|
Name |
Accession |
Description |
Interval |
E-value |
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
65-509 |
3.49e-54 |
|
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: 189.95 E-value: 3.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 65 VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLGELFREALLRNRETFLDLLVAEAH-PRKLAEWEFScllqvYS 143
Cdd:COG1012 33 VLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGkPLAEARGEVD-----RA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 144 PESISFYASQMH------TEFAYGDRRLIVRRQPDGVVCVNPPQNAPAPSAALAVLAL-MAGNAVVVRAPRSIALSTMyv 216
Cdd:COG1012 108 ADFLRYYAGEARrlygetIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPAlAAGNTVVLKPAEQTPLSAL-- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 217 lrdLVAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVWHD 296
Cdd:COG1012 186 ---LLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 297 ADLALAAEAI-TECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQA 372
Cdd:COG1012 263 ADLDAAVEAAvRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLiseAQLERVLAYIEDA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 373 LSRGAQLVCGGDRIELDGtvsetGVFLQPTVLR-VDglAGARtvdAVRDETFFPLLPVVvpePMSDadlLDRVIAYVNSN 451
Cdd:COG1012 343 VAEGAELLTGGRRPDGEG-----GYFVEPTVLAdVT--PDMR---IAREEIFGPVLSVI---PFDD---EEEAIALANDT 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 505433282 452 EYGLRNSLWSGSDEVVERFVREVgNGGLLKVNDSHIGFLPYLPtHGGTGLtSGVHGEA 509
Cdd:COG1012 407 EYGLAASVFTRDLARARRVARRL-EAGMVWINDGTTGAVPQAP-FGGVKQ-SGIGREG 461
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
94-516 |
2.16e-47 |
|
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: 170.47 E-value: 2.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 94 VPLPTRLRLGELFREALLRNRETFLDLLVAEAH-PRKLAEWEFSCLLQVyspesISFYASQ------MHTEFAYGDRRLI 166
Cdd:cd07078 17 LPPAERAAILRKLADLLEERREELAALETLETGkPIEEALGEVARAADT-----FRYYAGLarrlhgEVIPSPDPGELAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 167 VRRQPDGVVCVNPPQNAPAPSAALAVLAL-MAGNAVVVRAPRSIALSTmyvlrDLVAPLLSELGAPAGTLNVVCGKPREM 245
Cdd:cd07078 92 VRREPLGVVGAITPWNFPLLLAAWKLAPAlAAGNTVVLKPSELTPLTA-----LLLAELLAEAGLPPGVLNVVTGDGDEV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 246 IDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVWHDA-DLALAAEAITECFFGSGQICMVPNYVI 324
Cdd:cd07078 167 GAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDAdLDAAVKGAVFGAFGNAGQVCTAASRLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 325 VHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPVRRSEKFFRLL---EQALSRGAQLVCGGDRIELDGtvsetGVFLQP 401
Cdd:cd07078 247 VHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLayiEDAKAEGAKLLCGGKRLEGGK-----GYFVPP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 402 TVLrVDGLAGARtvdAVRDETFFPLLPVVvpePMSDadlLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVGNGGLLk 481
Cdd:cd07078 322 TVL-TDVDPDMP---IAQEEIFGPVLPVI---PFKD---EEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVW- 390
|
410 420 430
....*....|....*....|....*....|....*....
gi 505433282 482 VNDSHIGFLPYLPT----HGGTGLTSGVHGEANYPILKT 516
Cdd:cd07078 391 INDYSVGAEPSAPFggvkQSGIGREGGPYGLEEYTEPKT 429
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
52-508 |
3.41e-47 |
|
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: 170.79 E-value: 3.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 52 EGRPDPEALHHPY---VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLGELFREALLRNRETFLDLLVAEA-HP 127
Cdd:pfam00171 3 DSESETIEVINPAtgeVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENgKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 128 RKLAEWEFScllqvYSPESISFYASQMH-----TEFAYGDRRLIVRRQPDGVVCVNPPQNAPAPSAALAVLAL-MAGNAV 201
Cdd:pfam00171 83 LAEARGEVD-----RAIDVLRYYAGLARrldgeTLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPAlAAGNTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 202 VVRAPRSIALSTMyvlrdLVAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKP 281
Cdd:pfam00171 158 VLKPSELTPLTAL-----LLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 282 ILELAGNDGVVVWHDA-DLALAAEAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV- 359
Cdd:pfam00171 233 TLELGGKNPLIVLEDAdLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLi 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 360 --RRSEKFFRLLEQALSRGAQLVCGGDRIEldgtvsETGVFLQPTVlrvdgLAGARTVDAV-RDETFFPLLPVVvpePMS 436
Cdd:pfam00171 313 skAQLERVLKYVEDAKEEGAKLLTGGEAGL------DNGYFVEPTV-----LANVTPDMRIaQEEIFGPVLSVI---RFK 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505433282 437 DadlLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVgNGGLLKVNDSHIGFLPYLPtHGGTGLtSGVHGE 508
Cdd:pfam00171 379 D---EEEAIEIANDTEYGLAAGVFTSDLERALRVARRL-EAGMVWINDYTTGDADGLP-FGGFKQ-SGFGRE 444
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
63-504 |
2.26e-37 |
|
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: 143.64 E-value: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 63 PY---VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLGELFREALLRNRETFLDLLVAEA-HPRKLAEWEFSCL 138
Cdd:cd07145 6 PAngeVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVgKPIKQSRVEVERT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 139 LQVYspESISFYASQMHTEF------AYGDRRLIV-RRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRAPRSIA 210
Cdd:cd07145 86 IRLF--KLAAEEAKVLRGETipvdayEYNERRIAFtVREPIGVVGAITPFNFPANLFAhKIAPAIAVGNSVVVKPSSNTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 211 LSTMYVlrdlvAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDG 290
Cdd:cd07145 164 LTAIEL-----AKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 291 VVVWHDADLALAAEAITEC-FFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDP----GVLLSP--VRRSE 363
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGrFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDEstdlGPLISPeaVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 364 KFfrlLEQALSRGAQLVCGGDRIEldgtvsetGVFLQPTVLRVDGlagaRTVDAVRDETFFPLLPVVvpePMSDAdllDR 443
Cdd:cd07145 319 NL---VNDAVEKGGKILYGGKRDE--------GSFFPPTVLENDT----PDMIVMKEEVFGPVLPIA---KVKDD---EE 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505433282 444 VIAYVNSNEYGLRNSLWSGSDEVVERFVREVGNGGLLkVNDS---HIGFLPYlpthGGTGLTSG 504
Cdd:cd07145 378 AVEIANSTEYGLQASVFTNDINRALKVARELEAGGVV-INDStrfRWDNLPF----GGFKKSGI 436
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
161-505 |
2.22e-35 |
|
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: 137.88 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 161 GDRRLIVRRQPDGVVCVNPPQNAPApsaalavlalmagNAVVVRAPRSIALSTMYVLRD---------LVAPLLSELGAP 231
Cdd:cd07146 110 KARKIFTLREPLGVVLAITPFNHPL-------------NQVAHKIAPAIAANNRIVLKPsektplsaiYLADLLYEAGLP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 232 AGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQgeCVARGKKPILELAGNDGVVVWHDADLALAAEAITE-CF 310
Cdd:cd07146 177 PDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIA--ATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAgSY 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 311 FGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPVRRSE---KFFRLLEQALSRGAQLVCGGDRie 387
Cdd:cd07146 255 ANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEaaiQIENRVEEAIAQGARVLLGNQR-- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 388 ldgtvseTGVFLQPTVL-RVDglagaRTVDAVRDETFFPLLPVVvpePMSDadlLDRVIAYVNSNEYGLRNSLWSGSDEV 466
Cdd:cd07146 333 -------QGALYAPTVLdHVP-----PDAELVTEETFGPVAPVI---RVKD---LDEAIAISNSTAYGLSSGVCTNDLDT 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 505433282 467 VERFVREVgNGGLLKVNDSHiGF-LPYLPTHG----GTGLTSGV 505
Cdd:cd07146 395 IKRLVERL-DVGTVNVNEVP-GFrSELSPFGGvkdsGLGGKEGV 436
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
65-498 |
2.38e-35 |
|
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: 137.56 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 65 VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLGELFREALLRNRETFLDLLVAE---AHPRKLAEWEfscllqv 141
Cdd:cd07103 9 VIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEqgkPLAEARGEVD------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 142 YSPESISFYASQmhTEFAYGD--------RRLIVRRQPDGVVCVNPPQN----------APAPSAalavlalmaGNAVVV 203
Cdd:cd07103 82 YAASFLEWFAEE--ARRIYGRtipspapgKRILVIKQPVGVVAAITPWNfpaamitrkiAPALAA---------GCTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 204 RAPRSIALSTMYVlrdlvAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPIL 283
Cdd:cd07103 151 KPAEETPLSALAL-----AELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 284 ELAGN---------------DGVVVWHdadlalaaeaitecFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGY 348
Cdd:cd07103 226 ELGGNapfivfddadldkavDGAIASK--------------FRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 349 PDDPGVLLSPV---RRSEKFFRLLEQALSRGAQLVCGGDRIELDGTvsetgvFLQPTVlrvdgLAGA-RTVDAVRDETFF 424
Cdd:cd07103 292 GLDEGTDMGPLineRAVEKVEALVEDAVAKGAKVLTGGKRLGLGGY------FYEPTV-----LTDVtDDMLIMNEETFG 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505433282 425 PLLPVVvpePMSDadlLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVR--EVGNGGllkVNDSHIGfLPYLPtHGG 498
Cdd:cd07103 361 PVAPII---PFDT---EDEVIARANDTPYGLAAYVFTRDLARAWRVAEalEAGMVG---INTGLIS-DAEAP-FGG 425
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
104-505 |
2.01e-34 |
|
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: 134.58 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 104 ELFREA---LLRNRETFLDLLVAEA-HPRKLAEWEFSCLLQVYSpESISFyASQMHTEF---AYGDRRLIVRRQPDGVVC 176
Cdd:cd07104 26 AILRKAaeiLEERRDEIADWLIRESgSTRPKAAFEVGAAIAILR-EAAGL-PRRPEGEIlpsDVPGKESMVRRVPLGVVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 177 VNPPQNAPAPSAA-LAVLALMAGNAVVV----RAPRSIALstmyvlrdLVAPLLSELGAPAGTLNVVCGKPREMIDRWLA 251
Cdd:cd07104 104 VISPFNFPLILAMrSVAPALALGNAVVLkpdsRTPVTGGL--------LIAEIFEEAGLPKGVLNVVPGGGSEIGDALVE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 252 HPGVNDIFYFGGSREG-LVfqGECVARG-KKPILELAGNDGVVV--------------WHDadlalaaeaitecFFGSGQ 315
Cdd:cd07104 176 HPRVRMISFTGSTAVGrHI--GELAGRHlKKVALELGGNNPLIVlddadldlavsaaaFGA-------------FLHQGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 316 ICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQALSRGAQLVCGGDRieldgtv 392
Cdd:cd07104 241 ICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLineRQVDRVHAIVEDAVAAGARLLTGGTY------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 393 seTGVFLQPTVLrVDGLAGARtvdAVRDETFFPLLPVVVpepmsdADLLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVR 472
Cdd:cd07104 314 --EGLFYQPTVL-SDVTPDMP---IFREEIFGPVAPVIP------FDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAE 381
|
410 420 430
....*....|....*....|....*....|...
gi 505433282 473 EVgNGGLLKVNDSHIGFLPYLPtHGGTGlTSGV 505
Cdd:cd07104 382 RL-ETGMVHINDQTVNDEPHVP-FGGVK-ASGG 411
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
94-475 |
4.74e-32 |
|
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: 128.84 E-value: 4.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 94 VPLPTRLRLGELFREALLRNRETFLDLLVAE-AHPRKLAEWEFscllqVYSPESISFYAS---QMHTEFAYGDRRL---- 165
Cdd:cd07082 58 MPLEERIDCLHKFADLLKENKEEVANLLMWEiGKTLKDALKEV-----DRTIDYIRDTIEelkRLDGDSLPGDWFPgtkg 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 166 ---IVRRQPDGVVCVNPPQNAPAPSAALAVL-ALMAGNAVVVRAPRSIALSTMYVLRdlvapLLSELGAPAGTLNVVCGK 241
Cdd:cd07082 133 kiaQVRREPLGVVLAIGPFNYPLNLTVSKLIpALIMGNTVVFKPATQGVLLGIPLAE-----AFHDAGFPKGVVNVVTGR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 242 PREMIDRWLAHPGVnDIFYFGGSREGlvfqGECVAR--GKKP-ILELAGNDGVVVwhdADLALAAEAITECFFG----SG 314
Cdd:cd07082 208 GREIGDPLVTHGRI-DVISFTGSTEV----GNRLKKqhPMKRlVLELGGKDPAIV---LPDADLELAAKEIVKGalsySG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 315 QICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV--RRSEKFFR-LLEQALSRGAQLVCGGDRieldgt 391
Cdd:cd07082 280 QRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLidPKSADFVEgLIDDAVAKGATVLNGGGR------ 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 392 vsETGVFLQPTVLRVDglagarTVDAV--RDETFFPLLPVVvpePMSDadlLDRVIAYVNSNEYGLRNSLWSGSDEVVER 469
Cdd:cd07082 354 --EGGNLIYPTLLDPV------TPDMRlaWEEPFGPVLPII---RVND---IEEAIELANKSNYGLQASIFTKDINKARK 419
|
....*...
gi 505433282 470 FVR--EVG 475
Cdd:cd07082 420 LADalEVG 427
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
113-494 |
1.03e-31 |
|
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: 127.81 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 113 NRETFLDLLVAEA---HPRKLAEWEFScllQVYSPESISFyASQMHTEFAYGD---RRLIVRRQPDGVVCVNPPQNAPAP 186
Cdd:cd07151 70 RRDEIVEWLIRESgstRIKANIEWGAA---MAITREAATF-PLRMEGRILPSDvpgKENRVYREPLGVVGVISPWNFPLH 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 187 SAALAVL-ALMAGNAVVVRAprsiALSTMYVLRDLVAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPgVNDIFYFGGSR 265
Cdd:cd07151 146 LSMRSVApALALGNAVVLKP----ASDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHP-VPRLISFTGST 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 266 EglVFQ--GECVARG-KKPILELAGNDGVVVWH-DADLALAAEAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAA 341
Cdd:cd07151 221 P--VGRhiGELAGRHlKKVALELGGNNPFVVLEdADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 342 AEIRPGYPDDPGVLLSPVRRSEKFFRLL---EQALSRGAQLVCGGDRieldgtvseTGVFLQPTVlrvdgLAGART-VDA 417
Cdd:cd07151 299 KALPYGDPSDPDTVVGPLINESQVDGLLdkiEQAVEEGATLLVGGEA---------EGNVLEPTV-----LSDVTNdMEI 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505433282 418 VRDETFFPLLPVVvpePMSDAdllDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVgNGGLLKVNDSHIGFLPYLP 494
Cdd:cd07151 365 AREEIFGPVAPII---KADDE---EEALELANDTEYGLSGAVFTSDLERGVQFARRI-DAGMTHINDQPVNDEPHVP 434
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
164-518 |
5.19e-31 |
|
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: 125.82 E-value: 5.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 164 RLIVRRQPDGVVCVNPPQN----------APAPSAalavlalmaGNAVVVRaPRSIALSTMYVLrdlvAPLLSELGAPAG 233
Cdd:cd07097 128 EVETTREPLGVVGLITPWNfpiaipawkiAPALAY---------GNTVVFK-PAELTPASAWAL----VEILEEAGLPAG 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 234 TLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAG-NDGVVVWHDADLALAAEAITECFFG 312
Cdd:cd07097 194 VFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGkNPLVVLDDADLDLAVECAVQGAFFS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 313 SGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQALSRGAQLVCGGDRIELD 389
Cdd:cd07097 274 TGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVvseRQLEKDLRYIEIARSEGAKLVYGGERLKRP 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 390 gtvsETGVFLQPTVLrVDGLAGARTvdaVRDETFFPLLPVVvpepmsDADLLDRVIAYVNSNEYGLRNSLWSGSDEVVER 469
Cdd:cd07097 354 ----DEGYYLAPALF-AGVTNDMRI---AREEIFGPVAAVI------RVRDYDEALAIANDTEFGLSAGIVTTSLKHATH 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 505433282 470 FVREVgNGGLLKVNDSHIGFLPYLPtHGGTGLTS------GVHGEANYPILKTSH 518
Cdd:cd07097 420 FKRRV-EAGVVMVNLPTAGVDYHVP-FGGRKGSSygpreqGEAALEFYTTIKTVY 472
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
166-498 |
2.16e-30 |
|
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: 123.59 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 166 IVRRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRAPRSIALSTMYvLRDLVAPLLselgaPAGTLNVVCGKPRE 244
Cdd:cd07092 113 MIRREPIGVVAQIAPWNYPLMMAAwKIAPALAAGNTVVLKPSETTPLTTLL-LAELAAEVL-----PPGVVNVVCGGGAS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 245 MIDRWLAHPGVNDIfyfggSREGLVFQGECVARG-----KKPILELAGNDGVVVWHDADLALAAEAITEC-FFGSGQICM 318
Cdd:cd07092 187 AGDALVAHPRVRMV-----SLTGSVRTGKKVARAaadtlKRVHLELGGKAPVIVFDDADLDAAVAGIATAgYYNAGQDCT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 319 VPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQAlSRGAQLVCGGDRIEldgtvsET 395
Cdd:cd07092 262 AACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLnsaAQRERVAGFVERA-PAHARVLTGGRRAE------GP 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 396 GVFLQPTVlrvdgLAGARTVDA-VRDETFFpllPVVVPEPMSDAdllDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREV 474
Cdd:cd07092 335 GYFYEPTV-----VAGVAQDDEiVQEEIFG---PVVTVQPFDDE---DEAIELANDVEYGLASSVWTRDVGRAMRLSARL 403
|
330 340
....*....|....*....|....
