSASYAVYKVLRECG-LPPNIIQFLPADGPVfGDAVTSSEHLAGINFTGSVptfkrlw 103
Cdd:cd07084 118 LLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSS------- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 104 kQVAQNLDTYRTFPRLTGECGGKNFYFVHKSAD-VESVVKGTIRSAFEYGGQKCSACSRMYVPDGlwPQIKRGLLDIHSN 182
Cdd:cd07084 190 -RVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPEN--WSKTPLVEKLKAL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 183 IRvgdPVEDFSTFFSAVIDEKSFVRIKTW--LDRAKSSSNLNVIAGGNCDDKTGYFVEPTIIETTDPQDA---IMNEEIF 257
Cdd:cd07084 267 LA---RRKLEDLLLGPVQTFTTLAMIAHMenLLGSVLLFSGKELKNHSIPSIYGACVASALFVPIDEILKtyeLVTEEIF 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 258 GPVLAVYVYPEKHYKEVLQLIDNTSPyALTGAVFAQDKEVIAEAAEALRNAAGNYYVNDKSTGSVVAQQPFGGARASGTN 337
Cdd:cd07084 344 GPFAIVVEYKKDQLALVLELLERMHG-SLTAAIYSNDPIFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRG 422
|
330
....*....|....*...
gi 2108526399 338 DKPGGPHYVLRWTSPQVV 355
Cdd:cd07084 423 AGIGGPEAIKLVWRCHAE 440
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
32-335 |
4.25e-20 |
|
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: 91.36 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDtAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLd 111
Cdd:cd07116 161 LAAGNCVVLKPAE-QTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 tyrtFPrLTGECGGK--NFYF----VHKSADVESVVKGTIRSAFEYgGQKCSACSRMYVPDGLW-PQIKRGLLDIHSnIR 184
Cdd:cd07116 239 ----IP-VTLELGGKspNIFFadvmDADDAFFDKALEGFVMFALNQ-GEVCTCPSRALIQESIYdRFMERALERVKA-IK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 185 VGDPVeDFSTFFSAVIDEKSFVRIKTWLDRAKSSSnLNVIAGGN----CDDKTGYFVEPTIIETTDpQDAIMNEEIFGPV 260
Cdd:cd07116 312 QGNPL-DTETMIGAQASLEQLEKILSYIDIGKEEG-AEVLTGGErnelGGLLGGGYYVPTTFKGGN-KMRIFQEEIFGPV 388
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526399 261 LAVYVYpeKHYKEVLQlIDNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNdkSTGSVVAQQPFGGARASG 335
Cdd:cd07116 389 LAVTTF--KDEEEALE-IANDTLYGLGAGVWTRDGNTAYRMGRGIQ--AGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
32-335 |
4.28e-18 |
|
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: 85.23 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECgLPPNIIQFlpadgpVFGDAVTSSE-------HLAginFTGSVPTFKRLWK 104
Cdd:cd07133 126 LAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAV------VTGGADVAAAfsslpfdHLL---FTGSTAVGRHVMR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 105 QVAQNLdtyrTfPrLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQ--------IKRGL 176
Cdd:cd07133 196 AAAENL----T-P-VTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEfvaaakaaVAKMY 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 177 LDIHSNirvgdpvEDFStffsAVIDEKSFVRIKTWLD--RAKSSSNLNVIAGGNCDDKTGYFVePTIIETTDPQDAIMNE 254
Cdd:cd07133 270 PTLADN-------PDYT----SIINERHYARLQGLLEdaRAKGARVIELNPAGEDFAATRKLP-PTLVLNVTDDMRVMQE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 255 EIFGPVLAVYVYpeKHYKEVLQLI-DNTSPYALTgaVFAQDKeviAEAAEALRN-AAGNYYVNDksTGSVVAQ--QPFGG 330
Cdd:cd07133 338 EIFGPILPILTY--DSLDEAIDYInARPRPLALY--YFGEDK---AEQDRVLRRtHSGGVTIND--TLLHVAQddLPFGG 408
|
....*
gi 2108526399 331 ARASG 335
Cdd:cd07133 409 VGASG 413
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
32-335 |
8.07e-18 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 84.40 E-value: 8.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWK-PSDTAMSASYaVYKVLRECGLPPNIIQ-FLPADGPVfgDAVTSSEHLAGINFTGSVPTfKRLWKQVAQn 109
Cdd:PRK09406 148 LMAGNVGLLKhASNVPQTALY-LADLFRRAGFPDGCFQtLLVGSGAV--EAILRDPRVAAATLTGSEPA-GRAVAAIAG- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 110 ldtyRTFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDPV 189
Cdd:PRK09406 223 ----DEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPT 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 190 EDfSTFFSAVIDEKSFVRIKTWLDRAkSSSNLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYPEk 269
