|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
3-467 |
0e+00 |
|
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: 566.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 3 SPGDTTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVD 82
Cdd:cd07124 52 NPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 83 EAIDFLEFYSREITAADGYRFdtgEPTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLV 162
Cdd:cd07124 132 EAIDFLEYYAREMLRLRGFPV---EMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 163 AHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRG----PVIAELGGKNPV 238
Cdd:cd07124 209 AAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQkwlkRVIAEMGGKNAI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 239 IVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYRE 318
Cdd:cd07124 289 IVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRR 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 319 ISTQARSDGTVLTGGSVisDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLF 398
Cdd:cd07124 369 YIEIGKSEGRLLLGGEV--LELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVF 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2082837691 399 SEDESEIEQWFDEIEAGMCYVNRKqsaTTGALVQAQPFGGWKFSGTTGKfAGGYWYLQQFMREQSRTRV 467
Cdd:cd07124 447 SRSPEHLERARREFEVGNLYANRK---ITGALVGRQPFGGFKMSGTGSK-AGGPDYLLQFMQPKTVTEN 511
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
7-463 |
1.35e-169 |
|
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: 485.79 E-value: 1.35e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAID 86
Cdd:COG1012 30 TGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAAD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 87 FLEFYSREITAADGYRFDTgePTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKV 166
Cdd:COG1012 110 FLRYYAGEARRLYGETIPS--DAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 167 MDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEADL 246
Cdd:COG1012 188 AELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKR--VTLELGGKNPAIVLDDADL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 247 DAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSD 326
Cdd:COG1012 266 DAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 327 G-TVLTGGSVIsdsDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEI 405
Cdd:COG1012 346 GaELLTGGRRP---DGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARA 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2082837691 406 EQWFDEIEAGMCYVNRKqsaTTGALVQAqPFGGWKFSGtTGKfAGGYWYLQQFMREQS 463
Cdd:COG1012 423 RRVARRLEAGMVWINDG---TTGAVPQA-PFGGVKQSG-IGR-EGGREGLEEYTETKT 474
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
11-463 |
2.98e-160 |
|
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: 461.23 E-value: 2.98e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 11 IGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEF 90
Cdd:pfam00171 20 IATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 91 YSREITAADGyrfDTGEPTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLF 170
Cdd:pfam00171 100 YAGLARRLDG---ETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 171 EEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEADLDAAV 250
Cdd:pfam00171 177 EEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKR--VTLELGGKNPLIVLEDADLDAAV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 251 NGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TV 329
Cdd:pfam00171 255 EAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGaKL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 330 LTGGsvisDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWF 409
Cdd:pfam00171 335 LTGG----EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVA 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2082837691 410 DEIEAGMCYVNRkqsATTGALVQAqPFGGWKFSGtTGKFaGGYWYLQQFMREQS 463
Cdd:pfam00171 411 RRLEAGMVWIND---YTTGDADGL-PFGGFKQSG-FGRE-GGPYGLEEYTEVKT 458
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
36-465 |
3.98e-151 |
|
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: 437.02 E-value: 3.98e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFYSREitaADGYRFDTGEPTPGQHTT 115
Cdd:cd07078 14 WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGL---ARRLHGEVIPSPDPGELA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 116 NLLR-PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPL 194
Cdd:cd07078 91 IVRRePLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 195 VEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVY 274
Cdd:cd07078 171 ASHPRVDKISFTGSTAVGKAIMRAAAENLKR--VTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 275 ENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSVisdSDLPDGRYVEPTVVT 353
Cdd:cd07078 249 ESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGaKLLCGGKR---LEGGKGYFVPPTVLT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 354 EIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKqsatTGALVQA 433
Cdd:cd07078 326 DVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDY----SVGAEPS 401
|
410 420 430
....*....|....*....|....*....|..