gi 505433282 475 gNGGLLKVNDsHIGFLPYLPtHGG 498
Cdd:cd07092 404 -DFGTVWVNT-HIPLAAEMP-HGG 424
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
149-511 |
2.80e-30 |
|
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: 123.23 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 149 FYASQMHTEFAYGDRRL---------IVRRQPDGVVCVNPPQNAPAPSAALAVLALMAGNAVVVRAPRSIALSTMYVLRD 219
Cdd:cd07110 89 YYADLAEQLDAKAERAVplpsedfkaRVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 220 LVApllsELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREG-LVFQGecVARGKKPI-LELAGNDGVVVWHDA 297
Cdd:cd07110 169 IAA----EAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGsQVMQA--AAQDIKPVsLELGGKSPIIVFDDA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 298 DLALAAEAIT-ECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQAL 373
Cdd:cd07110 243 DLEKAVEWAMfGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLvsqAQYEKVLSFIARGK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 374 SRGAQLVCGGDRIELdgtvSETGVFLQPTVLRvdglagARTVDAV--RDETFFPLLPVvvpepmSDADLLDRVIAYVNSN 451
Cdd:cd07110 323 EEGARLLCGGRRPAH----LEKGYFIAPTVFA------DVPTDSRiwREEIFGPVLCV------RSFATEDEAIALANDS 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505433282 452 EYGLRNSLWSGSDEVVERFVREVgNGGLLKVNDSHIGFlPYLPtHGGTGLTS-----GVHGEANY 511
Cdd:cd07110 387 EYGLAAAVISRDAERCDRVAEAL-EAGIVWINCSQPCF-PQAP-WGGYKRSGigrelGEWGLDNY 448
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
162-515 |
1.24e-29 |
|
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: 121.69 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 162 DRRLIVRRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRAPRSIALSTmyvlrDLVAPLLSELGAPAGTLNVVCG 240
Cdd:cd07131 126 NKDAMTRRQPIGVVALITPWNFPVAIPSwKIFPALVCGNTVVFKPAEDTPACA-----LKLVELFAEAGLPPGVVNVVHG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 241 KPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVWHDADLALAAEAITECFFG-SGQICMV 319
Cdd:cd07131 201 RGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGtTGQRCTA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 320 PNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQALSRGAQLVCGGDRIelDGTVSETG 396
Cdd:cd07131 281 TSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLineAQLEKVLNYNEIGKEEGATLLLGGERL--TGGGYEKG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 397 VFLQPTVLRVDglagARTVDAVRDETFFPLLPVVvpePMSDadlLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVgN 476
Cdd:cd07131 359 YFVEPTVFTDV----TPDMRIAQEEIFGPVVALI---EVSS---LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDL-E 427
|
330 340 350
....*....|....*....|....*....|....*....
gi 505433282 477 GGLLKVNDSHIGFLPYLPtHGGTGLTSGVHGEANYPILK 515
Cdd:cd07131 428 AGITYVNAPTIGAEVHLP-FGGVKKSGNGHREAGTTALD 465
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
65-461 |
2.24e-29 |
|
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: 120.83 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 65 VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLGELFREALLRNRETFLDLLVAE-AHPRKLAEWEfscllqvys 143
Cdd:cd07088 25 VVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEqGKTLSLARVE--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 144 pesISFYASQM--HTEFAY--------GDR---RLIVRRQPDGVVCVNPPQNAPAPSAAL-AVLALMAGNAVVVRAPRSI 209
Cdd:cd07088 96 ---VEFTADYIdyMAEWARriegeiipSDRpneNIFIFKVPIGVVAGILPWNFPFFLIARkLAPALVTGNTIVIKPSEET 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 210 ALSTMyvlrdLVAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGND 289
Cdd:cd07088 173 PLNAL-----EFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 290 GVVVWHDADLALAAEAITECFFG-SGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKF 365
Cdd:cd07088 248 PAIVMKDADLDLAVKAIVDSRIInCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLvneAALDKV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 366 FRLLEQALSRGAQLVCGGDRIELDGtvsetGVFLQPTVLR-VDGlagarTVDAVRDETFFPLLPVVvpePMSDadlLDRV 444
Cdd:cd07088 328 EEMVERAVEAGATLLTGGKRPEGEK-----GYFYEPTVLTnVRQ-----DMEIVQEEIFGPVLPVV---KFSS---LDEA 391
|
410
....*....|....*..
gi 505433282 445 IAYVNSNEYGLRNSLWS 461
Cdd:cd07088 392 IELANDSEYGLTSYIYT 408
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
60-485 |
2.25e-29 |
|
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: 120.78 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 60 LHHPY---VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLgeLFREA--LLRNRETFLDLLVAEA-HPRKLAEW 133
Cdd:cd07149 3 VISPYdgeVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEI--LERAAqlLEERREEFARTIALEAgKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 134 EFSCLLQVY--SPESisfyASQMHTE------FAYGDRRL-IVRRQPDGVVCV----NPPQN------APAPSAalavla 194
Cdd:cd07149 81 EVDRAIETLrlSAEE----AKRLAGEtipfdaSPGGEGRIgFTIREPIGVVAAitpfNFPLNlvahkvGPAIAA------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 195 lmaGNAVVVRAPRSIALSTMyvlrdLVAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIfYFGGSREglvfQGEC 274
Cdd:cd07149 151 ---GNAVVLKPASQTPLSAL-----KLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMI-SFTGSPA----VGEA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 275 VARG---KKPILELAGNDGVVVwhdADLALAAEAITECFFG----SGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPG 347
Cdd:cd07149 218 IARKaglKKVTLELGSNAAVIV---DADADLEKAVERCVSGafanAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 348 YPDDPGVLLSP------VRRSEKFfrlLEQALSRGAQLVCGGDRIeldgtvsetGVFLQPTVL-RVDglagaRTVDAVRD 420
Cdd:cd07149 295 DPLDEDTDVGPmiseaeAERIEEW---VEEAVEGGARLLTGGKRD---------GAILEPTVLtDVP-----PDMKVVCE 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505433282 421 ETFfplLPVVVPEPMSDadlLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVGNGGLLkVNDS 485
Cdd:cd07149 358 EVF---APVVSLNPFDT---LDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVM-INDS 415
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
65-509 |
3.81e-29 |
|
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: 120.02 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 65 VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLGELFREALLRNRETFLDLLVAE-AHPRKLAEWEFscllqVYS 143
Cdd:cd07099 8 VLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAEtGKPRADAGLEV-----LLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 144 PESISFYASQ---------MHTEFAYGDRRLIVRRQPDGVVCVNPPQNAPAPSAALAVLAL-MAGNAVVV----RAPRSI 209
Cdd:cd07099 83 LEAIDWAARNaprvlaprkVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPAlAAGNAVVLkpseVTPLVG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 210 ALstmyvlrdlVAPLLSELGAPAGTLNVVCGKP---REMIDRwlahpGVNDIFYFGGSREGLVFQGECVARGKKPILELA 286
Cdd:cd07099 163 EL---------LAEAWAAAGPPQGVLQVVTGDGatgAALIDA-----GVDKVAFTGSVATGRKVMAAAAERLIPVVLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 287 GNDGVVVWHDADLALAAEAIT-ECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRS 362
Cdd:cd07099 229 GKDPMIVLADADLERAAAAAVwGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMttaRQL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 363 EKFFRLLEQALSRGAQLVCGGDRIELDGTvsetgvFLQPTVL-RVDglagaRTVDAVRDETFFPLLPVVvpePMSDAdll 441
Cdd:cd07099 309 DIVRRHVDDAVAKGAKALTGGARSNGGGP------FYEPTVLtDVP-----HDMDVMREETFGPVLPVM---PVADE--- 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505433282 442 DRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVgNGGLLKVNDsHIGF--LPYLPtHGGTGLTSG--VHGEA 509
Cdd:cd07099 372 DEAIALANDSRYGLSASVFSRDLARAEAIARRL-EAGAVSIND-VLLTagIPALP-FGGVKDSGGgrRHGAE 440
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
65-487 |
4.30e-29 |
|
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: 119.74 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 65 VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLGELFREALLRNRETFLDLLVAEA-HPRKLAEWEFscllqVYS 143
Cdd:cd07150 11 VYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGgSTYGKAWFET-----TFT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 144 PESISFYASQMHTEFA------YGDRRLIVRRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRaPRSIAlstmYV 216
Cdd:cd07150 86 PELLRAAAGECRRVRGetlpsdSPGTVSMSVRRPLGVVAGITPFNYPLILATkKVAFALAAGNTVVLK-PSEET----PV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 217 LRDLVAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVWH- 295
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLAd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 296 DADLALAAEAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQA 372
Cdd:cd07150 241 ADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLispRQVERIKRQVEDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 373 LSRGAQLVCGGdrieldgtvSETGVFLQPTVLR-VDglagaRTVDAVRDETFFPLLPVVvpePMSDAdllDRVIAYVNSN 451
Cdd:cd07150 321 VAKGAKLLTGG---------KYDGNFYQPTVLTdVT-----PDMRIFREETFGPVTSVI---PAKDA---EEALELANDT 380
|
410 420 430
....*....|....*....|....*....|....*.
gi 505433282 452 EYGLRNSLWSGSDEVVERFVREVgNGGLLKVNDSHI 487
Cdd:cd07150 381 EYGLSAAILTNDLQRAFKLAERL-ESGMVHINDPTI 415
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
166-461 |
5.18e-29 |
|
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: 119.22 E-value: 5.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 166 IVRRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRA----PRsialsTMYvlrdLVAPLLSELGAPAGTLNVVCG 240
Cdd:cd07105 93 MVVKEPVGVVLGIAPWNAPVILGTrAIAYPLAAGNTVVLKAselsPR-----THW----LIGRVFHEAGLPKGVLNVVTH 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 241 KP---REMIDRWLAHPGVNDIFYFGGSREGLVFQGECvARGKKP-ILELAGNDGVVVWHDADLALAAEAITE-CFFGSGQ 315
Cdd:cd07105 164 SPedaPEVVEALIAHPAVRKVNFTGSTRVGRIIAETA-AKHLKPvLLELGGKAPAIVLEDADLDAAANAALFgAFLNSGQ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 316 ICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGyPDDPGVLLSP--VRRSEkffRLLEQALSRGAQLVCGGDRIEldgtvS 393
Cdd:cd07105 243 ICMSTERIIVHESIADEFVEKLKAAAEKLFAG-PVVLGSLVSAaaADRVK---ELVDDALSKGAKLVVGGLADE-----S 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505433282 394 ETGVFLQPTVLrvDGLagARTVDAVRDETFFPLLPVVVPEpmSDADlldrVIAYVNSNEYGLRNSLWS 461
Cdd:cd07105 314 PSGTSMPPTIL--DNV--TPDMDIYSEESFGPVVSIIRVK--DEEE----AVRIANDSEYGLSAAVFT 371
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
145-488 |
8.63e-29 |
|
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: 119.21 E-value: 8.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 145 ESISFYASQMHTEFAygDRRLIVRRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRAPRSIALSTMYVLRdLVAP 223
Cdd:cd07086 109 LSRMLYGLTIPSERP--GHRLMEQWNPLGVVGVITAFNFPVAVPGwNAAIALVCGNTVVWKPSETTPLTAIAVTK-ILAE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 224 LLSELGAPAGTLNVVCGkPREmIDRWLAHPGVNDIFYFGGSRE-GLVFQGECVARGKKPILELAGNDGVVVWHDADLALA 302
Cdd:cd07086 186 VLEKNGLPPGVVNLVTG-GGD-GGELLVHDPRVPLVSFTGSTEvGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 303 AEAITECFFG-SGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV--RRS-EKFFRLLEQALSRGAQ 378
Cdd:cd07086 264 VRAVLFAAVGtAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLinQAAvEKYLNAIEIAKSQGGT 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 379 LVCGGDRIeldgTVSETGVFLQPTVLRVDglagARTVDAVRDETFFPLLPVVvpepmsDADLLDRVIAYVNSNEYGLRNS 458
Cdd:cd07086 344 VLTGGKRI----DGGEPGNYVEPTIVTGV----TDDARIVQEETFAPILYVI------KFDSLEEAIAINNDVPQGLSSS 409
|
330 340 350
....*....|....*....|....*....|.
gi 505433282 459 LWSGSDEVVERFVREVG-NGGLLKVNDSHIG 488
Cdd:cd07086 410 IFTEDLREAFRWLGPKGsDCGIVNVNIPTSG 440
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
65-465 |
1.09e-28 |
|
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: 118.40 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 65 VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLGELFREALLRNRETFLDLLVAEA-HPRKLAEWEFScllqvYS 143
Cdd:cd07106 9 VFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQgKPLAEAQFEVG-----GA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 144 PESISFYASQMHTEFAYGD---RRLIVRRQPDGVVCVNPPQNAPAPSAAL-AVLALMAGNAVVVRAPRSIALSTMyvlrd 219
Cdd:cd07106 84 VAWLRYTASLDLPDEVIEDddtRRVELRRKPLGVVAAIVPWNFPLLLAAWkIAPALLAGNTVVLKPSPFTPLCTL----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 220 lvapLLSELGA---PAGTLNVVCGKPRemIDRWL-AHPGVNDIfYFGGSREglvfQGECVARG-----KKPILELAGNDG 290
Cdd:cd07106 159 ----KLGELAQevlPPGVLNVVSGGDE--LGPALtSHPDIRKI-SFTGSTA----TGKKVMASaaktlKRVTLELGGNDA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 291 VVVWHDADLALAAEAITE-CFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPVRRS---EKFF 366
Cdd:cd07106 228 AIVLPDVDIDAVAPKLFWgAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKmqyDKVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 367 RLLEQALSRGAQLVCGGDRIELDgtvsetGVFLQPTVLRvDGLAGARTVDavrDETFFPLLPVVvpePMSDadlLDRVIA 446
Cdd:cd07106 308 ELVEDAKAKGAKVLAGGEPLDGP------GYFIPPTIVD-DPPEGSRIVD---EEQFGPVLPVL---KYSD---EDEVIA 371
|
410
....*....|....*....