Cdd:PRK09406 299 DP-DTDVGPLATEQGRDEVEKQVDDA-VAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVAD- 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108526399 270 hYKEVLQlIDNTSPYALTGAVFAQDkeviaeAAEALRNA----AGNYYVNdkstGSVVA--QQPFGGARASG 335
Cdd:PRK09406 376 -IDEAIE-IANATTFGLGSNAWTRD------EAEQERFIddleAGQVFIN----GMTVSypELPFGGVKRSG 435
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
32-336 |
2.67e-17 |
|
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: 82.84 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKvlrecglppNIIQFLPADG-PVFGDAVTSSEHLA-----GINFTGSVPTFKRLWKQ 105
Cdd:cd07137 126 IAAGNAVVLKPSELAPATSALLAK---------LIPEYLDTKAiKVIEGGVPETTALLeqkwdKIFFTGSPRVGRIIMAA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 106 VAQNLDTyrtfprLTGECGGKNFYFVHKSADVESVVKGTIrsAFEYG---GQKCSACSRMYVPDGLWPQIKRGLLDIHSN 182
Cdd:cd07137 197 AAKHLTP------VTLELGGKCPVIVDSTVDLKVAVRRIA--GGKWGcnnGQACIAPDYVLVEESFAPTLIDALKNTLEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 183 IRVGDPVEdfSTFFSAVIDEKSFVRIKTWLDRAKSSSNlnVIAGGNCDDKTGYfVEPTIIETTDPQDAIMNEEIFGPVLA 262
Cdd:cd07137 269 FFGENPKE--SKDLSRIVNSHHFQRLSRLLDDPSVADK--IVHGGERDEKNLY-IEPTILLDPPLDSSIMTEEIFGPLLP 343
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108526399 263 VYVYpeKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALrnAAGNYYVNDKSTGSVVAQQPFGGARASGT 336
Cdd:cd07137 344 IITV--KKIEESIEII-NSRPKPLAAYVFTKNKELKRRIVAET--SSGGVTFNDTVVQYAIDTLPFGGVGESGF 412
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
32-335 |
9.37e-16 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 78.36 E-value: 9.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGpvfgDAVT---SSEHLAGINFTGSVPTFKRLWKQVAQ 108
Cdd:PRK13968 151 LLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADN----DGVSqmiNDSRIAAVTVTGSVRAGAAIGAQAGA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 109 NLDtyrtfpRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDP 188
Cdd:PRK13968 227 ALK------KCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDP 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 189 vedfstffsavIDEKSFVRIKTWLD---------RAKSSSNLNVIAGGNCDDKTGYFVEPTIIETTDPQDAIMNEEIFGP 259
Cdd:PRK13968 301 -----------RDEENALGPMARFDlrdelhhqvEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGP 369
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526399 260 VLAVYVypEKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRnaAGNYYVNDKSTGSvvAQQPFGGARASG 335
Cdd:PRK13968 370 VAAITV--AKDAEHALELA-NDSEFGLSATIFTTDETQARQMAARLE--CGGVFINGYCASD--ARVAFGGVKKSG 438
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
28-294 |
1.61e-11 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 65.55 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 28 YTLHLAV---------GNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFGDAVTSSEHLAGINFTGSvpt 98
Cdd:PLN00412 170 YPVNLAVskiapaliaGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG--- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 99 fkrlwkqvaqnlDTYRTFPRLTG------ECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSA----CSRMYVPDGL 168
Cdd:PLN00412 247 ------------DTGIAISKKAGmvplqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAvkvvLVMESVADAL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 169 WPQIKRGLldihSNIRVGDPVEDFStfFSAVIDEKSFVRIKTWLDRAKSSsnlnviAGGNCDD--KTGYFVEPTIIETTD 246
Cdd:PLN00412 315 VEKVNAKV----AKLTVGPPEDDCD--ITPVVSESSANFIEGLVMDAKEK------GATFCQEwkREGNLIWPLLLDNVR 382
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2108526399 247 PQDAIMNEEIFGPVLAVYVYpeKHYKEVLQLIdNTSPYALTGAVFAQD 294
Cdd:PLN00412 383 PDMRIAWEEPFGPVLPVIRI--NSVEEGIHHC-NASNFGLQGCVFTRD 427
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
32-335 |
1.85e-11 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 65.13 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECgLPPNIIQFLPAdGPVFGDAVTssEH-LAGINFTGSVPTFKRLWKQVAQNL 110
Cdd:PLN02203 133 IAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEG-GPAVGEQLL--QHkWDKIFFTGSPRVGRIIMTAAAKHL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 111 DTyrtfprLTGECGGKN---FYFVHKSADVESVVKGTIRSAFEY-GGQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVG 186