gi 2082837691 434 QPFGGWKFSGtTGKFaGGYWYLQQFMREQSRT 465
Cdd:cd07078 402 APFGGVKQSG-IGRE-GGPYGLEEYTEPKTVT 431
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
4-463 |
9.36e-143 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 418.57 E-value: 9.36e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 4 PGDTTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDE 83
Cdd:PRK03137 57 PANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 84 AIDFLEFYSRE-ITAADGyrfDTGEPTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLV 162
Cdd:PRK03137 137 AIDFLEYYARQmLKLADG---KPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 163 AHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGI-ERTF-----QELGKRgpVIAELGGKN 236
Cdd:PRK03137 214 AAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIyERAAkvqpgQIWLKR--VIAEMGGKD 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 237 PVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDReTFVSPLIDDEAVDR- 315
Cdd:PRK03137 292 AIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN-AYMGPVINQASFDKi 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 316 --YREIstqARSDGTVLTGGsvisDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGL 393
Cdd:PRK03137 371 msYIEI---GKEEGRLVLGG----EGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGL 443
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 394 CAGLFSEDESEIEQWFDEIEAGMCYVNRKqsaTTGALVQAQPFGGWKFSGTTGKfAGGYWYLQQFMREQS 463
Cdd:PRK03137 444 TGAVISNNREHLEKARREFHVGNLYFNRG---CTGAIVGYHPFGGFNMSGTDSK-AGGPDYLLLFLQAKT 509
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
3-461 |
4.96e-133 |
|
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: 393.87 E-value: 4.96e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 3 SPGDTTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVD 82
Cdd:cd07125 52 DPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 83 EAIDFLEFYSREitaADGYRFDTGEPTP-GQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPL 161
Cdd:cd07125 132 EAIDFCRYYAAQ---ARELFSDPELPGPtGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 162 VAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTfqeLGKRG----PVIAELGGKNP 237
Cdd:cd07125 209 IAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRA---LAERDgpilPLIAETGGKNA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 238 VIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYR 317
Cdd:cd07125 286 MIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 318 EISTQARSDGTVLTGgsviSDSDLPDGRYVEPTVVtEIPHEHSLaREEHFVPF--VTIHPVSGLDAGIEKSNDSEFGLCA 395
Cdd:cd07125 366 AHTELMRGEAWLIAP----APLDDGNGYFVAPGII-EIVGIFDL-TTEVFGPIlhVIRFKAEDLDEAIEDINATGYGLTL 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2082837691 396 GLFSEDESEIEQWFDEIEAGMCYVNRkqsATTGALVQAQPFGGWKFSGtTGKFAGGYWYLQQFMRE 461
Cdd:cd07125 440 GIHSRDEREIEYWRERVEAGNLYINR---NITGAIVGRQPFGGWGLSG-TGPKAGGPNYLLRFGNE 501
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
4-466 |
1.19e-127 |
|
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: 379.00 E-value: 1.19e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 4 PGDTTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDE 83
Cdd:cd07131 21 PADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 84 AIDFLEFysreiTAADGYRFdTGEPTPGQ----HTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEAT 159
Cdd:cd07131 101 AIDMAQY-----AAGEGRRL-FGETVPSElpnkDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 160 PLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVI 239
Cdd:cd07131 175 PACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR--VALEMGGKNPII 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 240 VSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDD---EAVDRY 316
Cdd:cd07131 253 VMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEaqlEKVLNY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 317 REIstqARSDG-TVLTGGSVISDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCA 395
Cdd:cd07131 333 NEI---GKEEGaTLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSS 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2082837691 396 GLFSEDESEIEQWFDEIEAGMCYVNrkqSATTGALVQAqPFGGWKFSGtTGKFAGGYWYLQQFMREQSRTR 466
Cdd:cd07131 410 AIYTEDVNKAFRARRDLEAGITYVN---APTIGAEVHL-PFGGVKKSG-NGHREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
4-447 |
2.22e-122 |
|
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: 365.03 E-value: 2.22e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 4 PGDTTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDE 83
Cdd:cd07097 21 PSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 84 AIDFLEFYSREITAADGYRFDTGEPTPGQHTTNllRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVA 163
Cdd:cd07097 101 AGQIFRYYAGEALRLSGETLPSTRPGVEVETTR--EPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 164 HKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDE 243
Cdd:cd07097 179 WALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR--VQLEMGGKNPLVVLDD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 244 ADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQA 323
Cdd:cd07097 257 ADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 324 RSDG-TVLTGGSVISDSDlpDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDE 402
Cdd:cd07097 337 RSEGaKLVYGGERLKRPD--EGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSL 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2082837691 403 SEIEQWFDEIEAGMCYVNRKqsaTTGALVQAqPFGGWKFSGTTGK 447
Cdd:cd07097 415 KHATHFKRRVEAGVVMVNLP---TAGVDYHV-PFGGRKGSSYGPR 455
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
7-459 |
1.97e-121 |
|
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: 362.27 E-value: 1.97e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMA-DVDEAI 85
Cdd:cd07093 6 TGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrDIPRAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 86 DFLEFYSREITAADGYRFDTgepTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHK 165
Cdd:cd07093 86 ANFRFFADYILQLDGESYPQ---DGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 166 VMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKrgPVIAELGGKNPVIVSDEAD 245
Cdd:cd07093 163 LAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLK--PVSLELGGKNPNIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 246 LDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARS 325
Cdd:cd07093 241 LDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 326 DG-TVLTGGSVISDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESE 404
Cdd:cd07093 321 EGaTILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2082837691 405 IEQWFDEIEAGMCYVNRKqsattgaLVQ--AQPFGGWKFSGtTGKfAGGYWYLQQFM 459
Cdd:cd07093 401 AHRVARRLEAGTVWVNCW-------LVRdlRTPFGGVKASG-IGR-EGGDYSLEFYT 448
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
36-466 |
1.77e-116 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 346.14 E-value: 1.77e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFYSREitAADGYRFDTGEPTPGQHTT 115
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGL--ADKLGGPELPSPDPGGEAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 116 NLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLV 195
Cdd:cd06534 88 VRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 196 EHEAVDGIAFTGSRAVGVGIERTFQELGKrgPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYE 275
Cdd:cd06534 168 SHPRVDKISFTGSTAVGKAIMKAAAENLK--PVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 276 NIVDSFTDRLVeetenlvvgqptdretfvspliddeavdryreistqarsdgtvltggsvisdsdlpdgryvepTVVTEI 355
Cdd:cd06534 246 SIYDEFVEKLV---------------------------------------------------------------TVLVDV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 356 PHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKQSATTGalvqAQP 435
Cdd:cd06534 263 DPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGP----EAP 338
|
410 420 430
....*....|....*....|....*....|.