gi 505433282 447 YVNSNEYGLRNSLWSgSDE 465
Cdd:cd07106 372 RANDSEYGLGASVWS-SDL 389
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
106-507 |
6.97e-28 |
|
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: 116.19 E-value: 6.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 106 FREALLRNRETFLDLLVAEA-HPRKLAEwefscLLQVYSPESISFYASQMHTEFAY-----------GDRRLIVRRQPDG 173
Cdd:cd07089 51 LHEALEARKEELRALLVAEVgAPVMTAR-----AMQVDGPIGHLRYFADLADSFPWefdlpvpalrgGPGRRVVRREPVG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 174 VVCVNPPQNAPAPSAAL-AVLALMAGNAVVVR-APRSiALSTMyvlrdLVAPLLSELGAPAGTLNVVCGKPREMIDRWLA 251
Cdd:cd07089 126 VVAAITPWNFPFFLNLAkLAPALAAGNTVVLKpAPDT-PLSAL-----LLGEIIAETDLPAGVVNVVTGSDNAVGEALTT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 252 HPGVnDIFYFGGSRE-GLVFQGECVARGKKPILELAGNDGVVVWH-DADLALAAEAITECFFGSGQICMVPNYVIVHPAV 329
Cdd:cd07089 200 DPRV-DMVSFTGSTAvGRRIMAQAAATLKRVLLELGGKSANIVLDdADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 330 AEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQALSRGAQLVCGGDRIE-LDgtvseTGVFLQPTVLr 405
Cdd:cd07089 279 YDEVVEALAAAFEALPVGDPADPGTVMGPLisaAQRDRVEGYIARGRDEGARLVTGGGRPAgLD-----KGFYVEPTLF- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 406 vDGLAGARTVdaVRDETFFPLLpVVVPepmsdADLLDRVIAYVNSNEYGLRNSLWSGSdevVERFVR--------EVG-N 476
Cdd:cd07089 353 -ADVDNDMRI--AQEEIFGPVL-VVIP-----YDDDDEAVRIANDSDYGLSGGVWSAD---VDRAYRvarrirtgSVGiN 420
|
410 420 430
....*....|....*....|....*....|....*
gi 505433282 477 GGllkvndshIGFLPYLPTHG----GTGLTSGVHG 507
Cdd:cd07089 421 GG--------GGYGPDAPFGGykqsGLGRENGIEG 447
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
151-518 |
2.03e-27 |
|
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: 115.13 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 151 ASQMHTEfAY---GDRRL-IVRRQPDGVVCVNPPQNAPAPSAALAVL-ALMAGNAVVVRAPRSIALSTMyvlrdLVAPLL 225
Cdd:cd07118 96 ARTLHGD-SYnnlGDDMLgLVLREPIGVVGIITPWNFPFLILSQKLPfALAAGCTVVVKPSEFTSGTTL-----MLAELL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 226 SELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVWHDADLALAAEA 305
Cdd:cd07118 170 IEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 306 IT-ECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDP----GVLLSPvRRSEKFFRLLEQALSRGAQLV 380
Cdd:cd07118 250 VVfGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPetkvGAIINE-AQLAKITDYVDAGRAEGATLL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 381 CGGDRIEldgtvSETGVFLQPTVLR-VdglagARTVDAVRDETFFPLLPVVVpepmsdADLLDRVIAYVNSNEYGLRNSL 459
Cdd:cd07118 329 LGGERLA-----SAAGLFYQPTIFTdV-----TPDMAIAREEIFGPVLSVLT------FDTVDEAIALANDTVYGLSAGV 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505433282 460 WSGSDEVVERFVREVgNGGLLKVNDSHIGFlPYLPTHG----GTGLTSGVHGEANYPILKTSH 518
Cdd:cd07118 393 WSKDIDTALTVARRI-RAGTVWVNTFLDGS-PELPFGGfkqsGIGRELGRYGVEEYTELKTVH 453
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
59-497 |
3.50e-27 |
|
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: 114.07 E-value: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 59 ALHHPY---VVGRCAVAGAGEIEESLDAATAAAAGWAAvpLPTRLRLGELFREA--LLRNRETFLDLLVAEA-HPRKLAE 132
Cdd:cd07094 2 DVHNPYdgeVIGKVPADDRADAEEALATARAGAENRRA--LPPHERMAILERAAdlLKKRAEEFAKIIACEGgKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 133 WEFS-CL--LQVYSPESISFYASQ--MHTEFAYGDRRLIVRRQPDGVVCVNPPQNAPAPSAALAVLALMAGNAVVVRAPR 207
Cdd:cd07094 80 VEVDrAIdtLRLAAEEAERIRGEEipLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 208 SIALSTMYVLrdlvAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIfYFGGSREglvfQGECVAR---GKKPILE 284
Cdd:cd07094 160 SKTPLSALEL----AKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAML-SFTGSAA----VGEALRAnagGKRIALE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 285 LAGNDGVVVWHDA-DLALAAEAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYP----DDPGVLLSPv 359
Cdd:cd07094 231 LGGNAPVIVDRDAdLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPldedTDVGPLISE- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 360 RRSEKFFRLLEQALSRGAQLVCGGDRielDGTVsetgvfLQPTVLRVDglagARTVDAVRDETFFPLLPVVvpepmsDAD 439
Cdd:cd07094 310 EAAERVERWVEEAVEAGARLLCGGER---DGAL------FKPTVLEDV----PRDTKLSTEETFGPVVPII------RYD 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 505433282 440 LLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVGNGGLLkVNDSHIGFLPYLPTHG 497
Cdd:cd07094 371 DFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVM-VNDSSAFRTDWMPFGG 427
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
198-519 |
6.40e-27 |
|
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: 113.95 E-value: 6.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRAPRSIALSTMYVLRdlvapLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVAR 277
Cdd:cd07119 162 GNTVVIKPSEVTPLTTIALFE-----LIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 278 GKKPILELAGNDGVVVWHDA-DLALAAEAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLL 356
Cdd:cd07119 237 VKKVALELGGKNPNIVFADAdFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEM 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 357 SPVRRSE---KFFRLLEQALSRGAQLVCGGDRieLDGTVSETGVFLQPTVL-RVDglagaRTVDAVRDETFFpllPVVVP 432
Cdd:cd07119 317 GPLVSAEhreKVLSYIQLGKEEGARLVCGGKR--PTGDELAKGYFVEPTIFdDVD-----RTMRIVQEEIFG---PVLTV 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 433 EPMSDAdllDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVgNGGLLKVNDSHigflPYLPT-------HGGTGLTSGV 505
Cdd:cd07119 387 ERFDTE---EEAIRLANDTPYGLAGAVWTKDIARANRVARRL-RAGTVWINDYH----PYFAEapwggykQSGIGRELGP 458
|
330
....*....|....
gi 505433282 506 HGEANYPILKTSHQ 519
Cdd:cd07119 459 TGLEEYQETKHINI 472
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
198-483 |
8.14e-27 |
|
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: 113.08 E-value: 8.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRAPRSIALSTmyvLRdlVAPLLSELGAPAGTLNVVCGKPREmIDRWLA-HPGVNDIFYFGGSREG---LVFQGE 273
Cdd:cd07112 152 GNSVVLKPAEQSPLTA---LR--LAELALEAGLPAGVLNVVPGFGHT-AGEALGlHMDVDALAFTGSTEVGrrfLEYSGQ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 274 cvARGKKPILELAGNDGVVVWHDADLALAAEAITE--CFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDD 351
Cdd:cd07112 226 --SNLKRVWLECGGKSPNIVFADAPDLDAAAEAAAagIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLD 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 352 PGVLLSPV---RRSEKFFRLLEQALSRGAQLVCGGDRIELDGtvseTGVFLQPTVLrvDGLAGARTVdaVRDETFFPLLP 428
Cdd:cd07112 304 PATRMGALvseAHFDKVLGYIESGKAEGARLVAGGKRVLTET----GGFFVEPTVF--DGVTPDMRI--AREEIFGPVLS 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 505433282 429 VvvpepmSDADLLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVgNGGLLKVN 483
Cdd:cd07112 376 V------ITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRL-RAGTVWVN 423
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
65-483 |
1.31e-26 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 113.00 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 65 VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLGELFREALLRNRETFLDLLVAEaHPRKLAE-----------W 133
Cdd:cd07085 28 VIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLE-HGKTLADargdvlrglevV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 134 EFSC----LLQVYSPESIsfyASQMHTEfaygdrrliVRRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRAPRS 208
Cdd:cd07085 107 EFACsiphLLKGEYLENV---ARGIDTY---------SYRQPLGVVAGITPFNFPAMIPLwMFPMAIACGNTFVLKPSER 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 209 IALSTMYVlrdlvAPLLSELGAPAGTLNVVCGKpREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKpILELAG- 287
Cdd:cd07085 175 VPGAAMRL-----AELLQEAGLPDGVLNVVHGG-KEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR-VQALGGa 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 288 -NDGVVVwHDADLALAAEAITECFFGS-GQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV--RRS- 362
Cdd:cd07085 248 kNHAVVM-PDADLEQTANALVGAAFGAaGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVisPAAk 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 363 EKFFRLLEQALSRGAQLVCGGDRIELDGtvSETGVFLQPTVLrvDGLAGarTVDAVRDETFFPLLPVVvpepmsDADLLD 442
Cdd:cd07085 327 ERIEGLIESGVEEGAKLVLDGRGVKVPG--YENGNFVGPTIL--DNVTP--DMKIYKEEIFGPVLSIV------RVDTLD 394
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 505433282 443 RVIAYVNSNEYGLRNSLWSGSDEVVERFVREVgNGGLLKVN 483
Cdd:cd07085 395 EAIAIINANPYGNGAAIFTRSGAAARKFQREV-DAGMVGIN 434
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
167-511 |
2.32e-26 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 112.52 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 167 VRRQPDGVVCVNPPQNAPAPSAALAVLALMAGNAVVVRAPRSIALSTMYVLRDLVApllsELGAPAGTLNVVCGKPREMI 246
Cdd:PLN02467 147 VLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICR----EVGLPPGVLNVVTGLGTEAG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 247 DRWLAHPGVNDIFYFGGSREGLVFQGECvARGKKPI-LELAGNDGVVVWHDADLALAAE-AITECFFGSGQICMVPNYVI 324
Cdd:PLN02467 223 APLASHPGVDKIAFTGSTATGRKIMTAA-AQMVKPVsLELGGKSPIIVFDDVDLDKAVEwAMFGCFWTNGQICSATSRLL 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 325 VHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQALSRGAQLVCGGDRieldGTVSETGVFLQP 401
Cdd:PLN02467 302 VHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVvseGQYEKVLKFISTAKSEGATILCGGKR----PEHLKKGFFIEP 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 402 TVlrvdgLAGARTVDAV-RDETFFPLLpvVVPEPMSDadllDRVIAYVNSNEYGLRNSLWSGSDEVVERfVREVGNGGLL 480
Cdd:PLN02467 378 TI-----ITDVTTSMQIwREEVFGPVL--CVKTFSTE----DEAIELANDSHYGLAGAVISNDLERCER-VSEAFQAGIV 445
|
330 340 350
....*....|....*....|....*....|....*
gi 505433282 481 KVNDSHIGFLpYLPTHG----GTGLTSGVHGEANY 511
Cdd:PLN02467 446 WINCSQPCFC-QAPWGGikrsGFGRELGEWGLENY 479
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
168-490 |
4.78e-26 |
|
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: 110.93 E-value: 4.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 168 RRQPDGVVCVNPPQNAPAP-SAALAVLALMAGNAVVVRAPRSIALSTMyvlrdLVAPLLSELgAPAGTLNVVCGKPREMI 246
Cdd:cd07107 113 LREPYGVVARIVAFNHPLMfAAAKIAAPLAAGNTVVVKPPEQAPLSAL-----RLAELAREV-LPPGVFNILPGDGATAG 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 247 DRWLAHPGVNDIFYFGGSREGLVFQgECVARGKKPI-LELAGNDGVVVWHDADLALAAEAITEC--FFGSGQICMVPNYV 323
Cdd:cd07107 187 AALVRHPDVKRIALIGSVPTGRAIM-RAAAEGIKHVtLELGGKNALIVFPDADPEAAADAAVAGmnFTWCGQSCGSTSRL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 324 IVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQALSRGAQLVCGGDRIEldGTVSETGVFLQ 400
Cdd:cd07107 266 FVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLvsrQQYDRVMHYIDSAKREGARLVTGGGRPE--GPALEGGFYVE 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 401 PTVLrVDGLAGARTvdaVRDETFFPLLPVVvpePMSDadlLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVgNGGLL 480
Cdd:cd07107 344 PTVF-ADVTPGMRI---AREEIFGPVLSVL---RWRD---EAEMVAQANGVEYGLTAAIWTNDISQAHRTARRV-EAGYV 412
|
330
....*....|
gi 505433282 481 KVNDSHIGFL 490
Cdd:cd07107 413 WINGSSRHFL 422
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
65-476 |
1.46e-25 |
|
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: 110.00 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 65 VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLgeLFREA-LLRNRETFLD-LLVAEA-HPRKLAEWEFScllqv 141
Cdd:cd07124 59 VLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARL--LLRAAaLLRRRRFELAaWMVLEVgKNWAEADADVA----- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 142 yspESISF---YASQMH--TEFAYGDRRLIVRR---QPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRaPRSIALS 212
Cdd:cd07124 132 ---EAIDFleyYAREMLrlRGFPVEMVPGEDNRyvyRPLGVGAVISPWNFPLAILAgMTTAALVTGNTVVLK-PAEDTPV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 213 TMYvlrdLVAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVnDIFYFGGSRE-GLVFQGEC--VARG----KKPILEL 285
Cdd:cd07124 208 IAA----KLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDV-RFIAFTGSREvGLRIYERAakVQPGqkwlKRVIAEM 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 286 AGNDGVVVWHDADLALAAEAITECFFG-SGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RR 361
Cdd:cd07124 283 GGKNAIIVDEDADLDEAAEGIVRSAFGfQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVidkGA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 362 SEKFFRLLEQALSRGaQLVCGGDRIELDgtvsETGVFLQPTVLrVDGLAGARTvdaVRDETFFPLLPVVvpepmsDADLL 441
Cdd:cd07124 363 RDRIRRYIEIGKSEG-RLLLGGEVLELA----AEGYFVQPTIF-ADVPPDHRL---AQEEIFGPVLAVI------KAKDF 427
|
410 420 430
....*....|....*....|....*....|....*..
gi 505433282 442 DRVIAYVNSNEYGLRNSLWSGSDEVVERFVRE--VGN 476
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREfeVGN 464
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
167-477 |
2.03e-25 |
|
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: 109.07 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 167 VRRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRAPRSIALSTmyvLRdlVAPLLSELGAPAGTLNVVCGKPREM 245
Cdd:cd07115 113 TVREPVGVVGAIVPWNFPLMFAAwKVAPALAAGNTVVLKPAELTPLSA---LR--IAELMAEAGFPAGVLNVVTGFGEVA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 246 IDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVW-HDADLALAAEAITECFFGSGQICMVPNYVI 324
Cdd:cd07115 188 GAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFaDADLDAAVRAAATGIFYNQGQMCTAGSRLL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 325 VHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPVRRSEKFFRLL---EQALSRGAQLVCGGDRIeldgtvSETGVFLQP 401
Cdd:cd07115 268 VHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLdyvDVGREEGARLLTGGKRP------GARGFFVEP 341
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505433282 402 TVlrvdgLAGARTVDAV-RDETFFPLLPVVVPEPMSDAdlldrvIAYVNSNEYGLRNSLWSGSDEVVERFVREVGNG 477
Cdd:cd07115 342 TI-----FAAVPPEMRIaQEEIFGPVVSVMRFRDEEEA------LRIANGTEYGLAAGVWTRDLGRAHRVAAALKAG 407
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
95-508 |
7.85e-25 |
|
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: 106.16 E-value: 7.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 95 PLPTRLRLGELFREALLRNRETFLDLLVAEAH-PRKLAEWEFSCLLQVyspesISFYASQ------MHTEFAYGDRRLIV 167
Cdd:cd06534 14 PPAERAAILRKIADLLEERREELAALETLETGkPIEEALGEVARAIDT-----FRYAAGLadklggPELPSPDPGGEAYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 168 RRQPDGVVCVNPPQNAPAPSAALAVLAL-MAGNAVVVRAPRSIALSTmyvlrDLVAPLLSELGAPAGTLNVVCGKPREMI 246
Cdd:cd06534 89 RREPLGVVGVITPWNFPLLLAAWKLAPAlAAGNTVVLKPSELTPLTA-----LALAELLQEAGLPPGVVNVVPGGGDEVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 247 DRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVWHDADLALAAEAI-TECFFGSGQICMVPNYVIV 325
Cdd:cd06534 164 AALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAvFGAFFNAGQICTAASRLLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 326 HPAVAEELLDLVVKaaaeirpgypddpgvLLSPVRRSEKFfrlleqalsrgaqlvcggdrieldgtvsetgvflqptvlr 405
Cdd:cd06534 244 HESIYDEFVEKLVT---------------VLVDVDPDMPI---------------------------------------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 406 vdglagartvdaVRDETFFPLLPVVVpepmsdADLLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVGNGGLLkVNDS 485
Cdd:cd06534 269 ------------AQEEIFGPVLPVIR------FKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVY-INDS 329
|
410 420
....*....|....*....|...