Cdd:PLN02203 209 TP------VALELGGKCpciVDSLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 187 DPVEdfSTFFSAVIDEKSFVRIKTWL-DRAKSSSnlnVIAGGNCDDKTgYFVEPTIIETTDPQDAIMNEEIFGPVLAVYV 265
Cdd:PLN02203 283 NPRE--SKSMARILNKKHFQRLSNLLkDPRVAAS---IVHGGSIDEKK-LFIEPTILLNPPLDSDIMTEEIFGPLLPIIT 356
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108526399 266 YpeKHYKEVLQLIdNTSPYALTGAVFAQD----KEVIAEaaealrNAAGNYYVNDKSTGSVVAQQPFGGARASG 335
Cdd:PLN02203 357 V--KKIEDSIAFI-NSKPKPLAIYAFTNNeklkRRILSE------TSSGSVTFNDAIIQYACDSLPFGGVGESG 421
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
28-291 |
1.34e-10 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 62.84 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 28 YTLHLAVGNVVLWKPSDTAMSASYAVYKVLRECGLPPNIIQFLPADGPVFgDAVTSSEHLAGINFTGSVPTFKRLWKQVA 107
Cdd:PLN02419 270 FPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAA 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 108 QNldtyrtFPRLTGECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRM-YVPDGLWPQIKrgLLDIHSNIRV- 185
Cdd:PLN02419 349 AK------GKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVvFVGDAKSWEDK--LVERAKALKVt 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 186 --GDPVEDFSTFFSAVIDEKSFVRIKTWLDRAKSS--SNLNVIAGGNcddKTGYFVEPTIIETTDPQDAIMNEEIFGPVL 261
Cdd:PLN02419 421 cgSEPDADLGPVISKQAKERICRLIQSGVDDGAKLllDGRDIVVPGY---EKGNFIGPTILSGVTPDMECYKEEIFGPVL 497
|
250 260 270
....*....|....*....|....*....|
gi 2108526399 262 AvyVYPEKHYKEVLQLIdNTSPYALTGAVF 291
Cdd:PLN02419 498 V--CMQANSFDEAISII-NKNKYGNGAAIF 524
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
32-335 |
2.62e-10 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 61.60 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTAMSASYAVYKVLRECgLPPNIIQFLpaDGPVFGDAVTSSEHLAGINFTGSVPTFKRLWKQVAQNLD 111
Cdd:PLN02174 137 ISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVV--EGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLT 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 112 TyrtfprLTGECGGKNFYFVHKSADVESVVKGTIrsAFEYG---GQKCSACSRMYVPDGLWPQIKRGLLDIHSNIRVGDP 188
Cdd:PLN02174 214 P------VVLELGGKSPVVVDSDTDLKVTVRRII--AGKWGcnnGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNP 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 189 VEdfSTFFSAVIDEKSFVRIKTWLDRAKSSSNlnVIAGGNcDDKTGYFVEPTIIETTDPQDAIMNEEIFGPVLAVYVYPE 268
Cdd:PLN02174 286 ME--SKDMSRIVNSTHFDRLSKLLDEKEVSDK--IVYGGE-KDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNN 360
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108526399 269 KHykEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALrnAAGNYYVNDKSTGSVVAQQPFGGARASG 335
Cdd:PLN02174 361 LE--ESFDVI-RSRPKPLAAYLFTHNKKLKERFAATV--SAGGIVVNDIAVHLALHTLPFGGVGESG 422
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
25-335 |
4.07e-10 |
|
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: 61.13 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 25 WEQYTLHLAVGNVVLWKP-SDTAMSAsYAVYKVLRECG-LPPNIIQFLPAD-GPVFgDAVTSSEHLAginFTGSVPTFKR 101
Cdd:cd07128 162 LEKFAPALLAGVPVIVKPaTATAYLT-EAVVKDIVESGlLPEGALQLICGSvGDLL-DHLGEQDVVA---FTGSAATAAK 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 102 LwkqvaqnldtyRTFP-------RLTGECGGKNFYFVhkSADVES-------VVKGTIRSAFEYGGQKCSACSRMYVPDG 167
Cdd:cd07128 237 L-----------RAHPnivarsiRFNAEADSLNAAIL--GPDATPgtpefdlFVKEVAREMTVKAGQKCTAIRRAFVPEA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 168 LWPQIKRGLLDIHSNIRVGDPVEDFSTFFSAV-IDEKSFVRIKTwldrAKSSSNLNVIAGGN-------CDDKTGYFVEP 239
Cdd:cd07128 304 RVDAVIEALKARLAKVVVGDPRLEGVRMGPLVsREQREDVRAAV----ATLLAEAEVVFGGPdrfevvgADAEKGAFFPP 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 240 TIIETTDP--QDAIMNEEIFGPVLAVYVYpeKHYKEVLQLIdNTSPYALTGAVFAQDKEVIAEAAEALRNAAGNYYVNDK 317
Cdd:cd07128 380 TLLLCDDPdaATAVHDVEAFGPVATLMPY--DSLAEAIELA-ARGRGSLVASVVTNDPAFARELVLGAAPYHGRLLVLNR 456
|
330 340
....*....|....*....|....*.