gi 2082837691 436 FGGWKFSGtTGKfAGGYWYLQQFMREQSRTR 466
Cdd:cd06534 339 FGGVKNSG-IGR-EGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
7-465 |
8.54e-115 |
|
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: 345.70 E-value: 8.54e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAID 86
Cdd:cd07086 22 NGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMID 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 87 FLEFY---SREItaaDGYRFDTgEpTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVA 163
Cdd:cd07086 102 ICDYAvglSRML---YGLTIPS-E-RPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 164 HKVMDLFEEA----GIPDGVLNLVTGDGPTtGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVI 239
Cdd:cd07086 177 IAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGR--VLLELGGNNAII 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 240 VSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREI 319
Cdd:cd07086 254 VMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 320 STQARSDG-TVLTGGSVISDSDlpDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLF 398
Cdd:cd07086 334 IEIAKSQGgTVLTGGKRIDGGE--PGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIF 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2082837691 399 SEDESEIEQWFD--EIEAGMCYVNrkqSATTGALVQAqPFGGWKFSGttGKFAGGYWYLQQFMREQSRT 465
Cdd:cd07086 412 TEDLREAFRWLGpkGSDCGIVNVN---IPTSGAEIGG-AFGGEKETG--GGRESGSDAWKQYMRRSTCT 474
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
3-465 |
4.83e-114 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 344.95 E-value: 4.83e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 3 SPGDTTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVD 82
Cdd:cd07083 38 SPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 83 EAIDFLEFYSReitAADGYRFDTGE--PTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATP 160
Cdd:cd07083 118 EAIDFIRYYAR---AALRLRYPAVEvvPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 161 LVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRG----PVIAELGGKN 236
Cdd:cd07083 195 VVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPGQtwfkRLYVETGGKN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 237 PVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEA---V 313
Cdd:cd07083 275 AIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQeakV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 314 DRYREIstqARSDGTVLTGGSVisdsDLPDGRYVEPTVVTEIPHEHSLAREEHFVPF--VTIHPVSGLDAGIEKSNDSEF 391
Cdd:cd07083 355 LSYIEH---GKNEGQLVLGGKR----LEGEGYFVAPTVVEEVPPKARIAQEEIFGPVlsVIRYKDDDFAEALEVANSTPY 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2082837691 392 GLCAGLFSEDESEIEQWFDEIEAGMCYVNRKQsatTGALVQAQPFGGWKFSGTTGKfAGGYWYLQQFMREQSRT 465
Cdd:cd07083 428 GLTGGVYSRKREHLEEARREFHVGNLYINRKI---TGALVGVQPFGGFKLSGTNAK-TGGPHYLRRFLEMKAVA 497
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
7-466 |
3.91e-113 |
|
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: 340.74 E-value: 3.91e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAID 86
Cdd:cd07099 5 TGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 87 FLEFYSREITAADGYRF-DTGEPTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHK 165
Cdd:cd07099 85 AIDWAARNAPRVLAPRKvPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 166 VMDLFEEAGIPDGVLNLVTGDGPtTGQPLVEHEaVDGIAFTGS----RAVGVGIERTFQelgkrgPVIAELGGKNPVIVS 241
Cdd:cd07099 165 LAEAWAAAGPPQGVLQVVTGDGA-TGAALIDAG-VDKVAFTGSvatgRKVMAAAAERLI------PVVLELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 242 DEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREIST 321
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 322 QARSDG-TVLTGGSVISDsdlpDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSE 400
Cdd:cd07099 317 DAVAKGaKALTGGARSNG----GGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSR 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 401 DESEIEQWFDEIEAGMCYVNrkqSATTGALVQAQPFGGWKFSGttgkfaGGYWY----LQQFMREQSRTR 466
Cdd:cd07099 393 DLARAEAIARRLEAGAVSIN---DVLLTAGIPALPFGGVKDSG------GGRRHgaegLREFCRPKAIAR 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
11-444 |
1.03e-111 |
|
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: 337.26 E-value: 1.03e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 11 IGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEF 90
Cdd:cd07149 12 IGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 91 ysreitAADGYRFDTGEPTPGQHTTN--------LLRPYGVFGVISPFNFPLAiLVGMTTG-ALITGNTVVLKPAEATPL 161