gi 505433282 486 HIGFLPYLPtHGGTGLtSGVHGE 508
Cdd:cd06534 330 SIGVGPEAP-FGGVKN-SGIGRE 350
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
65-500 |
1.09e-24 |
|
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: 106.61 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 65 VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRlrlGELFREA---LLRNRETFLDLLVAEAHP-RKLAEWEFSCLLQ 140
Cdd:cd07152 3 VLGEVGVADAADVDRAAARAAAAQRAWAATPPRER---AAVLRRAadlLEEHADEIADWIVRESGSiRPKAGFEVGAAIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 141 VYspesisFYASQMHTE-----FAYGDRRL-IVRRQPDGVVCVNPPQNAPAPSAALAVL-ALMAGNAVVVR-APRSiALS 212
Cdd:cd07152 80 EL------HEAAGLPTQpqgeiLPSAPGRLsLARRVPLGVVGVISPFNFPLILAMRSVApALALGNAVVLKpDPRT-PVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 213 TMYVLrdlvAPLLSELGAPAGTLNVVCGKPrEMIDRWLAHPGVNDIFYFGGSREGLVFqGECVARG-KKPILELAGNDGV 291
Cdd:cd07152 153 GGVVI----ARLFEEAGLPAGVLHVLPGGA-DAGEALVEDPNVAMISFTGSTAVGRKV-GEAAGRHlKKVSLELGGKNAL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 292 VVWHDADLALAAEAIT-ECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFR 367
Cdd:cd07152 227 IVLDDADLDLAASNGAwGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLinaRQLDRVHA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 368 LLEQALSRGAQLVCGGDRieldgtvseTGVFLQPTVLrVDGLAGARtvdAVRDETFFPLLPVVVpepmsdADLLDRVIAY 447
Cdd:cd07152 307 IVDDSVAAGARLEAGGTY---------DGLFYRPTVL-SGVKPGMP---AFDEEIFGPVAPVTV------FDSDEEAVAL 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 505433282 448 VNSNEYGLRNSLWSGSdevVERFVR--EVGNGGLLKVNDSHIGFLPYLPtHGGTG 500
Cdd:cd07152 368 ANDTEYGLSAGIISRD---VGRAMAlaDRLRTGMLHINDQTVNDEPHNP-FGGMG 418
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
139-488 |
1.40e-24 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 107.08 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 139 LQVYSPESISFYASQMHTEFAygDRRLIVRRQPDGVVCVNPPQNAPApsaalavlalmagnAVVVR--APRSIALSTMYV 216
Cdd:PLN02278 130 LEYFAEEAKRVYGDIIPSPFP--DRRLLVLKQPVGVVGAITPWNFPL--------------AMITRkvGPALAAGCTVVV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 217 ----LRDLVAPLLSEL----GAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGN 288
Cdd:PLN02278 194 kpseLTPLTALAAAELalqaGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGN 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 289 DGVVVWH-DADLALAAEAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEK 364
Cdd:PLN02278 274 APFIVFDdADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLineAAVQK 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 365 FFRLLEQALSRGAQLVCGGDRIELDGTvsetgvFLQPTVLrvdglaGARTVDAV--RDETFFPLLPVVVPEPMSDAdlld 442
Cdd:PLN02278 354 VESHVQDAVSKGAKVLLGGKRHSLGGT------FYEPTVL------GDVTEDMLifREEVFGPVAPLTRFKTEEEA---- 417
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 505433282 443 rvIAYVNSNEYGLRNSLWSGSDEVVERFVREVGNgGLLKVNDSHIG 488
Cdd:PLN02278 418 --IAIANDTEAGLAAYIFTRDLQRAWRVSEALEY-GIVGVNEGLIS 460
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
60-455 |
2.59e-24 |
|
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: 105.79 E-value: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 60 LHHPY---VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLGELFREALLRNRETFLDLLVAEA-HPRKLAEWEF 135
Cdd:cd07147 3 VTNPYtgeVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAgKPIKDARGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 136 SCLL---QVYSPESISFYASQMHTE-FAYGD-RRLIVRRQPDGVVCVNPPQN----------APAPSAalavlalmaGNA 200
Cdd:cd07147 83 ARAIdtfRIAAEEATRIYGEVLPLDiSARGEgRQGLVRRFPIGPVSAITPFNfplnlvahkvAPAIAA---------GCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 201 VVVRAPRSIALSTMyvlrdLVAPLLSELGAPAGTLNVV-CgkPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECvarGK 279
Cdd:cd07147 154 FVLKPASRTPLSAL-----ILGEVLAETGLPKGAFSVLpC--SRDDADLLVTDERIKLLSFTGSPAVGWDLKARA---GK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 280 KPI-LELAGNDGVVVWHDADLALAAEAITECFFG-SGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLS 357
Cdd:cd07147 224 KKVvLELGGNAAVIVDSDADLDFAAQRIIFGAFYqAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 358 PV---RRSEKFFRLLEQALSRGAQLVCGGDRieldgtvseTGVFLQPTVL-RVDglagaRTVDAVRDETFfplLPVVVPE 433
Cdd:cd07147 304 PMiseSEAERVEGWVNEAVDAGAKLLTGGKR---------DGALLEPTILeDVP-----PDMEVNCEEVF---GPVVTVE 366
|
410 420
....*....|....*....|..
gi 505433282 434 PMSDadlLDRVIAYVNSNEYGL 455
Cdd:cd07147 367 PYDD---FDEALAAVNDSKFGL 385
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
168-505 |
7.06e-24 |
|
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: 104.83 E-value: 7.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 168 RRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRaPRSIALSTMyvLRdlVAPLLSELGAPAGTLNVVCGK---PR 243
Cdd:cd07113 139 RREPVGVVAGIVPWNFSVMIAVwKIGAALATGCTIVIK-PSEFTPLTL--LR--VAELAKEAGIPDGVLNVVNGKgavGA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 244 EMIDrwlaHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVWHDADLALAAEAITEC-FFGSGQICMVPNY 322
Cdd:cd07113 214 QLIS----HPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAgFLHQGQVCAAPER 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 323 VIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPVRRS---EKFFRLLEQALSRGAQLVCGGdrieldGTVSETGVFL 399
Cdd:cd07113 290 FYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQphfDKVCSYLDDARAEGDEIVRGG------EALAGEGYFV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 400 QPTVLRvdglagARTVDA--VRDETFFPLLPVVvpePMSDADLLdrvIAYVNSNEYGLRNSLWSGSDEVVERFVREVgNG 477
Cdd:cd07113 364 QPTLVL------ARSADSrlMREETFGPVVSFV---PYEDEEEL---IQLINDTPFGLTASVWTNNLSKALRYIPRI-EA 430
|
330 340
....*....|....*....|....*...
gi 505433282 478 GLLKVNdSHIGFLPYLPTHGGTGltSGV 505
Cdd:cd07113 431 GTVWVN-MHTFLDPAVPFGGMKQ--SGI 455
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
150-483 |
1.21e-23 |
|
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: 103.80 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 150 YASQMHTEFAYGDRRLI--VRRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRaPRSIALSTMYVLrdlvAPLLS 226
Cdd:cd07093 94 YILQLDGESYPQDGGALnyVLRQPVGVAGLITPWNLPLMLLTwKIAPALAFGNTVVLK-PSEWTPLTAWLL----AELAN 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 227 ELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQgECVARGKKPI-LELAGNDGVVVWHDADLALAAEA 305
Cdd:cd07093 169 EAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIM-RAAAPNLKPVsLELGGKNPNIVFADADLDRAVDA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 306 ITECFFG-SGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDP----GVLLSPVRRsEKFFRLLEQALSRGAQLV 380
Cdd:cd07093 248 AVRSSFSnNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPdtevGPLISKEHL-EKVLGYVELARAEGATIL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 381 CGGDRIELDGTvsETGVFLQPTVLRvdGLAGARTVdaVRDETFFpllPVVVPEPMSDAdllDRVIAYVNSNEYGLRNSLW 460
Cdd:cd07093 327 TGGGRPELPDL--EGGYFVEPTVIT--GLDNDSRV--AQEEIFG---PVVTVIPFDDE---EEAIELANDTPYGLAAYVW 394
|
330 340
....*....|....*....|...
gi 505433282 461 SGSDEVVERFVREVgNGGLLKVN 483
Cdd:cd07093 395 TRDLGRAHRVARRL-EAGTVWVN 416
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
198-477 |
1.43e-23 |
|
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: 103.47 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRAPRSIALSTMyvlrdLVAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIfYFGGSreglVFQGECVAR 277
Cdd:cd07109 145 GNAVVVKPAEDAPLTAL-----RLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHI-SFTGS----VETGIAVMR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 278 --------------GKKPILELAGND-----GVVVWHDadlalaaeaitecFFGSGQICMVPNYVIVHPAVAEELLDLVV 338
Cdd:cd07109 215 aaaenvvpvtlelgGKSPQIVFADADleaalPVVVNAI-------------IQNAGQTCSAGSRLLVHRSIYDEVLERLV 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 339 KAAAEIRPGYP-DDP--GVLLSPVRRsEKFFRLLEQALSRGAQLVCGGDRIEldgTVSETGVFLQPTVLRvDGLAGARtv 415
Cdd:cd07109 282 ERFRALRVGPGlEDPdlGPLISAKQL-DRVEGFVARARARGARIVAGGRIAE---GAPAGGYFVAPTLLD-DVPPDSR-- 354
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505433282 416 dAVRDETFFPLLpVVVPepmsdADLLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVGNG 477
Cdd:cd07109 355 -LAQEEIFGPVL-AVMP-----FDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAG 409
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
99-461 |
3.93e-23 |
|
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: 102.04 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 99 RLRLGELFR--EALLRNRETFLDLLVAE-AHPRKLAEWEFScllqvYSPESISFYASQMHTEFAY------GDRRLIVRr 169
Cdd:cd07120 42 RLRARVLLElaDAFEANAERLARLLALEnGKILGEARFEIS-----GAISELRYYAGLARTEAGRmiepepGSFSLVLR- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 170 QPDGVVCVNPPQNAPAPSAALAVL-ALMAGNAVVVRAPRSIALSTMYVLRDLVAplLSELgaPAGTLNVVCGKPREMIDR 248
Cdd:cd07120 116 EPMGVAGIIVPWNSPVVLLVRSLApALAAGCTVVVKPAGQTAQINAAIIRILAE--IPSL--PAGVVNLFTESGSEGAAH 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 249 WLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVWHDADLALAAEAITECFF-GSGQICMVPNYVIVHP 327
Cdd:cd07120 192 LVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTiFAGQFCMAGSRVLVQR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 328 AVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV--RRS-EKFFRLLEQALSRGAQLVCGGDRieLDGTVSEtGVFLQPTVL 404
Cdd:cd07120 272 SIADEVRDRLAARLAAVKVGPGLDPASDMGPLidRANvDRVDRMVERAIAAGAEVVLRGGP--VTEGLAK-GAFLRPTLL 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 505433282 405 RVDglagARTVDAVRDETFFpllPVVVPEPMSDAdllDRVIAYVNSNEYGLRNSLWS 461
Cdd:cd07120 349 EVD----DPDADIVQEEIFG---PVLTLETFDDE---AEAVALANDTDYGLAASVWT 395
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
107-461 |
9.61e-23 |
|
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: 101.09 E-value: 9.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 107 REALLRNretFLDLLvaEAHPRKLAEWEFS--------CLLQV-YSPESISFYASQMHTE------FAYGDRRLIVRRQP 171
Cdd:cd07114 45 RGKLLRR---LADLI--EANAEELAELETRdngklireTRAQVrYLAEWYRYYAGLADKIegavipVDKGDYLNFTRREP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 172 DGVVCVNPPQNAPAPSAALAVLAL-MAGNAVVVRAPRSIALSTMyvlrdLVAPLLSELGAPAGTLNVVCGKPREMIDRWL 250
Cdd:cd07114 120 LGVVAAITPWNSPLLLLAKKLAPAlAAGNTVVLKPSEHTPASTL-----ELAKLAEEAGFPPGVVNVVTGFGPETGEALV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 251 AHPGVNDIFYFGGSREGLVFqGECVARGKKPI-LELAGNDGVVVWHDADLALAAEAITECFFG-SGQICMVPNYVIVHPA 328
Cdd:cd07114 195 EHPLVAKIAFTGGTETGRHI-ARAAAENLAPVtLELGGKSPNIVFDDADLDAAVNGVVAGIFAaAGQTCVAGSRLLVQRS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 329 VAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQALSRGAQLVCGGDRieLDGTVSETGVFLQPTVLR 405
Cdd:cd07114 274 IYDEFVERLVARARAIRVGDPLDPETQMGPLateRQLEKVERYVARAREEGARVLTGGER--PSGADLGAGYFFEPTILA 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 505433282 406 VDglagarTVDA--VRDETFFPLLPVVvpePMSDAdllDRVIAYVNSNEYGLRNSLWS 461
Cdd:cd07114 352 DV------TNDMriAQEEVFGPVLSVI---PFDDE---EEAIALANDSEYGLAAGIWT 397
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
155-522 |
1.60e-22 |
|
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: 99.91 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 155 HTEFAYGDRRLIVRRQPDGVVCVNPPQNAPAPSAAL-AVLALMAGNAVVVRaPRSIALSTMYVLRDLVAPLLselgaPAG 233
Cdd:cd07087 84 SVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALApLIGAIAAGNTVVLK-PSELAPATSALLAKLIPKYF-----DPE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 234 TLNVVCGKPREmIDRWLAHPgVNDIFYFGGSREG-LVFQGecVARGKKP-ILELAGNDGVVV--------------WHDa 297
Cdd:cd07087 158 AVAVVEGGVEV-ATALLAEP-FDHIFFTGSPAVGkIVMEA--AAKHLTPvTLELGGKSPCIVdkdanlevaarriaWGK- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 298 dlalaaeaitecFFGSGQICMVPNYVIVHPAVAEELLDLVVKAaaeIRPGYPDDPgvllspvRRSEKFFRLL-EQALSRG 376
Cdd:cd07087 233 ------------FLNAGQTCIAPDYVLVHESIKDELIEELKKA---IKEFYGEDP-------KESPDYGRIInERHFDRL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 377 AQLVCGGDrIELDGTVSETGVFLQPTVLRVDGLAgartvDAV-RDETFFPLLPVVvpePMSDadlLDRVIAYVNSNEYGL 455
Cdd:cd07087 291 ASLLDDGK-VVIGGQVDKEERYIAPTILDDVSPD-----SPLmQEEIFGPILPIL---TYDD---LDEAIEFINSRPKPL 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505433282 456 RNSLWSGSDEVVERFVREVGNGGLLkVNDS--HIGfLPYLPtHGGTGlTSGV---HGEANYPILktSHQQGV 522
Cdd:cd07087 359 ALYLFSEDKAVQERVLAETSSGGVC-VNDVllHAA-IPNLP-FGGVG-NSGMgayHGKAGFDTF--SHLKSV 424
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
198-484 |
1.31e-21 |
|
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: 97.76 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRAPRSIALSTMYVLRdLVAPLLSELGAPAGTLNVVCGKPrEMIDRWLAHPGVNDIFYFGGSREG-LVFqgECVA 276
Cdd:cd07098 148 GNAIVVKVSEQVAWSSGFFLS-IIRECLAACGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGkKVM--AAAA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 277 RGKKP-ILELAGNDGVVVWHDADLALAAEAITE-CFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPD---- 350
Cdd:cd07098 224 ESLTPvVLELGGKDPAIVLDDADLDQIASIIMRgTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLdgdv 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 351 DPGVLLSPVrRSEKFFRLLEQALSRGAQLVCGGDRIELDGTVSetGVFLQPTVLrVDGLAGartVDAVRDETFFPLLPVV 430
Cdd:cd07098 304 DVGAMISPA-RFDRLEELVADAVEKGARLLAGGKRYPHPEYPQ--GHYFPPTLL-VDVTPD---MKIAQEEVFGPVMVVM 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 505433282 431 vpePMSDAdllDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVgNGGLLKVND 484
Cdd:cd07098 377 ---KASDD---EEAVEIANSTEYGLGASVFGKDIKRARRIASQL-ETGMVAIND 423
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
166-465 |
2.54e-21 |
|
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: 96.88 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 166 IVRRQPDGVVCVNPPQNAPAPSAALAVLAL-MAGNAVVVRAPRSIALStMYVLRDLVApllsELGAPAGTLNVVCGKpRE 244
Cdd:cd07139 132 LVRREPVGVVAAIVPWNAPLFLAALKIAPAlAAGCTVVLKPSPETPLD-AYLLAEAAE----EAGLPPGVVNVVPAD-RE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 245 MIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVWHDADLALAAEAITECFFG-SGQICMVPNYV 323
Cdd:cd07139 206 VGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMnNGQVCVALTRI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 324 IVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQALSRGAQLVCGGDRIE-LDGtvsetGVFL 399
Cdd:cd07139 286 LVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLasaRQRERVEGYIAKGRAEGARLVTGGGRPAgLDR-----GWFV 360
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505433282 400 QPTVlrvdgLAGARTVDAV-RDETFFPLLpVVVPepmsdADLLDRVIAYVNSNEYGLRNSLWSGSDE 465
Cdd:cd07139 361 EPTL-----FADVDNDMRIaQEEIFGPVL-SVIP-----YDDEDDAVRIANDSDYGLSGSVWTADVE 416
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
72-477 |
7.02e-21 |
|
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: 95.39 E-value: 7.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 72 AGAGEIEESLDAATAAAAGWAAVPLPTRLRLGELFREALLRNRETFLDLLVAE-AHPRKLAEWEFSCLLqvyspESISFY 150
Cdd:cd07102 15 ASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQmGRPIAQAGGEIRGML-----ERARYM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 151 ASQM------HTEFAYGDRRLIVRRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVR-APRSIALSTMyvlrdlVA 222
Cdd:cd07102 90 ISIAeealadIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVnAVIPALLAGNAVILKhSPQTPLCGER------FA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 223 PLLSELGAPAGTLNVVCGKpREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVWHDADLALA 302
Cdd:cd07102 164 AAFAEAGLPEGVFQVLHLS-HETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 303 AEAITE-CFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPVRRSEKFFRLLEQ---ALSRGAQ 378
Cdd:cd07102 243 AESLVDgAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQiadAIAKGAR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 379 LVCGGDRIELDgtvSETGVFLQPTVL-RVDglagaRTVDAVRDETFFPLLPVVVPEpmSDADlldrVIAYVNSNEYGLRN 457
Cdd:cd07102 323 ALIDGALFPED---KAGGAYLAPTVLtNVD-----HSMRVMREETFGPVVGIMKVK--SDAE----AIALMNDSEYGLTA 388
|
410 420
....*....|....*....|
gi 505433282 458 SLWSGSDEVVERFVREVGNG 477
Cdd:cd07102 389 SVWTKDIARAEALGEQLETG 408
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
167-504 |
7.07e-21 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 95.36 E-value: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 167 VRRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRAPRSIALSTMYVlrdlvAPLLSELgAPAGTLNVVCGKPREM 245
Cdd:PRK13473 134 IRRDPVGVVASIAPWNYPLMMAAwKLAPALAAGNTVVLKPSEITPLTALKL-----AELAADI-LPPGVLNVVTGRGATV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 246 IDRWLAHPGVnDIFYFGGSreglVFQGECVAR-----GKKPILELAGNDGVVVWHDADLALAAEAI-TECFFGSGQICMV 319
Cdd:PRK13473 208 GDALVGHPKV-RMVSLTGS----IATGKHVLSaaadsVKRTHLELGGKAPVIVFDDADLDAVVEGIrTFGYYNAGQDCTA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 320 PNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQALSRG-AQLVCGGDRIELDgtvset 395
Cdd:PRK13473 283 ACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLisaAHRDRVAGFVERAKALGhIRVVTGGEAPDGK------ 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 396 GVFLQPTVlrvdgLAGARTVDA-VRDETFFpllPVVVPEPMSDAdllDRVIAYVNSNEYGLRNSLWSgsdevverfvREV 474
Cdd:PRK13473 357 GYYYEPTL-----LAGARQDDEiVQREVFG---PVVSVTPFDDE---DQAVRWANDSDYGLASSVWT----------RDV 415
|
330 340 350
....*....|....*....|....*....|....*....