gi 2108526399 318 -----ST--GSVVAQQPFGG-ARASG 335
Cdd:cd07128 457 dsakeSTghGSPLPQLVHGGpGRAGG 482
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
25-335 |
1.97e-09 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 58.95 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 25 WEQYTLHLAVGNVVLWKP-SDTAMSASYAVYKVLRECGLPPNIIQFlpadgpVFGDAVTSSEHLAG---INFTGSVPTFK 100
Cdd:PRK11903 166 WEKAAPALLAGVPVIVKPaTATAWLTQRMVKDVVAAGILPAGALSV------VCGSSAGLLDHLQPfdvVSFTGSAETAA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 101 RLwkqvaqnldtyRTFPRLTGEcggknfyFVHKSADVESV-------------------VKGTIRSAFEYGGQKCSACSR 161
Cdd:PRK11903 240 VL-----------RSHPAVVQR-------SVRVNVEADSLnsallgpdaapgseafdlfVKEVVREMTVKSGQKCTAIRR 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 162 MYVPDGLWPQIKRGLLDIHSNIRVGDPVEDfSTFFSAVIDEKSFVRIKTWLDRAKSSSNLnVIAGGNC-----DDKTGYF 236
Cdd:PRK11903 302 IFVPEALYDAVAEALAARLAKTTVGNPRND-GVRMGPLVSRAQLAAVRAGLAALRAQAEV-LFDGGGFalvdaDPAVAAC 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 237 VEPTIIETTDPQDA--IMNEEIFGPVLAVYVY-PEKHYKEVLQLIDNTspyaLTGAVFAQDKEVIAEAAEALRNAAGNYY 313
Cdd:PRK11903 380 VGPTLLGASDPDAAtaVHDVEVFGPVATLLPYrDAAHALALARRGQGS----LVASVYSDDAAFLAAAALELADSHGRVH 455
|
330 340 350
....*....|....*....|....*....|
gi 2108526399 314 VNDKST-------GSVVAQQPFGG-ARASG 335
Cdd:PRK11903 456 VISPDVaalhtghGNVMPQSLHGGpGRAGG 485
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
32-337 |
1.52e-05 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 46.70 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 32 LAVGNVVLWKPSDTA---MSASYAVYK-VLRECGLPPNIIQfLPADGPvfGDAVTssEHLAG------INFTGSvPTFKR 101
Cdd:cd07127 218 LATGNPVIVKPHPAAilpLAITVQVAReVLAEAGFDPNLVT-LAADTP--EEPIA--QTLATrpevriIDFTGS-NAFGD 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 102 LWKQVAQNLDTYRtfprltgECGGKNFYFVHKSADVESVVKGTIRSAFEYGGQKCSACSRMYVP-DGLwpQIKRGLL--- 177
Cdd:cd07127 292 WLEANARQAQVYT-------EKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPrDGI--QTDDGRKsfd 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 178 ----DIHSNIR--VGDPvEDFSTFFSAVIDEKSFVRIktwldrAKSSSNLNVIAGG----NCDDKTGYFVEPTIIETTDP 247
Cdd:cd07127 363 evaaDLAAAIDglLADP-ARAAALLGAIQSPDTLARI------AEARQLGEVLLASeavaHPEFPDARVRTPLLLKLDAS 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526399 248 QDAIMNEEIFGPVL-AVYVYPEKHYKEVLQLIDNTSPyALTGAVFAQDKEVIAEAAEALRNAAGNYYVNdkSTGSVVAQQ 326
Cdd:cd07127 436 DEAAYAEERFGPIAfVVATDSTDHSIELARESVREHG-AMTVGVYSTDPEVVERVQEAALDAGVALSIN--LTGGVFVNQ 512
|
330
....*....|...
gi 2108526399 327 P--FGGARASGTN 337
Cdd:cd07127 513 SaaFSDFHGTGAN 525
|
|
| |