Cdd:cd07149 92 ------SAEEAKRLAGETIPFDASPGgegrigftIREPIGVVAAITPFNFPLN-LVAHKVGpAIAAGNAVVLKPASQTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 162 VAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTfqeLGKRgPVIAELGGKNPVIVS 241
Cdd:cd07149 165 SALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARK---AGLK-KVTLELGSNAAVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 242 DEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREIST 321
Cdd:cd07149 241 ADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 322 QARSDG-TVLTGGSVisdsdlpDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSE 400
Cdd:cd07149 321 EAVEGGaRLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTN 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2082837691 401 DESEIEQWFDEIEAGMCYVNRkqsaTTGALVQAQPFGGWKFSGT 444
Cdd:cd07149 394 DLQKALKAARELEVGGVMIND----SSTFRVDHMPYGGVKESGT 433
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
7-443 |
3.17e-111 |
|
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: 335.94 E-value: 3.17e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAID 86
Cdd:cd07103 6 TGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 87 FLEFYSREITAADGyrfDTGE-PTPGQHTTNLLRPYGVFGVISPFNFPLAilvgMTT----GALITGNTVVLKPAEATPL 161
Cdd:cd07103 86 FLEWFAEEARRIYG---RTIPsPAPGKRILVIKQPVGVVAAITPWNFPAA----MITrkiaPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 162 VAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGvgiertfQELGKRG-----PVIAELGGKN 236
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVG-------KLLMAQAadtvkRVSLELGGNA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 237 PVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRY 316
Cdd:cd07103 232 PFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 317 REISTQARSDG-TVLTGGSVISDsdlpDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCA 395
Cdd:cd07103 312 EALVEDAVAKGaKVLTGGKRLGL----GGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2082837691 396 GLFSEDESEIEQWFDEIEAGMCYVNrkqsatTGALVQAQ-PFGGWKFSG 443
Cdd:cd07103 388 YVFTRDLARAWRVAEALEAGMVGIN------TGLISDAEaPFGGVKESG 430
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
36-462 |
3.43e-110 |
|
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: 332.57 E-value: 3.43e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLefysREiTAADGYRFdTGE----PTPG 111
Cdd:cd07104 16 WAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAIL----RE-AAGLPRRP-EGEilpsDVPG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 112 QHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATP-----LVAHkvmdLFEEAGIPDGVLNLVTGD 186
Cdd:cd07104 90 KESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIAE----IFEEAGLPKGVLNVVPGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 187 GPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCS 266
Cdd:cd07104 166 GSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKK--VALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 267 ATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSVisdsdlpDGR 345
Cdd:cd07104 244 AAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGaRLLTGGTY-------EGL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 346 YVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrKQSA 425
Cdd:cd07104 317 FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIN-DQTV 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 2082837691 426 TTGALVqaqPFGGWKFSGtTGKFaGGYWYLQQFMREQ 462
Cdd:cd07104 396 NDEPHV---PFGGVKASG-GGRF-GGPASLEEFTEWQ 427
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
36-443 |
1.44e-107 |
|
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: 326.82 E-value: 1.44e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFYSreiTAADGYRFDTgEPT--PGQH 113
Cdd:cd07114 37 WRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYA---GLADKIEGAV-IPVdkGDYL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 114 TTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQP 193
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 194 LVEHEAVDGIAFTGSRAVGVGIERTFQElgKRGPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYV 273
Cdd:cd07114 193 LVEHPLVAKIAFTGGTETGRHIARAAAE--NLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 274 YENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSVISDSDLPDGRYVEPTVV 352
Cdd:cd07114 271 QRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGaRVLTGGERPSGADLGAGYFFEPTIL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 353 TEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqsaTTGALVQ 432
Cdd:cd07114 351 ADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVN-----TYRALSP 425
|
410
....*....|.