gi 505433282 475 GNG---------GLLKVNDsHIGFLPYLPtHGGTGLtSG 504
Cdd:PRK13473 416 GRAhrvsarlqyGCTWVNT-HFMLVSEMP-HGGQKQ-SG 451
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
65-523 |
8.33e-21 |
|
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: 95.07 E-value: 8.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 65 VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLGELFREALLRNRETFLDLLVAEA-HPRKLAeweFSCLLQVYS 143
Cdd:cd07101 8 PLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETgKARRHA---FEEVLDVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 144 peSISFYASQMHTEFAYGDRR--------LIVRRQPDGVVCVNPPQNAPAPSAAL-AVLALMAGNAVVVRAPRSIALSTM 214
Cdd:cd07101 85 --VARYYARRAERLLKPRRRRgaipvltrTTVNRRPKGVVGVISPWNYPLTLAVSdAIPALLAGNAVVLKPDSQTALTAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 215 YVLRdlvapLLSELGAPAGTLNVVCGKPREMIDRWLAHpgVNDIFYFGGSREGLVFQGECVAR---------GKKPILEL 285
Cdd:cd07101 163 WAVE-----LLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRligcslelgGKNPMIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 286 AGNDgvvvwhdaDLALAAEAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPG----YPDDPGVLLSPvRR 361
Cdd:cd07101 236 EDAD--------LDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGaaldYGPDMGSLISQ-AQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 362 SEKFFRLLEQALSRGAQLVCGGDRieldgtVSETG-VFLQPTVLrvDGLAGARTVdaVRDETFFpllPVVVPEPMSDadl 440
Cdd:cd07101 307 LDRVTAHVDDAVAKGATVLAGGRA------RPDLGpYFYEPTVL--TGVTEDMEL--FAEETFG---PVVSIYRVAD--- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 441 LDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVgNGGLLKVNDShigflpYLPTHGGTGL------TSGV---HGEANy 511
Cdd:cd07101 371 DDEAIELANDTDYGLNASVWTRDGARGRRIAARL-RAGTVNVNEG------YAAAWASIDApmggmkDSGLgrrHGAEG- 442
|
490
....*....|..
gi 505433282 512 pILKTSHQQGVS 523
Cdd:cd07101 443 -LLKYTETQTVA 453
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
95-472 |
1.32e-20 |
|
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: 94.49 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 95 PLPTRLRLGELFREALLRNRETFLDLLVAE-AHPRKLAEWefsclLQVYSPESISFYASQMHTEFAYGDRR--LIVRRQP 171
Cdd:cd07138 56 SVEERAALLERIAEAYEARADELAQAITLEmGAPITLARA-----AQVGLGIGHLRAAADALKDFEFEERRgnSLVVREP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 172 DGVV-CVNP---PQN------APAPSAalavlalmaGNAVVVRaPRSIA-LSTMyvlrdLVAPLLSELGAPAGTLNVVCG 240
Cdd:cd07138 131 IGVCgLITPwnwPLNqivlkvAPALAA---------GCTVVLK-PSEVApLSAI-----ILAEILDEAGLPAGVFNLVNG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 241 KPREMIDRWLAHPGVnDIFYFGGS-REGLVFQGECVARGKKPILELAGNDGVVVWHDA-DLALAAEAITECFFGSGQICM 318
Cdd:cd07138 196 DGPVVGEALSAHPDV-DMVSFTGStRAGKRVAEAAADTVKRVALELGGKSANIILDDAdLEKAVPRGVAACFANSGQSCN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 319 VPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQALSRGAQLVCGG-DRIEldgtVSE 394
Cdd:cd07138 275 APTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLasaAQFDRVQGYIQKGIEEGARLVAGGpGRPE----GLE 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505433282 395 TGVFLQPTVL-RVDglagaRTVDAVRDETFFPLLpVVVPepmsdADLLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVR 472
Cdd:cd07138 351 RGYFVKPTVFaDVT-----PDMTIAREEIFGPVL-SIIP-----YDDEDEAIAIANDTPYGLAGYVWSADPERARAVAR 418
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
162-455 |
1.45e-20 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 94.59 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 162 DRRLIVRRQPDGVVCVNPPQNAPAPSAALAVLALMAGNAVVVRAPRSIALSTMYVLrdlvAPLLSELGAPAGTLNVVCGK 241
Cdd:PRK11241 137 DKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALAL----AELAIRAGIPAGVFNVVTGS 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 242 PREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVWHDADLALAAE-AITECFFGSGQICMVP 320
Cdd:PRK11241 213 AGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEgALASKFRNAGQTCVCA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 321 NYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPVRRSEKFFRLLEQ---ALSRGAQLVCGGDRIELDGTvsetgv 397
Cdd:PRK11241 293 NRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHiadALEKGARVVCGGKAHELGGN------ 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 505433282 398 FLQPTVLrVDGLAGARTvdaVRDETFFPLLPVVVPEPMSDadlldrVIAYVNSNEYGL 455
Cdd:PRK11241 367 FFQPTIL-VDVPANAKV---AKEETFGPLAPLFRFKDEAD------VIAQANDTEFGL 414
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
65-476 |
1.52e-20 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 94.62 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 65 VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLgeLFREA--LLRNRETFLDLLVAEA-HPRKLAEWEFScllqv 141
Cdd:PRK03137 63 VVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARI--LLRAAaiIRRRKHEFSAWLVKEAgKPWAEADADTA----- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 142 yspESISF---YASQM---------------HTEFAYgdrrlivrrQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVV 202
Cdd:PRK03137 136 ---EAIDFleyYARQMlkladgkpvesrpgeHNRYFY---------IPLGVGVVISPWNFPFAIMAgMTLAAIVAGNTVL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 203 VRaPRSIALSTMYvlrdLVAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIfYFGGSRE-GL-VFQ-GECVARG- 278
Cdd:PRK03137 204 LK-PASDTPVIAA----KFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFI-TFTGSREvGLrIYErAAKVQPGq 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 279 ---KKPILELAGNDGVVVWHDADLALAAEAITECFFG-SGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGV 354
Cdd:PRK03137 278 iwlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGfSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAY 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 355 lLSPVrRSEKFFRLLEQALSRG---AQLVCGGDRIEldgtvsETGVFLQPTVLR-VDglAGARTvdaVRDETFFPLLPVv 430
Cdd:PRK03137 358 -MGPV-INQASFDKIMSYIEIGkeeGRLVLGGEGDD------SKGYFIQPTIFAdVD--PKARI---MQEEIFGPVVAF- 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 505433282 431 vpepmSDADLLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVRE--VGN 476
Cdd:PRK03137 424 -----IKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREfhVGN 466
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
170-511 |
2.05e-20 |
|
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: 94.10 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 170 QPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRAPRSIALSTMYVlrdlvAPLLSELGAPAGTLNVVCGKPREMIDR 248
Cdd:cd07142 140 EPIGVVGQIIPWNFPLLMFAwKVGPALACGNTIVLKPAEQTPLSALLA-----AKLAAEAGLPDGVLNIVTGFGPTAGAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 249 WLAHPGVNDIFYFGGSREGLVFQGECVARGKKPI-LELAGNDGVVVWHDADL-ALAAEAITECFFGSGQICMVPNYVIVH 326
Cdd:cd07142 215 IASHMDVDKVAFTGSTEVGKIIMQLAAKSNLKPVtLELGGKSPFIVCEDADVdKAVELAHFALFFNQGQCCCAGSRTFVH 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 327 PAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPVRRSEKFFRLL---EQALSRGAQLVCGGDRIeldgtvSETGVFLQPTV 403
Cdd:cd07142 295 ESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILsyiEHGKEEGATLITGGDRI------GSKGYYIQPTI 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 404 LR--VDGLAGArtvdavRDETFFPLLPVVvpePMSDadlLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVgNGGLLK 481
Cdd:cd07142 369 FSdvKDDMKIA------RDEIFGPVQSIL---KFKT---VDEVIKRANNSKYGLAAGVFSKNIDTANTLSRAL-KAGTVW 435
|
330 340 350
....*....|....*....|....*....|....
gi 505433282 482 VNdSHIGFLPYLPTHG----GTGLTSGVHGEANY 511
Cdd:cd07142 436 VN-CYDVFDASIPFGGykmsGIGREKGIYALNNY 468
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
310-522 |
7.27e-20 |
|
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: 91.90 E-value: 7.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 310 FFGSGQICMVPNYVIVHPAVAEELLDLVVkaaAEIRPGYPDDPGVLLSP----VRRSEKFFR---LLEQALSRGAQLVCG 382
Cdd:cd07134 233 FLNAGQTCIAPDYVFVHESVKDAFVEHLK---AEIEKFYGKDAARKASPdlarIVNDRHFDRlkgLLDDAVAKGAKVEFG 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 383 gdrieldGTVSETGVFLQPTVLR-VDglagaRTVDAVRDETFFPLLPVVvpePMSDadlLDRVIAYVNSNEYGLRNSLWS 461
Cdd:cd07134 310 -------GQFDAAQRYIAPTVLTnVT-----PDMKIMQEEIFGPVLPII---TYED---LDEVIEYINAKPKPLALYVFS 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505433282 462 GSDEVVERFVREVGNGGLLkVNDSHIGFL-PYLPtHGGTGlTSGV---HGEanYPILKTSHQQGV 522
Cdd:cd07134 372 KDKANVNKVLARTSSGGVV-VNDVVLHFLnPNLP-FGGVN-NSGIgsyHGV--YGFKAFSHERAV 431
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
198-483 |
9.69e-20 |
|
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: 91.88 E-value: 9.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRAPRSIALSTMYVLRdLVAPLLSELGAPAGTLNVVCGkPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVAR 277
Cdd:cd07130 160 GNVVVWKPSPTTPLTAIAVTK-IVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAAR 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 278 GKKPILELAGNDGVVVwhdADLALAAEAITECFFG----SGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPG 353
Cdd:cd07130 238 FGRSLLELGGNNAIIV---MEDADLDLAVRAVLFAavgtAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDG 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 354 VLLSPV--RRS-EKFFRLLEQALSRGAQLVCGGDRIELDGTvsetgvFLQPTVlrVDGLAGArtvDAVRDETFFPLLPVV 430
Cdd:cd07130 315 TLVGPLhtKAAvDNYLAAIEEAKSQGGTVLFGGKVIDGPGN------YVEPTI--VEGLSDA---PIVKEETFAPILYVL 383
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 505433282 431 vpepmsDADLLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVGNG-GLLKVN 483
Cdd:cd07130 384 ------KFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSDcGIVNVN 431
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
198-518 |
1.81e-19 |
|
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: 91.12 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRAPRSIALSTMYVlrdlvAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVAR 277
Cdd:cd07091 169 GNTVVLKPAEQTPLSALYL-----AELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKS 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 278 G-KKPILELAGNDGVVVWHDADLALAAEAITE-CFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVL 355
Cdd:cd07091 244 NlKKVTLELGGKSPNIVFDDADLDKAVEWAAFgIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 356 LSPVRRSEKFFRLL---EQALSRGAQLVCGGDRieldgtVSETGVFLQPTVLrVDGLAGARTvdaVRDETFFpllPVVVP 432
Cdd:cd07091 324 QGPQVSKAQFDKILsyiESGKKEGATLLTGGER------HGSKGYFIQPTVF-TDVKDDMKI---AKEEIFG---PVVTI 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 433 EPMSDadlLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVgNGGLLKVNDSHIgFLPYLPTHG----GTGLTSGVHGE 508
Cdd:cd07091 391 LKFKT---EDEVIERANDTEYGLAAGVFTKDINKALRVSRAL-KAGTVWVNTYNV-FDAAVPFGGfkqsGFGRELGEEGL 465
|
330
....*....|
gi 505433282 509 ANYPILKTSH 518
Cdd:cd07091 466 EEYTQVKAVT 475
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
155-488 |
2.89e-19 |
|
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: 90.54 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 155 HTEFAYgdrrliVRRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRAPRSIALSTMYVlrdlvAPLLSELGAPAG 233
Cdd:cd07144 134 PNKLAY------TLHEPYGVCGQIIPWNYPLAMAAwKLAPALAAGNTVVIKPAENTPLSLLYF-----ANLVKEAGFPPG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 234 TLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQG-----------ECvaRGKKP--ILELAGNDGVVVWhdadla 300
Cdd:cd07144 203 VVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKaaaqnlkavtlEC--GGKSPalVFEDADLDQAVKW------ 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 301 laaeAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEI-RPGYPDDPGVLLSPVRRSEKFFRLL---EQALSRG 376
Cdd:cd07144 275 ----AAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDTVVGPQVSKTQYDRVLsyiEKGKKEG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 377 AQLVCGGDRIELDGtvsETGVFLQPTVLrvdgLAGARTVDAVRDETFFpllPVVVPEPMSDAdllDRVIAYVNSNEYGLR 456
Cdd:cd07144 351 AKLVYGGEKAPEGL---GKGYFIPPTIF----TDVPQDMRIVKEEIFG---PVVVISKFKTY---EEAIKKANDTTYGLA 417
|
330 340 350
....*....|....*....|....*....|....