gi 2082837691 433 AQPFGGWKFSG 443
Cdd:cd07114 426 SSPFGGFKDSG 436
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
7-462 |
4.53e-105 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 320.75 E-value: 4.53e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAID 86
Cdd:cd07088 22 TGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 87 FLEFYsreitaADGYRFDTGE----PTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLV 162
Cdd:cd07088 102 YIDYM------AEWARRIEGEiipsDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 163 AHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKrgPVIAELGGKNPVIVSD 242
Cdd:cd07088 176 ALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENIT--KVSLELGGKAPAIVMK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 243 EADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQ 322
Cdd:cd07088 254 DADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVER 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 323 ARSDG-TVLTGGSVisdSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSED 401
Cdd:cd07088 334 AVEAGaTLLTGGKR---PEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTEN 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2082837691 402 ESEIEQWFDEIEAGMCYVNRkqsattGALVQAQPF-GGWKFSGTTGkfAGGYWYLQQFMREQ 462
Cdd:cd07088 411 LNTAMRATNELEFGETYINR------ENFEAMQGFhAGWKKSGLGG--ADGKHGLEEYLQTK 464
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
36-443 |
2.29e-103 |
|
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: 316.46 E-value: 2.29e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQL-RDRKfEFAATLSLENGKTRIEAM-ADVDEAIDFLEFYSreiTAADGYrfdTGE--PTPG 111
Cdd:cd07091 59 WRKMDPRERGRLLNKLADLIeRDRD-ELAALESLDNGKPLEESAkGDVALSIKCLRYYA---GWADKI---QGKtiPIDG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 112 QHTTNLLR-PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTT 190
Cdd:cd07091 132 NFLAYTRRePIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 191 GQPLVEHEAVDGIAFTGSRAVGvgieRTFQELG-----KRgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKC 265
Cdd:cd07091 212 GAAISSHMDVDKIAFTGSTAVG----RTIMEAAaksnlKK--VTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCC 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 266 SATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSVISDsdlpDG 344
Cdd:cd07091 286 CAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGaTLLTGGERHGS----KG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 345 RYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqs 424
Cdd:cd07091 362 YFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN---- 437
|
410
....*....|....*....
gi 2082837691 425 aTTGALVQAQPFGGWKFSG 443
Cdd:cd07091 438 -TYNVFDAAVPFGGFKQSG 455
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
11-444 |
1.45e-102 |
|
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: 313.90 E-value: 1.45e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 11 IGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLE- 89
Cdd:cd07145 12 IDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 90 --FYSREITAADgYRFDTGEPTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVM 167
Cdd:cd07145 92 aaEEAKVLRGET-IPVDAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 168 DLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEADLD 247
Cdd:cd07145 171 KILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKK--VALELGGSDPMIVLKDADLE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 248 AAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG 327
Cdd:cd07145 249 RAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 328 -TVLTGGSVisdsdlPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIE 406
Cdd:cd07145 329 gKILYGGKR------DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRAL 402
|
410 420 430
....*....|....*....|....*....|....*...
gi 2082837691 407 QWFDEIEAGMCYVNRKQSATTGALvqaqPFGGWKFSGT 444
Cdd:cd07145 403 KVARELEAGGVVINDSTRFRWDNL----PFGGFKKSGI 436
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
36-458 |
1.59e-102 |
|
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: 313.50 E-value: 1.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEfysreiTAADGYRFDTGE----PTPG 111
Cdd:cd07150 37 WAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELLR------AAAGECRRVRGEtlpsDSPG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 112 QHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTG 191
Cdd:cd07150 111 TVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 192 QPLVEHEAVDGIAFTGSRAVGVGI-ERTFQELGKrgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSR 270
Cdd:cd07150 191 DELVDDPRVRMVTFTGSTAVGREIaEKAGRHLKK---ITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 271 VYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDGT-VLTGGSVisdsdlpDGRYVEP 349
Cdd:cd07150 268 IIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAKGAkLLTGGKY-------DGNFYQP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 350 TVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqSATTGA 429
Cdd:cd07150 341 TVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHIN---DPTILD 417
|
410 420
....*....|....*....|....*....
gi 2082837691 430 LVQAqPFGGWKFSGtTGKFaGGYWYLQQF 458
Cdd:cd07150 418 EAHV-PFGGVKASG-FGRE-GGEWSMEEF 443
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
7-443 |
1.95e-101 |
|
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: 310.82 E-value: 1.95e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAID 86
Cdd:cd07110 6 TEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 87 FLEFYSREitaADGYRFDTGEPTP---GQHTTNLLR-PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLV 162
Cdd:cd07110 86 CFEYYADL---AEQLDAKAERAVPlpsEDFKARVRRePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 163 AHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKrgPVIAELGGKNPVIVSD 242
Cdd:cd07110 163 ELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIK--PVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 243 EADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQ 322
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 323 ARSDG-TVLTGGSVisDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSED 401
Cdd:cd07110 321 GKEEGaRLLCGGRR--PAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRD 398
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2082837691 402 ESEIEQWFDEIEAGMCYVNRKQSATTGAlvqaqPFGGWKFSG 443
Cdd:cd07110 399 AERCDRVAEALEAGIVWINCSQPCFPQA-----PWGGYKRSG 435
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
36-443 |
1.21e-100 |
|
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: 309.63 E-value: 1.21e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFYSREITAADGYRFDTGEPTpgqHTT 115
Cdd:cd07119 53 WPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHV---ISR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 116 NLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLV 195
Cdd:cd07119 130 TVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 196 EHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYE 275
Cdd:cd07119 210 ESPDVDLVSFTGGTATGRSIMRAAAGNVKK--VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 276 NIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSVISDSDLPDGRYVEPTVVTE 354
Cdd:cd07119 288 SIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGaRLVCGGKRPTGDELAKGYFVEPTIFDD 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 355 IPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKQSATTGAlvqaq 434
Cdd:cd07119 368 VDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEA----- 442
|
....*....
gi 2082837691 435 PFGGWKFSG 443
Cdd:cd07119 443 PWGGYKQSG 451
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
36-443 |
4.33e-98 |
|
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: 302.95 E-value: 4.33e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFysreiTAADGYRFDtGEPTPG---- 111
Cdd:cd07082 55 WPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRD-----TIEELKRLD-GDSLPGdwfp 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 112 --QHTTNLLR--PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDG 187
Cdd:cd07082 129 gtKGKIAQVRrePLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 188 PTTGQPLVEHEAVDGIAFTGSRAVGVGIertfQELGKRGPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSA 267
Cdd:cd07082 209 REIGDPLVTHGRIDVISFTGSTEVGNRL----KKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 268 TSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSVISDSdlpdgrY 346
Cdd:cd07082 285 IKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGaTVLNGGGREGGN------L 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 347 VEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKQSAT 426
Cdd:cd07082 359 IYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRG 438
|
410
....*....|....*..
gi 2082837691 427 TGALvqaqPFGGWKFSG 443
Cdd:cd07082 439 PDHF----PFLGRKDSG 451
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
36-443 |
7.88e-98 |
|
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: 300.73 E-value: 7.88e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFysrEITAADGYRFDTGEPTPGQHTT 115
Cdd:cd07095 16 WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDI---SIKAYHERTGERATPMAQGRAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 116 NLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGdGPTTGQPLV 195
Cdd:cd07095 93 LRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG-GRETGEALA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 196 EHEAVDGIAFTGSRAVGVGIERTFqeLGKRGPVIA-ELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVY 274
Cdd:cd07095 172 AHEGIDGLLFTGSAATGLLLHRQF--AGRPGKILAlEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 275 ENIV-DSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYreISTQARsdgTVLTGGSVISDSDLPDGR--YVEPTV 351
Cdd:cd07095 250 DGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARY--LLAQQD---LLALGGEPLLAMERLVAGtaFLSPGI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 352 --VTEIpheHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKqsaTTGA 429
Cdd:cd07095 325 idVTDA---ADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRP---TTGA 398
|
410
....*....|....
gi 2082837691 430 lVQAQPFGGWKFSG 443
Cdd:cd07095 399 -SSTAPFGGVGLSG 411
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
36-443 |
1.28e-97 |
|
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: 301.06 E-value: 1.28e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMA-DVDEAIDFLEFYSReitAADGyRFDTGEPTPGQHT 114
Cdd:cd07112 42 WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAvDVPSAANTFRWYAE---AIDK-VYGEVAPTGPDAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 115 TNLLR-PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQP 193
Cdd:cd07112 118 ALITRePLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 194 LVEHEAVDGIAFTGSRAVGvgieRTFQELGKRG---PVIAELGGKNPVIV-SDEADLDAAVNGVMKGAFSFAGQKCSATS 269
Cdd:cd07112 198 LGLHMDVDALAFTGSTEVG----RRFLEYSGQSnlkRVWLECGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 270 RVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSvisdSDLPD--GRY 346
Cdd:cd07112 274 RLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGaRLVAGGK----RVLTEtgGFF 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 347 VEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqsaT 426
Cdd:cd07112 350 VEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVN-----C 424
|
410
....*....|....*..
gi 2082837691 427 TGALVQAQPFGGWKFSG 443
Cdd:cd07112 425 FDEGDITTPFGGFKQSG 441
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
1-443 |
2.34e-97 |
|
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: 300.30 E-value: 2.34e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 1 MDSPGdTTRQIGTFAVGDSSEVDDA-VAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMA 79
Cdd:cd07109 1 VFDPS-TGEVFARIARGGAADVDRAvQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 80 DVDEAIDFLEFYSreiTAADGYRFDTGEPTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEAT 159
Cdd:cd07109 80 DVEAAARYFEYYG---GAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 160 PLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKrgPVIAELGGKNPVI 239
Cdd:cd07109 157 PLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVV--PVTLELGGKSPQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 240 VSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETfVSPLIDDEAVDRYREI 319
Cdd:cd07109 235 VFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPD-LGPLISAKQLDRVEGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 320 STQARSDGT-VLTGGSVISDSdLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLF 398
Cdd:cd07109 314 VARARARGArIVAGGRIAEGA-PAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVW 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2082837691 399 SEDESEIEQWFDEIEAGMCYVNrkqSATTGALVQAqPFGGWKFSG 443
Cdd:cd07109 393 TRDGDRALRVARRLRAGQVFVN---NYGAGGGIEL-PFGGVKKSG 433
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
3-465 |
2.39e-97 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 314.83 E-value: 2.39e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 3 SPGDTTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVD 82