gi 505433282 457 NSLWSGSDEVVERFVREVGNGGLL--KVNDSHIG 488
Cdd:cd07144 418 AAVFTKDIRRAHRVARELEAGMVWinSSNDSDVG 451
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
49-527 |
5.52e-19 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 89.94 E-value: 5.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 49 RALEGRPDPEA-----LHHPY---VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLGELFREALLRNRETFLDL 120
Cdd:PRK09407 20 RRLTARVDGAAgptreVTAPFtgePLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 121 LVAEA-HPRKLAEWEfscLLQVYSpeSISFYASqmHTEFAYGDRR----------LIVRRQPDGVVCVNPPQNAPAPSAA 189
Cdd:PRK09407 100 VQLETgKARRHAFEE---VLDVAL--TARYYAR--RAPKLLAPRRragalpvltkTTELRQPKGVVGVISPWNYPLTLAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 190 L-AVLALMAGNAVVVRAPRSIALSTMYVLRdlvapLLSELGAPAGTLNVVCGKPREMIDRWLAHpgVNDIFYFGGSREGL 268
Cdd:PRK09407 173 SdAIPALLAGNAVVLKPDSQTPLTALAAVE-----LLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 269 VFQGECVAR---------GKKPILELAGNDgvvvwhdaDLALAAEAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVK 339
Cdd:PRK09407 246 VLAEQAGRRligfslelgGKNPMIVLDDAD--------LDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 340 AAAEIRPG----YPDDPGVLLSPvRRSEKFFRLLEQALSRGAQLVCGGD-RIELdgtvsetG-VFLQPTVLR-VDglaga 412
Cdd:PRK09407 318 AVRAMRLGagydYSADMGSLISE-AQLETVSAHVDDAVAKGATVLAGGKaRPDL-------GpLFYEPTVLTgVT----- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 413 RTVDAVRDETFFpllPVVVPEPMSDadlLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVgNGGLLKVNDShigflpY 492
Cdd:PRK09407 385 PDMELAREETFG---PVVSVYPVAD---VDEAVERANDTPYGLNASVWTGDTARGRAIAARI-RAGTVNVNEG------Y 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 505433282 493 LPTHGGTGLT------SGV---HGEANypILKTSHQQGVSIARG 527
Cdd:PRK09407 452 AAAWGSVDAPmggmkdSGLgrrHGAEG--LLKYTESQTIATQRV 493
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
168-489 |
8.65e-19 |
|
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: 88.96 E-value: 8.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 168 RRQPDGVVCVNPPQNAPAPSAAL-AVLALMAGNAVVVRAPRSIALSTMyvlrdLVAPLLSELgAPAGTLNVVCGKPREMI 246
Cdd:cd07108 114 VREPLGVVGAILPWNAPLMLAALkIAPALVAGNTVVLKAAEDAPLAVL-----LLAEILAQV-LPAGVLNVITGYGEECG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 247 DRWLAHPGVNDIfYFGGSREglvfQGECVAR--GKKPI---LELAG-NDGVVVWHDADLALAAEAITECFFG-SGQICMV 319
Cdd:cd07108 188 AALVDHPDVDKV-TFTGSTE----VGKIIYRaaADRLIpvsLELGGkSPMIVFPDADLDDAVDGAIAGMRFTrQGQSCTA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 320 PNYVIVHPAVAEELLDLVVKAAAEIRPGYP----DDPGVLLSPvRRSEKFFRLLEQALSR-GAQLVCGGDrIELDGTVSE 394
Cdd:cd07108 263 GSRLFVHEDIYDAFLEKLVAKLSKLKIGDPldeaTDIGAIISE-KQFAKVCGYIDLGLSTsGATVLRGGP-LPGEGPLAD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 395 tGVFLQPTVlrvdgLAGARTVDAV-RDETFFpllPVVVPEPMSDadlLDRVIAYVNSNEYGLRNSLW--------SGSDE 465
Cdd:cd07108 341 -GFFVQPTI-----FSGVDNEWRLaREEIFG---PVLCAIPWKD---EDEVIAMANDSHYGLAAYVWtrdlgralRAAHA 408
|
330 340
....*....|....*....|....
gi 505433282 466 VVERFVrEVGNGGLLKVNDSHIGF 489
Cdd:cd07108 409 LEAGWV-QVNQGGGQQPGQSYGGF 431
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
166-477 |
2.10e-18 |
|
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: 88.17 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 166 IVRRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRAPRSIALSTMyVLRDLVAPLLselgaPAGTLNVVCGKPRE 244
Cdd:cd07559 131 YHFHEPLGVVGQIIPWNFPLLMAAwKLAPALAAGNTVVLKPASQTPLSIL-VLMELIGDLL-----PKGVVNVVTGFGSE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 245 mIDRWLA-HPGVNDIFYFGGSREG-LVFQgecvARGKKPI---LELAGN------DGVVVWHDADLALAAEAITECFFGS 313
Cdd:cd07559 205 -AGKPLAsHPRIAKLAFTGSTTVGrLIMQ----YAAENLIpvtLELGGKspniffDDAMDADDDFDDKAEEGQLGFAFNQ 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 314 GQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSP---VRRSEKFFRLLEQALSRGAQLVCGGDRIELDG 390
Cdd:cd07559 280 GEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAqvsKDQLEKILSYVDIGKEEGAEVLTGGERLTLGG 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 391 TVSetGVFLQPTVLrvdgLAGARTVDAVRDETFFPLLPVVvpePMSDAdllDRVIAYVNSNEYGLRNSLWSGSDEVVERF 470
Cdd:cd07559 360 LDK--GYFYEPTLI----KGGNNDMRIFQEEIFGPVLAVI---TFKDE---EEAIAIANDTEYGLGGGVWTRDINRALRV 427
|
....*..
gi 505433282 471 VREVGNG 477
Cdd:cd07559 428 ARGIQTG 434
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
161-506 |
5.28e-18 |
|
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: 86.56 E-value: 5.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 161 GDRRLIVRRQPDGVVCVNPPQNAPA-PSAALAVLALMAGNAVVVR----APRSialstmyvlRDLVAPLLSELGAPAGTL 235
Cdd:cd07095 87 AQGRAVLRHRPHGVMAVFGPFNFPGhLPNGHIVPALLAGNTVVFKpselTPAV---------AELMVELWEEAGLPPGVL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 236 NVVCGKpREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVAR-GKKPILELAGNDGVVVWHDADLALAAEAITE-CFFGS 313
Cdd:cd07095 158 NLVQGG-RETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRpGKILALEMGGNNPLVVWDVADIDAAAYLIVQsAFLTA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 314 GQICMVPNYVIVHP-AVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQALSRGAQLVCGGDRIELD 389
Cdd:cd07095 237 GQRCTCARRLIVPDgAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLiiaAAAARYLLAQQDLLALGGEPLLAMERLVAG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 390 GTvsetgvFLQPTVLRVDGLAGartvdaVRDETFF-PLLPVVvpepmsDADLLDRVIAYVNSNEYGLRNSLWSGSDEVVE 468
Cdd:cd07095 317 TA------FLSPGIIDVTDAAD------VPDEEIFgPLLQVY------RYDDFDEAIALANATRFGLSAGLLSDDEALFE 378
|
330 340 350
....*....|....*....|....*....|....*...
gi 505433282 469 RFVREVgNGGLLKVNDSHIGFLPYLPtHGGTGLtSGVH 506
Cdd:cd07095 379 RFLARI-RAGIVNWNRPTTGASSTAP-FGGVGL-SGNH 413
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
167-522 |
8.56e-18 |
|
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: 85.73 E-value: 8.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 167 VRRQPDGVVCVNPPQNAPAPSAALAVLAL-MAGNAVVVRaPRSIALSTMYVLRDLVAPLLselgaPAGTLNVVCGKPREM 245
Cdd:cd07135 104 IRKEPLGVVLIIGPWNYPVLLALSPLVGAiAAGCTVVLK-PSELTPHTAALLAELVPKYL-----DPDAFQVVQGGVPET 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 246 iDRWLAHpGVNDIFYFGGSREGLVFqGECVARGKKP-ILELAGNDGVVVWHDADLALAAEAItecFFG----SGQICMVP 320
Cdd:cd07135 178 -TALLEQ-KFDKIFYTGSGRVGRII-AEAAAKHLTPvTLELGGKSPVIVTKNADLELAAKRI---LWGkfgnAGQICVAP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 321 NYVIVHPAVAEELLDLVVKAAAEIRPG---YPDDPGVLLSPvRRSEKFFRLLEQalSRGaqlvcggdRIELDGTVSETGV 397
Cdd:cd07135 252 DYVLVDPSVYDEFVEELKKVLDEFYPGganASPDYTRIVNP-RHFNRLKSLLDT--TKG--------KVVIGGEMDEATR 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 398 FLQPTVLRVDGLAGArtvdAVRDETFFPLLPVVvpepmsDADLLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVGNG 477
Cdd:cd07135 321 FIPPTIVSDVSWDDS----LMSEELFGPVLPII------KVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSG 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 505433282 478 GLLkVNDS--HIGF--LPYlpthGGTGlTSG---VHGEanYPILKTSHQQGV 522
Cdd:cd07135 391 GVV-INDTliHVGVdnAPF----GGVG-DSGygaYHGK--YGFDTFTHERTV 434
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
198-497 |
4.17e-17 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 84.12 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRAPRSIALSTMYVLRdLVAPLLSELGAPAGTLNVVCGKPR--EMIDRWLAHPGVNdifYFGGSREGLVFQGECV 275
Cdd:PLN02315 182 GNCVVWKGAPTTPLITIAMTK-LVAEVLEKNNLPGAIFTSFCGGAEigEAIAKDTRIPLVS---FTGSSKVGLMVQQTVN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 276 ARGKKPILELAGNDGVVVWHDADLALAAEAITECFFGS-GQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGV 354
Cdd:PLN02315 258 ARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTaGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGT 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 355 LLSPVRRSEK---FFRLLEQALSRGAQLVCGGDRIELDGTvsetgvFLQPTVLRVDGLAgartvDAVRDETFFPLLPVVV 431
Cdd:PLN02315 338 LLGPLHTPESkknFEKGIEIIKSQGGKILTGGSAIESEGN------FVQPTIVEISPDA-----DVVKEELFGPVLYVMK 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505433282 432 PEPMSDAdlldrvIAYVNSNEYGLRNSLWSGSDEVVERFVREVGNG-GLLKVNdshigflpyLPTHG 497
Cdd:PLN02315 407 FKTLEEA------IEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDcGIVNVN---------IPTNG 458
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
198-455 |
4.66e-17 |
|
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: 83.51 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRaPRSIALSTMYVLrdlvAPLLSELGAPAGTLNVVCGKPrEMIDRWLAHPGVNDIFYFGGSREGLVFQGECVAR 277
Cdd:cd07090 144 GNAMVYK-PSPFTPLTALLL----AEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 278 GKKPILELAGNDGVVVWH-DADLALAAEAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDP---- 352
Cdd:cd07090 218 IKHVTLELGGKSPLIIFDdADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEdtqm 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 353 GVLLSPVRRsEKFFRLLEQALSRGAQLVCGGDRIELDGTVsETGVFLQPTVLrvDGLAGARTVdaVRDETFFPLLPVVvp 432
Cdd:cd07090 298 GALISEEHL-EKVLGYIESAKQEGAKVLCGGERVVPEDGL-ENGFYVSPCVL--TDCTDDMTI--VREEIFGPVMSIL-- 369
|
250 260
....*....|....*....|...
gi 505433282 433 epmsDADLLDRVIAYVNSNEYGL 455
Cdd:cd07090 370 ----PFDTEEEVIRRANDTTYGL 388
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
109-474 |
5.59e-17 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 83.25 E-value: 5.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 109 ALLRNRETFL-DLLVAE-AHPRKLAEWE--FSCLLQVYSPEsisfYASQMHTEFAYGDR---RLIVRRQPDGVVCVNPPQ 181
Cdd:PRK10090 6 AGIRERASEIsALIVEEgGKIQQLAEVEvaFTADYIDYMAE----WARRYEGEIIQSDRpgeNILLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 182 NAPA-PSAALAVLALMAGNAVVVRaPRSIALSTMYVLrdlvAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVnDIFY 260
Cdd:PRK10090 82 NFPFfLIARKMAPALLTGNTIVIK-PSEFTPNNAIAF----AKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKV-AMVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 261 FGGSREGLVFQGECVARG-KKPILELAGNDGVVVWHDADLALAAEAITEC-FFGSGQICMVPNYVIVHPAVAEELLDLVV 338
Cdd:PRK10090 156 MTGSVSAGEKIMAAAAKNiTKVCLELGGKAPAIVMDDADLDLAVKAIVDSrVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 339 KAAAEIRPGYP---DDP--GVLLSP--VRRSEKffrLLEQALSRGAQLVCGGDRIEldgtvsETGVFLQPTVL-RVDgla 410
Cdd:PRK10090 236 EAMQAVQFGNPaerNDIamGPLINAaaLERVEQ---KVARAVEEGARVALGGKAVE------GKGYYYPPTLLlDVR--- 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505433282 411 gaRTVDAVRDETFFPLLPVVVpepmsdADLLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREV 474
Cdd:PRK10090 304 --QEMSIMHEETFGPVLPVVA------FDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGL 359
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
198-474 |
9.81e-17 |
|
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: 82.51 E-value: 9.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRA----PRSiALstmyvlrdLVAPLLSELGAPAGTLNVVCGkPREMIDRWLAHPGVNDIFYFGGSREGLVFQGE 273
Cdd:cd07100 124 GNTVLLKHasnvPGC-AL--------AIEELFREAGFPEGVFQNLLI-DSDQVEAIIADPRVRGVTLTGSERAGRAVAAE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 274 CVARGKKPILELAGNDGVVVWHdadLALAAEAITECFFG----SGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYP 349
Cdd:cd07100 194 AGKNLKKSVLELGGSDPFIVLD---DADLDKAVKTAVKGrlqnAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDP 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 350 DDPGVLLSPVRRS---EKFFRLLEQALSRGAQLVCGGDRIELDGTvsetgvFLQPTVLrVDGLAGARtvdAVRDETFFPL 426
Cdd:cd07100 271 MDEDTDLGPLARKdlrDELHEQVEEAVAAGATLLLGGKRPDGPGA------FYPPTVL-TDVTPGMP---AYDEELFGPV 340
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 505433282 427 LPVVVpepmsdADLLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREV 474
Cdd:cd07100 341 AAVIK------VKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRL 382
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
166-477 |
1.07e-16 |
|
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: 82.50 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 166 IVRRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRAPRSIALSTMYVLRdLVAPLLselgaPAGTLNVVCGKPRE 244
Cdd:cd07117 131 IVLREPIGVVGQIIPWNFPFLMAAwKLAPALAAGNTVVIKPSSTTSLSLLELAK-IIQDVL-----PKGVVNIVTGKGSK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 245 MIDRWLAHPGVNDIFYFGGSREGlvfQGECVARGKKPI---LELAGNDGVVVWHDADLALAAEAIT-ECFFGSGQICMVP 320
Cdd:cd07117 205 SGEYLLNHPGLDKLAFTGSTEVG---RDVAIAAAKKLIpatLELGGKSANIIFDDANWDKALEGAQlGILFNQGQVCCAG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 321 NYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSP---VRRSEKFFRLLEQALSRGAQLVCGGDRIELDGTVSetGV 397
Cdd:cd07117 282 SRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAqvnKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDK--GF 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 398 FLQPTVLrVDGLAGARTvdaVRDETFFPLLPVVvpePMSDAdllDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVGNG 477
Cdd:cd07117 360 FIEPTLI-VNVTNDMRV---AQEEIFGPVATVI---KFKTE---DEVIDMANDSEYGLGGGVFTKDINRALRVARAVETG 429
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
198-461 |
3.52e-15 |
|
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: 77.82 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRAPRSIALSTMyvlrdLVAPLLSELGAPAGTLNVVCGkPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVAR 277
Cdd:cd07111 175 GNTVVLKPAEYTPLTAL-----LFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGT 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 278 GKKPILELAGNDGVVVWHDADLALAAEAITEC-FFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYP----DDP 352
Cdd:cd07111 249 GKKLSLELGGKSPFIVFDDADLDSAVEGIVDAiWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPldkaIDM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 353 GVLLSPVRRsEKFFRLLEQALSRGAQlvcggdRIELDGTVSETGVFLQPTVlrVDGLAGARTVdaVRDETFFpllPVVVP 432
Cdd:cd07111 329 GAIVDPAQL-KRIRELVEEGRAEGAD------VFQPGADLPSKGPFYPPTL--FTNVPPASRI--AQEEIFG---PVLVV 394
|
250 260
....*....|....*....|....*....