Cdd:PRK11904 568 SPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVR 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 83 EAIDFLEFYsreitAADGYR-FDTGEPTP---GQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEA 158
Cdd:PRK11904 648 EAVDFCRYY-----AAQARRlFGAPEKLPgptGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQ 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 159 TPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTfqeLGKRG----PVIAELGG 234
Cdd:PRK11904 723 TPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRT---LAARDgpivPLIAETGG 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 235 KNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATsRV-YVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAV 313
Cdd:PRK11904 800 QNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSAL-RVlFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAK 878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 314 DRYREISTQARSDGTVLTGGSVisDSDLPDGRYVEPTVVtEIPHEHSLaREEHFVPF--VTIHPVSGLDAGIEKSNDSEF 391
Cdd:PRK11904 879 ANLDAHIERMKREARLLAQLPL--PAGTENGHFVAPTAF-EIDSISQL-EREVFGPIlhVIRYKASDLDKVIDAINATGY 954
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2082837691 392 GLCAGLFSEDESEIEQWFDEIEAGMCYVNRKQsatTGALVQAQPFGGWKFSGTTGKfAGGYWYLQQFMREQSRT 465
Cdd:PRK11904 955 GLTLGIHSRIEETADRIADRVRVGNVYVNRNQ---IGAVVGVQPFGGQGLSGTGPK-AGGPHYLLRFATEKTVT 1024
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
11-458 |
2.60e-97 |
|
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: 300.38 E-value: 2.60e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 11 IGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFL-- 88
Cdd:cd07151 23 LAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAITre 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 89 --EFYSR---EITAADgyrfdtgepTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATP--- 160
Cdd:cd07151 103 aaTFPLRmegRILPSD---------VPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPitg 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 161 --LVAHkvmdLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPV 238
Cdd:cd07151 174 glLLAK----IFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKK--VALELGGNNPF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 239 IVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYRE 318
Cdd:cd07151 248 VVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 319 ISTQARSDG-TVLTGGSVisdsdlpDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGL 397
Cdd:cd07151 328 KIEQAVEEGaTLLVGGEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2082837691 398 FSEDESEIEQWFDEIEAGMCYVNrKQSATTGALVqaqPFGGWKFSGtTGKFaGGYWYLQQF 458
Cdd:cd07151 401 FTSDLERGVQFARRIDAGMTHIN-DQPVNDEPHV---PFGGEKNSG-LGRF-NGEWALEEF 455
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
3-465 |
1.60e-96 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 314.57 E-value: 1.60e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 3 SPGDTTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVD 82
Cdd:COG4230 576 NPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVR 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 83 EAIDFLEFYSREItaadgyRFDTGEPTPgqhttnlLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLV 162
Cdd:COG4230 656 EAVDFCRYYAAQA------RRLFAAPTV-------LRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLI 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 163 AHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTfqeLGKRG----PVIAELGGKNPV 238
Cdd:COG4230 723 AARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRT---LAARDgpivPLIAETGGQNAM 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 239 IVSDEADLDAAVNGVMKGAFSFAGQKCSATsRV-YVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEA---VD 314
Cdd:COG4230 800 IVDSSALPEQVVDDVLASAFDSAGQRCSAL-RVlCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEAranLE 878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 315 RYREistQARSDGTVLTGGSVisDSDLPDGRYVEPTVVtEIPHEHSLAReEHFVPFVtiHPV----SGLDAGIEKSNDSE 390
Cdd:COG4230 879 AHIE---RMRAEGRLVHQLPL--PEECANGTFVAPTLI-EIDSISDLER-EVFGPVL--HVVrykaDELDKVIDAINATG 949
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2082837691 391 FGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKQsatTGALVQAQPFGGWKFSGTTGKfAGGYWYLQQFMREQSRT 465
Cdd:COG4230 950 YGLTLGVHSRIDETIDRVAARARVGNVYVNRNI---IGAVVGVQPFGGEGLSGTGPK-AGGPHYLLRFATERTVT 1020
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
7-443 |
1.20e-95 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 295.89 E-value: 1.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAM-ADVDEAI 85
Cdd:cd07115 6 TGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLDVPRAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 86 DFLEFYSREITAADGyrfDTGEPTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHK 165
Cdd:cd07115 86 DTFRYYAGWADKIEG---EVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 166 VMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEAD 245
Cdd:cd07115 163 IAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKR--VSLELGGKSANIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 246 LDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARS 325
Cdd:cd07115 241 LDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 326 DG-TVLTGGSVISDSdlpdGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESE 404
Cdd:cd07115 321 EGaRLLTGGKRPGAR----GFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430
....*....|....*....|....*....|....*....