gi 505433282 433 EPMSDAdllDRVIAYVNSNEYGLRNSLWS 461
Cdd:cd07111 395 LTFRTA---KEAVALANNTPYGLAASVWS 420
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
198-455 |
5.43e-15 |
|
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: 77.57 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRAPRSIALSTMYVlrdlvAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREG-LVFQGECVA 276
Cdd:cd07143 172 GNTIVLKPSELTPLSALYM-----TKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGrKVMEAAAKS 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 277 RGKKPILELAGNDGVVVWHDADLALAAEAITE-CFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVL 355
Cdd:cd07143 247 NLKKVTLELGGKSPNIVFDDADLESAVVWTAYgIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTF 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 356 LSPVRRSEKFFRLL---EQALSRGAQLVCGGDRieldgtVSETGVFLQPTVLrvdglaGARTVDA--VRDETFFpllPVV 430
Cdd:cd07143 327 QGPQVSQIQYERIMsyiESGKAEGATVETGGKR------HGNEGYFIEPTIF------TDVTEDMkiVKEEIFG---PVV 391
|
250 260
....*....|....*....|....*
gi 505433282 431 VPEPMSDAdllDRVIAYVNSNEYGL 455
Cdd:cd07143 392 AVIKFKTE---EEAIKRANDSTYGL 413
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
198-511 |
9.77e-15 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 76.77 E-value: 9.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRAPRSIALSTMYVlrdlvAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVAR 277
Cdd:PLN02466 223 GNTIVLKTAEQTPLSALYA-----AKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 278 GKKPI-LELAGNDGVVVWHDADLALAAEAI-TECFFGSGQICMVPNYVIVHPAVAEELLDlVVKAAAEIRP-GYPDDPGV 354
Cdd:PLN02466 298 NLKPVtLELGGKSPFIVCEDADVDKAVELAhFALFFNQGQCCCAGSRTFVHERVYDEFVE-KAKARALKRVvGDPFKKGV 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 355 LLSPVRRSEKF---FRLLEQALSRGAQLVCGGDRIeldgtvSETGVFLQPTVLR--VDGLAGArtvdavRDETFFPLLPV 429
Cdd:PLN02466 377 EQGPQIDSEQFekiLRYIKSGVESGATLECGGDRF------GSKGYYIQPTVFSnvQDDMLIA------QDEIFGPVQSI 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 430 VvpePMSDadlLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVGNGGL----LKVNDSHIGFLPYlpTHGGTGLTSGV 505
Cdd:PLN02466 445 L---KFKD---LDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVwvncFDVFDAAIPFGGY--KMSGIGREKGI 516
|
....*.
gi 505433282 506 HGEANY 511
Cdd:PLN02466 517 YSLNNY 522
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
221-455 |
1.34e-14 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 76.07 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 221 VAPLLSELGAPAGTLNVVCGKPRemIDRWL-AHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVWH-DAD 298
Cdd:PRK13252 188 LAEIYTEAGLPDGVFNVVQGDGR--VGAWLtEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDdADL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 299 LALAAEAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDP----GVLLSPVRRsEKFFRLLEQALS 374
Cdd:PRK13252 266 DRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPatnfGPLVSFAHR-DKVLGYIEKGKA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 375 RGAQLVCGGDRIELDGtvSETGVFLQPTVLrvdglagARTVDA---VRDETFFPLLPVVvpepmsDADLLDRVIAYVNSN 451
Cdd:PRK13252 345 EGARLLCGGERLTEGG--FANGAFVAPTVF-------TDCTDDmtiVREEIFGPVMSVL------TFDDEDEVIARANDT 409
|
....
gi 505433282 452 EYGL 455
Cdd:PRK13252 410 EYGL 413
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
219-479 |
2.32e-14 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 75.28 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 219 DLVAPLLSELGAPAGTLNVVcGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVWH-DA 297
Cdd:PRK13968 170 QLIAQVFKDAGIPQGVYGWL-NADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNdAD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 298 DLALAAEAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPVRR---SEKFFRLLEQALS 374
Cdd:PRK13968 249 LELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARfdlRDELHHQVEATLA 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 375 RGAQLVCGGDRIELDGTvsetgvFLQPTVlrvdgLAG-ARTVDAVRDETFFPLLPVVVPEpmsDAdllDRVIAYVNSNEY 453
Cdd:PRK13968 329 EGARLLLGGEKIAGAGN------YYAPTV-----LANvTPEMTAFREELFGPVAAITVAK---DA---EHALELANDSEF 391
|
250 260
....*....|....*....|....*.
gi 505433282 454 GLRNSLWSGSDEVVERFVREVGNGGL 479
Cdd:PRK13968 392 GLSATIFTTDETQARQMAARLECGGV 417
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
171-456 |
5.65e-14 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 74.41 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 171 PDGVVCVNPPQNAPAPSAALAVL-ALMAGNAVVVRAPRSIALSTMYVLRDLVAPllselGAPAGTLNVVCGKPREMIDRW 249
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIApALIAGNAVVLKPPTQGAVAALHMVHCFHLA-----GFPKGLISCVTGKGSEIGDFL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 250 LAHPGVNDIFYFGGSreglvfQGECVAR--GKKPI-LELAGNDGVVVWHDADLALAAEAITECFFG-SGQICMVPNYVIV 325
Cdd:PLN00412 233 TMHPGVNCISFTGGD------TGIAISKkaGMVPLqMELGGKDACIVLEDADLDLAAANIIKGGFSySGQRCTAVKVVLV 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 326 HPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPVRRSEKFF--RLLEQALSRGAQLVCGGDRieldgtvseTGVFLQPTV 403
Cdd:PLN00412 307 MESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFieGLVMDAKEKGATFCQEWKR---------EGNLIWPLL 377
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 404 LrvdglagartvDAVRD-------ETFFPLLPVVVPEPMSDAdlldrvIAYVNSNEYGLR 456
Cdd:PLN00412 378 L-----------DNVRPdmriaweEPFGPVLPVIRINSVEEG------IHHCNASNFGLQ 420
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
61-488 |
6.19e-14 |
|
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: 74.15 E-value: 6.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 61 HHPYVVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLGELFREALLRNRETFLDLLVAEAHpRKLAEwefsCLLQ 140
Cdd:cd07125 55 DHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAG-KTLAD----ADAE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 141 VysPESISF---YASQMHTEFAYG------DRRLIVRRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVR-APRS- 208
Cdd:cd07125 130 V--REAIDFcryYAAQARELFSDPelpgptGELNGLELHGRGVFVCISPWNFPLAIFTgQIAAALAAGNTVIAKpAEQTp 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 209 -IALstmyvlrdLVAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGkKPILEL-- 285
Cdd:cd07125 208 lIAA--------RAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERD-GPILPLia 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 286 -------------AGNDGVVVwhdadlalaaEAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDP 352
Cdd:cd07125 279 etggknamivdstALPEQAVK----------DVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 353 GVLLSPVRRSEKFFRL--LEQALSRGAQLVCGGDRIELDGTvsetgvFLQPTVLRVDGLagartvDAVRDETFFPLLPVV 430
Cdd:cd07125 349 STDVGPLIDKPAGKLLraHTELMRGEAWLIAPAPLDDGNGY------FVAPGIIEIVGI------FDLTTEVFGPILHVI 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 431 vpepMSDADLLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVR--EVGNgglLKVNDSHIG 488
Cdd:cd07125 417 ----RFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRErvEAGN---LYINRNITG 469
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
198-522 |
7.03e-14 |
|
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: 73.60 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRaPRSIALSTMYVLRDLVAPLLSelgapAGTLNVVCGKPRE----MIDRWlahpgvNDIFYFGGSREGLVFQGe 273
Cdd:cd07137 129 GNAVVLK-PSELAPATSALLAKLIPEYLD-----TKAIKVIEGGVPEttalLEQKW------DKIFFTGSPRVGRIIMA- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 274 CVARGKKPI-LELAGNDGVVVWHDADLALAAEAITECFFGS--GQICMVPNYVIVHPAVAEELLDLVVKaaaEIRPGYPD 350
Cdd:cd07137 196 AAAKHLTPVtLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnnGQACIAPDYVLVEESFAPTLIDALKN---TLEKFFGE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 351 DPGV--LLSPVRRSeKFFRLLEQALSRGAQlvcgGDRIELDGTVSETGVFLQPTVLRVDGLAGARTVdavrDETFFPLLP 428
Cdd:cd07137 273 NPKEskDLSRIVNS-HHFQRLSRLLDDPSV----ADKIVHGGERDEKNLYIEPTILLDPPLDSSIMT----EEIFGPLLP 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 429 VVVPEPMSDAdlldrvIAYVNSNEYGLRNSLWSGSDEVVERFVREVGNGGLLkVNDSHIGFL-PYLPtHGGTGlTSGV-- 505
Cdd:cd07137 344 IITVKKIEES------IEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVT-FNDTVVQYAiDTLP-FGGVG-ESGFga 414
|
330
....*....|....*...
gi 505433282 506 -HGEANYPILktSHQQGV 522
Cdd:cd07137 415 yHGKFSFDAF--SHKKAV 430
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
166-516 |
9.88e-14 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 73.39 E-value: 9.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 166 IVRRQPDGVVCVNPPQNAPAPSAA-LAVLALMAGNAVVVRAPRSIALSTMYVlrdlvAPLLSELGAPAGTLNVVCGKPRE 244
Cdd:PRK09847 152 MIVREPVGVIAAIVPWNFPLLLTCwKLGPALAAGNSVILKPSEKSPLSAIRL-----AGLAKEAGLPDGVLNVVTGFGHE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 245 MIDRWLAHPGVNDIFYFGGSREG---LVFQGEcvARGKKPILELAGNDGVVVWHDADLALAAEAITEC--FFGSGQICMV 319
Cdd:PRK09847 227 AGQALSRHNDIDAIAFTGSTRTGkqlLKDAGD--SNMKRVWLEAGGKSANIVFADCPDLQQAASATAAgiFYNQGQVCIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 320 PNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDP----GVLLSPVrRSEKFFRLLEQALSRGAQLvcggdrieLDGTVSET 395
Cdd:PRK09847 305 GTRLLLEESIADEFLALLKQQAQNWQPGHPLDPattmGTLIDCA-HADSVHSFIREGESKGQLL--------LDGRNAGL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 396 GVFLQPTVL-RVDglagaRTVDAVRDETFFPLLPVVVPEPMSDADLLdrviayVNSNEYGLRNSLWSGSDEVVERFVREV 474
Cdd:PRK09847 376 AAAIGPTIFvDVD-----PNASLSREEIFGPVLVVTRFTSEEQALQL------ANDSQYGLGAAVWTRDLSRAHRMSRRL 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 505433282 475 GNGGLLKVN----DSHIGFLPYlpTHGGTGLTSGVHGEANYPILKT 516
Cdd:PRK09847 445 KAGSVFVNNyndgDMTVPFGGY--KQSGNGRDKSLHALEKFTELKT 488
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
310-522 |
1.24e-13 |
|
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: 72.92 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 310 FFGSGQICMVPNYVIVHPAVAEELLDLVVKaaaEIRPGYPDDPgvLLSP--VRR-SEKFFRLLEQALSrGAQLVCGGDri 386
Cdd:cd07136 233 FLNAGQTCVAPDYVLVHESVKEKFIKELKE---EIKKFYGEDP--LESPdyGRIiNEKHFDRLAGLLD-NGKIVFGGN-- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 387 eldgtVSETGVFLQPTVL---RVDglagartvDAV-RDETFFPLLPVVVpepmsdADLLDRVIAYVNSNEYGLRNSLWSG 462
Cdd:cd07136 305 -----TDRETLYIEPTILdnvTWD--------DPVmQEEIFGPILPVLT------YDTLDEAIEIIKSRPKPLALYLFSE 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505433282 463 SDEVVERFVREVGNGGLLkVNDS--HIGfLPYLPtHGGTGlTSGV---HGEANYpilKT-SHQQGV 522
Cdd:cd07136 366 DKKVEKKVLENLSFGGGC-INDTimHLA-NPYLP-FGGVG-NSGMgsyHGKYSF---DTfSHKKSI 424
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
198-520 |
2.80e-13 |
|
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: 72.10 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRAPRSIALSTMyVLRDLVAPLLselgaPAGTLNVVCGKPREmIDRWLA-HPGVNDIFYFGGSREG-LVFQgeCV 275
Cdd:cd07116 164 GNCVVLKPAEQTPASIL-VLMELIGDLL-----PPGVVNVVNGFGLE-AGKPLAsSKRIAKVAFTGETTTGrLIMQ--YA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 276 ARGKKPI-LELAGN------DGVVVWHDADLALAAEAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGY 348
Cdd:cd07116 235 SENIIPVtLELGGKspniffADVMDADDAFFDKALEGFVMFALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGN 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 349 PDDPGVLL---SPVRRSEKFFRLLEQALSRGAQLVCGGDRIELDGTVSetGVFLQPTVLrvdglAGARTVDAVRDETFFP 425
Cdd:cd07116 315 PLDTETMIgaqASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLG--GGYYVPTTF-----KGGNKMRIFQEEIFGP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 426 LLPVVVPEPMSDAdlldrvIAYVNSNEYGLRNSLWSGSDEVVERFVREVgNGGLLKVNDSHIgflpyLPTHGGTG--LTS 503
Cdd:cd07116 388 VLAVTTFKDEEEA------LEIANDTLYGLGAGVWTRDGNTAYRMGRGI-QAGRVWTNCYHL-----YPAHAAFGgyKQS 455
|
330
....*....|....*..
gi 505433282 504 GVhGEANYPILKTSHQQ 520
Cdd:cd07116 456 GI-GRENHKMMLDHYQQ 471
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
156-522 |
1.29e-12 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 70.06 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 156 TEFAYGDRRLIVRRQPDGVVCVNPPQNAPAPSAAL-AVLALMAGNAVVVRaPRSIALSTMYVLRDLVAPLLSElgapagT 234
Cdd:PTZ00381 94 TVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIpLAGAIAAGNTVVLK-PSELSPHTSKLMAKLLTKYLDP------S 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 235 LNVVCGKPREMIDRWLAHPgVNDIFYFGGSREG-LVFQGecVARGKKP-ILELAGNDGVVVWHDADLALAAEAITEC-FF 311
Cdd:PTZ00381 167 YVRVIEGGVEVTTELLKEP-FDHIFFTGSPRVGkLVMQA--AAENLTPcTLELGGKSPVIVDKSCNLKVAARRIAWGkFL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 312 GSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIrpgYPDDPgvllspvRRSEKFFRLL-EQALSRGAQLVCG-GDRIELD 389
Cdd:PTZ00381 244 NAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEF---FGEDP-------KKSEDYSRIVnEFHTKRLAELIKDhGGKVVYG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 390 GTVSETGVFLQPTVL-RVDglagartVDAV--RDETFFPLLPVVVPEPmsdadlLDRVIAYVNSNEYGLRNSLWSGSDEV 466
Cdd:PTZ00381 314 GEVDIENKYVAPTIIvNPD-------LDSPlmQEEIFGPILPILTYEN------IDEVLEFINSRPKPLALYYFGEDKRH 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 467 VERFVREVGNGGLLkVNDSHIGFL-PYLPtHGGTGlTSGV---HGEANYPILktSHQQGV 522
Cdd:PTZ00381 381 KELVLENTSSGAVV-INDCVFHLLnPNLP-FGGVG-NSGMgayHGKYGFDTF--SHPKPV 435
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
159-478 |
1.34e-12 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 69.77 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 159 AYGDRRLIVRRQPDGVVCVNPPQNAPA-PSAALAVLALMAGNAVVVRAPRSIALSTMYvLRDLVApllsELGAPAG---T 234
Cdd:PRK09406 111 AVGASRAYVRYQPLGVVLAVMPWNFPLwQVVRFAAPALMAGNVGLLKHASNVPQTALY-LADLFR----RAGFPDGcfqT 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 235 LNVvcgkPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVW-HDADLALAAEAITECFFGS 313
Cdd:PRK09406 186 LLV----GSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMpSADLDRAAETAVTARVQNN 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 314 GQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQALSRGAQLVCGGDRIELDG 390
Cdd:PRK09406 262 GQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLateQGRDEVEKQVDDAVAAGATILCGGKRPDGPG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 391 TvsetgvFLQPTVlrvdgLAGARTVDAV-RDETFFPLlpvvvpEPMSDADLLDRVIAYVNSNEYGLRNSLWSGSDEVVER 469
Cdd:PRK09406 342 W------FYPPTV-----ITDITPDMRLyTEEVFGPV------ASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQER 404
|
....*....
gi 505433282 470 FVREVGNGG 478
Cdd:PRK09406 405 FIDDLEAGQ 413
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
310-507 |
1.43e-12 |
|
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: 69.56 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 310 FFGSGQICMVPNYVIVHPAVAEELLDlvvKAAAEIRPGYPDDPgvllspvRRSEKFFRLL-EQALSRGAQLVCGGdRIEL 388
Cdd:cd07132 233 FINAGQTCIAPDYVLCTPEVQEKFVE---ALKKTLKEFYGEDP-------KESPDYGRIInDRHFQRLKKLLSGG-KVAI 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 389 DGTVSETGVFLQPTVlrvdgLAGARTVDAV-RDETFFPLLPVVVPEPMSDAdlldrvIAYVNSNEYGLRNSLWSGSDEVV 467
Cdd:cd07132 302 GGQTDEKERYIAPTV-----LTDVKPSDPVmQEEIFGPILPIVTVNNLDEA------IEFINSREKPLALYVFSNNKKVI 370
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505433282 468 ERFVREVGNGGLLkVNDS--HIgFLPYLPtHGGTGLtSGV---HG 507
Cdd:cd07132 371 NKILSNTSSGGVC-VNDTimHY-TLDSLP-FGGVGN-SGMgayHG 411
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
220-511 |
3.90e-12 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 68.62 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 220 LVAPLLSELGAPAGTLNVVCGKpREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVARGKKPILEL-AGNDGVVVWHDAD 298
Cdd:PLN02419 294 ILAELAMEAGLPDGVLNIVHGT-NDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMgAKNHGLVLPDANI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 299 LALAAEAITECFFGSGQICMVPNyVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPV---RRSEKFFRLLEQALSR 375
Cdd:PLN02419 373 DATLNALLAAGFGAAGQRCMALS-TVVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPViskQAKERICRLIQSGVDD 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 376 GAQLVCGGDRIELDGTvsETGVFLQPTVLRvdglAGARTVDAVRDETFFPLLPVVvpepmsDADLLDRVIAYVNSNEYGL 455
Cdd:PLN02419 452 GAKLLLDGRDIVVPGY--EKGNFIGPTILS----GVTPDMECYKEEIFGPVLVCM------QANSFDEAISIINKNKYGN 519
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 505433282 456 RNSLWSGSDEVVERFVREVgNGGLLKVNdshIGFLPYLPTHGGTGLTSGVHGEANY 511
Cdd:PLN02419 520 GAAIFTSSGAAARKFQMDI-EAGQIGIN---VPIPVPLPFFSFTGNKASFAGDLNF 571
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
169-516 |
4.97e-12 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 68.31 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 169 RQPDGVVCVNPPQNAPAPS-AALAVLALMAGNAVVVRAPRSIALSTMYVlrdlvAPLLSELGAPAGTLNVVCGKPREMID 247
Cdd:PLN02766 156 KEPIGVVGHIIPWNFPSTMfFMKVAPALAAGCTMVVKPAEQTPLSALFY-----AHLAKLAGVPDGVINVVTGFGPTAGA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 248 RWLAHPGVnDIFYFGGSRE--GLVFQGECVARGKKPILELAGNDGVVVWHDADL-ALAAEAITECFFGSGQICMVPNYVI 324
Cdd:PLN02766 231 AIASHMDV-DKVSFTGSTEvgRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVdMAVDLALLGIFYNKGEICVASSRVY 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 325 VHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPVRRSEKFFRLL---EQALSRGAQLVCGGDrieldgTVSETGVFLQP 401
Cdd:PLN02766 310 VQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILsyiEHGKREGATLLTGGK------PCGDKGYYIEP 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 402 TVLrVDglaGARTVDAVRDETFFPLLPVVvpepmsDADLLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVREVgNGGLLK 481
Cdd:PLN02766 384 TIF-TD---VTEDMKIAQDEIFGPVMSLM------KFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSI-RAGTIW 452
|
330 340 350
....*....|....*....|....*....|....*....
gi 505433282 482 VNdSHIGFLPYLPTHG----GTGLTSGVHGEANYPILKT 516
Cdd:PLN02766 453 VN-CYFAFDPDCPFGGykmsGFGRDQGMDALDKYLQVKS 490
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
310-522 |
2.95e-10 |
|
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: 62.50 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 310 FFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPgvLLSPV---RRSEKFFRLLEQALSRGAQLV-CGGDR 385
Cdd:cd07133 234 LLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNP--DYTSIineRHYARLQGLLEDARAKGARVIeLNPAG 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 386 IELDGTvsetgVFLQPT-VLRVDglagaRTVDAVRDETFFPLLPVVvpePMSDadlLDRVIAYVNSNEYGLRNSLWSGSD 464
Cdd:cd07133 312 EDFAAT-----RKLPPTlVLNVT-----DDMRVMQEEIFGPILPIL---TYDS---LDEAIDYINARPRPLALYYFGEDK 375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505433282 465 EVVERFVREVGNGGLLkVNDS--HIGF--LPYlpthGGTGlTSGV---HGEANYpilKT-SHQQGV 522
Cdd:cd07133 376 AEQDRVLRRTHSGGVT-INDTllHVAQddLPF----GGVG-ASGMgayHGKEGF---LTfSHAKPV 432
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
198-504 |
3.47e-09 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 59.33 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRAPRSIALSTMYVLRDLV-APLLselgaPAGTLNVVCGKPREMIDrwlaHPGVNDIFYFGGSREG---LVFQGE 273
Cdd:PRK11903 176 GVPVIVKPATATAWLTQRMVKDVVaAGIL-----PAGALSVVCGSSAGLLD----HLQPFDVVSFTGSAETaavLRSHPA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 274 CVARGKKPILE-------LAGNDgVVVWHDADLALAAEAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAEIRP 346
Cdd:PRK11903 247 VVQRSVRVNVEadslnsaLLGPD-AAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTV 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 347 GYPDDPGVLLSPVRRSEKFFRLLE--QALSRGAQLVCGGDRIELDGTVSETGVFLQPTVLRVDGLAGARTVDAVrdETFF 424
Cdd:PRK11903 326 GNPRNDGVRMGPLVSRAQLAAVRAglAALRAQAEVLFDGGGFALVDADPAVAACVGPTLLGASDPDAATAVHDV--EVFG 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 425 PLLPVVVPEPMSDAdlldrvIAYVNSNEYGLRNSLWSGSDEVVERFVREVG--NGGLL----KVNDSHIGFLPYLPT--H 496
Cdd:PRK11903 404 PVATLLPYRDAAHA------LALARRGQGSLVASVYSDDAAFLAAAALELAdsHGRVHvispDVAALHTGHGNVMPQslH 477
|
....*...
gi 505433282 497 GGTGLTSG 504
Cdd:PRK11903 478 GGPGRAGG 485
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
170-522 |
6.74e-07 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 51.97 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 170 QPDGVVCVNPPQNAP-APSAALAVLALMAGNAVVVRaPRSIALSTMYVLRDLVAPLLSelgapAGTLNVVCGKPRE---- 244
Cdd:PLN02174 111 EPLGVVLVISAWNYPfLLSIDPVIGAISAGNAVVLK-PSELAPASSALLAKLLEQYLD-----SSAVRVVEGAVTEttal 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 245 MIDRWlahpgvNDIFYFGGSREGLVFQGECVARGKKPILELAGNDGVVVWHDADLALAAEAITECFFG--SGQICMVPNY 322
Cdd:PLN02174 185 LEQKW------DKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcnNGQACISPDY 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 323 VIVHPAVAEELLDLVVKaaaEIRPGYPDDP--GVLLSPVRRSEKFFRLLEQALSRGAQlvcggDRIELDGTVSETGVFLQ 400
Cdd:PLN02174 259 ILTTKEYAPKVIDAMKK---ELETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDEKEVS-----DKIVYGGEKDRENLKIA 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 401 PTVL---RVDGLagartvdAVRDETFFPLLPVVVPEPMSDAdlldrvIAYVNSNEYGLRNSLWSGSDEVVERFVREVGNG 477
Cdd:PLN02174 331 PTILldvPLDSL-------IMSEEIFGPLLPILTLNNLEES------FDVIRSRPKPLAAYLFTHNKKLKERFAATVSAG 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 505433282 478 GLLkVNDSHIGFLPYLPTHGGTGlTSGV---HGEANYPILktSHQQGV 522
Cdd:PLN02174 398 GIV-VNDIAVHLALHTLPFGGVG-ESGMgayHGKFSFDAF--SHKKAV 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
169-504 |
3.44e-06 |
|
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: 49.54 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 169 RQPDGVVCVNPPQNAPAPSAALAVLAL-MAGNAVVVRAPRSIALSTMYVLRDLVAPLLselgAPAGTLNVVCGKPREMiD 247
Cdd:cd07084 98 RWPYGPVLVIGAFNFPLWIPLLQLAGAlAMGNPVIVKPHTAVSIVMQIMVRLLHYAGL----LPPEDVTLINGDGKTM-Q 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 248 RWLAHPGVNDIFYFGGSReglvfQGECVARGKKPI---LELAGNDGVVVwhDADLALAAEAITECFF----GSGQICMVP 320
Cdd:cd07084 173 ALLLHPNPKMVLFTGSSR-----VAEKLALDAKQAriyLELAGFNWKVL--GPDAQAVDYVAWQCVQdmtaCSGQKCTAQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 321 NYVIVHPAVA-EELLDLVVKAAAEIRPGypddpGVLLSPVRRSEKFFRLLEQALSRGAQLVCGGDRIELDGTVSETGVfL 399
Cdd:cd07084 246 SMLFVPENWSkTPLVEKLKALLARRKLE-----DLLLGPVQTFTTLAMIAHMENLLGSVLLFSGKELKNHSIPSIYGA-C 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 400 QPTVLRVDGLAGARTVDAVRDETFFPLLPVVVPEPMSDADLLDRVIAYVNSneygLRNSLWSGSDEVVERFVREVG-NGG 478
Cdd:cd07084 320 VASALFVPIDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGS----LTAAIYSNDPIFLQELIGNLWvAGR 395
|
330 340
....*....|....*....|....*.
gi 505433282 479 LLKVNDSHIGFLPyLPTHGGTGLTSG 504
Cdd:cd07084 396 TYAILRGRTGVAP-NQNHGGGPAADP 420
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
53-504 |
1.40e-05 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 47.89 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 53 GRPDPEALHHPY----VVGRCAVAGAGEIEESLDAATAAAAGWAAVPLPTRLRLGELFREALLRNRETFLDLLVAEAhpR 128
Cdd:PRK11904 559 GEGEARPVVSPAdrrrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREA--G 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 129 K-----LAEWEfscllqvyspESISF---YASQMHTEFA--------YGDRRlIVRRQPDGV-VCVNP---P------QN 182
Cdd:PRK11904 637 KtlqdaIAEVR----------EAVDFcryYAAQARRLFGapeklpgpTGESN-ELRLHGRGVfVCISPwnfPlaiflgQV 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 183 ApapsaalavLALMAGNAVVVR-APRS--IAlstmyvlrDLVAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNdif 259
Cdd:PRK11904 706 A---------AALAAGNTVIAKpAEQTplIA--------AEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIA--- 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 260 yfggsreGLVFQGEC-VAR-------GKK-PILELAGNDG---------------VVVwhdadlalaaEAITECFFGSGQ 315
Cdd:PRK11904 766 -------GVAFTGSTeTARiinrtlaARDgPIVPLIAETGgqnamivdstalpeqVVD----------DVVTSAFRSAGQ 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 316 ICMVPNYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPVRRSEKFFRLLE--QALSRGAQLVCggdRIELDGTvS 393
Cdd:PRK11904 829 RCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAhiERMKREARLLA---QLPLPAG-T 904
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 394 ETGVFLQPTVLRVDGLagartvDAVRDETFFPLLPVVvpepMSDADLLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVRE 473
Cdd:PRK11904 905 ENGHFVAPTAFEIDSI------SQLEREVFGPILHVI----RYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADR 974
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 505433282 474 --VGNgglLKVNDSHIG-------FlpylpthGGTGLtSG 504
Cdd:PRK11904 975 vrVGN---VYVNRNQIGavvgvqpF-------GGQGL-SG 1003
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
198-448 |
3.15e-05 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 46.38 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNAVVVRA-PRSIALSTMyvLRDLVAPLLSELGAPAGTLNVVCGKPREMIDRWLAHPGVNDIFYFGGSREGLVFQGECVA 276
Cdd:cd07129 135 GCPVVVKAhPAHPGTSEL--VARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 277 RgKKPI---LELAGNDGVVV----WHDADLALAAEAITECFFGSGQICMVPNYVIV-HPAVAEELLDLVVKAAAEIrpgy 348
Cdd:cd07129 213 R-PEPIpfyAELGSVNPVFIlpgaLAERGEAIAQGFVGSLTLGAGQFCTNPGLVLVpAGPAGDAFIAALAEALAAA---- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 349 pdDPGVLLSP-VRRSekFFRLLEQALSRGAQLVCGGdrieldGTVSETGVFLQPTVLRVDGlAGARTVDAVRDETFFPLL 427
Cdd:cd07129 288 --PAQTMLTPgIAEA--YRQGVEALAAAPGVRVLAG------GAAAEGGNQAAPTLFKVDA-AAFLADPALQEEVFGPAS 356
|
250 260
....*....|....*....|.
gi 505433282 428 PVVVPEpmsDADLLDRVIAYV 448
Cdd:cd07129 357 LVVRYD---DAAELLAVAEAL 374
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
198-468 |
5.00e-05 |
|
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: 46.04 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 198 GNaVVVRAPRSIALSTMYvlrdLVAPLLSELGAPAGTLNVVCGKPREMIDRWLAHP---GVNdifyFGGSREglVFQ--- 271
Cdd:cd07123 197 GN-VVLWKPSDTAVLSNY----LVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPhlaGLH----FTGSTP--TFKslw 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 272 ---GECVARGKK-PIL--ELAGNDGVVVwHDA--DLALAAEAITECFFGSGQICMVPNYVIVHPAVAEELLDLVVKAAAE 343
Cdd:cd07123 266 kqiGENLDRYRTyPRIvgETGGKNFHLV-HPSadVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 344 IRPGYPDDPGVLLSPV--RRS-EKFFRLLEQA-LSRGAQLVCGGdriELDGtvsETGVFLQPTVLRV-DGLAgartvDAV 418
Cdd:cd07123 345 IKMGDPDDFSNFMGAVidEKAfDRIKGYIDHAkSDPEAEIIAGG---KCDD---SVGYFVEPTVIETtDPKH-----KLM 413
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 505433282 419 RDETFFPLLPVVVPEpmsDADlLDRVIAYVN-SNEYGLRNSLWSGSDEVVE 468
Cdd:cd07123 414 TEEIFGPVLTVYVYP---DSD-FEETLELVDtTSPYALTGAIFAQDRKAIR 460
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
165-366 |
2.32e-04 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 43.75 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 165 LIVRRQPDGVVCVNPPQNAPAPSAALAVLALMAGNAVVVR----APRSIALSTMyVLRDLVApllseLGAPAGTLNVVCG 240
Cdd:cd07077 94 TYVRAFPIGVTMHILPSTNPLSGITSALRGIATRNQCIFRphpsAPFTNRALAL-LFQAADA-----AHGPKILVLYVPH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 241 KPREMIDRWLAHPGVNDIFYFGGsrEGLVFQGECVARGKKPILELAGNDGVVVWHDADLALAAEAITECFFGSGQICMVP 320
Cdd:cd07077 168 PSDELAEELLSHPKIDLIVATGG--RDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQNACASE 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505433282 321 NYVIVHPAVAEELLDLVVKAAAEIRPGYPDDPGVLLSPVRRSEKFF 366
Cdd:cd07077 246 QNLYVVDDVLDPLYEEFKLKLVVEGLKVPQETKPLSKETTPSFDDE 291
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
329-504 |
1.12e-03 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 41.77 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 329 VAEELLDLVVKAAAEIRPGYPDDPGVLLSPVRRSEKFFRLL---EQALSRGAQLvcggDRIELDGTVsETGVFLQPTVLR 405
Cdd:PRK11905 834 VADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEahiEAMRAAGRLV----HQLPLPAET-EKGTFVAPTLIE 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505433282 406 VDGLAgartvdAVRDETFFPLLPVVvpepMSDADLLDRVIAYVNSNEYGLRNSLWSGSDEVVERFVR--EVGNgglLKVN 483
Cdd:PRK11905 909 IDSIS------DLEREVFGPVLHVV----RFKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSriRAGN---IYVN 975
|
170 180
....*....|....*....|....*...
gi 505433282 484 DSHIG-------FlpylpthGGTGLtSG 504
Cdd:PRK11905 976 RNIIGavvgvqpF-------GGEGL-SG 995
|
|
| |