gi 2082837691 405 IEQWFDEIEAGMCYVNrkqsaTTGALVQAQPFGGWKFSG 443
Cdd:cd07115 397 AHRVAAALKAGTVWIN-----TYNRFDPGSPFGGYKQSG 430
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
7-443 |
1.25e-95 |
|
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: 296.14 E-value: 1.25e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAID 86
Cdd:cd07090 6 TGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 87 FLEFYSREITAADGYRFDTGEptpGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKV 166
Cdd:cd07090 86 CLEYYAGLAPTLSGEHVPLPG---GSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 167 MDLFEEAGIPDGVLNLVTGDGpTTGQPLVEHEAVDGIAFTGSRAVGVGIERtfQELGKRGPVIAELGGKNPVIVSDEADL 246
Cdd:cd07090 163 AEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMS--AAAKGIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 247 DAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSD 326
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 327 G-TVLTGGSVISDSD-LPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESE 404
Cdd:cd07090 320 GaKVLCGGERVVPEDgLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQR 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2082837691 405 IEQWFDEIEAGMCYVNrkqsatTGALVQAQ-PFGGWKFSG 443
Cdd:cd07090 400 AHRVIAQLQAGTCWIN------TYNISPVEvPFGGYKQSG 433
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
3-444 |
8.28e-94 |
|
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: 291.20 E-value: 8.28e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 3 SPGdTTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVD 82
Cdd:cd07107 3 NPA-TGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 83 EAIDFLEFYSREITAADGyrfDTGEPTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLV 162
Cdd:cd07107 82 VAAALLDYFAGLVTELKG---ETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 163 AHKVMDLFEEAgIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKrgPVIAELGGKNPVIVSD 242
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK--HVTLELGGKNALIVFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 243 EADLDAAVNGVMKGA-FSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREIST 321
Cdd:cd07107 236 DADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 322 QARSDGT-VLTGGSVISDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSE 400
Cdd:cd07107 316 SAKREGArLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2082837691 401 DESEIEQWFDEIEAGMCYVNRKQSATTGAlvqaqPFGGWKFSGT 444
Cdd:cd07107 396 DISQAHRTARRVEAGYVWINGSSRHFLGA-----PFGGVKNSGI 434
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
6-443 |
1.06e-92 |
|
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: 288.49 E-value: 1.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 6 DTTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKT-RIEAMADVDEA 84
Cdd:cd07108 5 ATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNAlRTQARPEAAVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 85 IDFLEFYSREITAADGyrfDTGEPTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAH 164
Cdd:cd07108 85 ADLFRYFGGLAGELKG---ETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 165 KVMDLFEEAgIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTfqELGKRGPVIAELGGKNPVIVSDEA 244
Cdd:cd07108 162 LLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRA--AADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 245 DLDAAVNGVMKGA-FSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDR---YREIS 320
Cdd:cd07108 239 DLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKvcgYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 321 tQARSDGTVLTGGSVISDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSE 400
Cdd:cd07108 319 -LSTSGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2082837691 401 DESEIEQWFDEIEAGMCYVNRkqsatTGALVQAQPFGGWKFSG 443
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVNQ-----GGGQQPGQSYGGFKQSG 435
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
3-461 |
1.22e-92 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 304.87 E-value: 1.22e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 3 SPGDTTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVD 82
Cdd:PRK11905 573 NPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVR 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 83 EAIDFLEFYSREITAAdgyrfdtgePTPGQHttnllRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLV 162
Cdd:PRK11905 653 EAVDFLRYYAAQARRL---------LNGPGH-----KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLI 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 163 AHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQE-LGKRGPVIAELGGKNPVIVS 241
Cdd:PRK11905 719 AARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKrSGPPVPLIAETGGQNAMIVD 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 242 DEADLDAAVNGVMKGAFSFAGQKCSATsRV-YVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREIS 320
Cdd:PRK11905 799 SSALPEQVVADVIASAFDSAGQRCSAL-RVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHI 877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 321 TQARSDGTVLTggSVISDSDLPDGRYVEPTVVtEIPHEHSLAReEHFVPFVtiHPV----SGLDAGIEKSNDSEFGLCAG 396
Cdd:PRK11905 878 EAMRAAGRLVH--QLPLPAETEKGTFVAPTLI-EIDSISDLER-EVFGPVL--HVVrfkaDELDRVIDDINATGYGLTFG 951
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2082837691 397 LFSEDESEIEQWFDEIEAGMCYVNRKQsatTGALVQAQPFGGWKFSGTTGKfAGGYWYLQQFMRE 461
Cdd:PRK11905 952 LHSRIDETIAHVTSRIRAGNIYVNRNI---IGAVVGVQPFGGEGLSGTGPK-AGGPLYLGRLVRE 1012
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
11-443 |
1.91e-91 |
|
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: 285.10 E-value: 1.91e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 11 IGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEF 90
Cdd:cd07094 12 IGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 91 ysreitAADGYRFDTGEPTPGQHTTN--------LLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLV 162
Cdd:cd07094 92 ------AAEEAERIRGEEIPLDATQGsdnrlawtIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 163 AHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERtfQELGKRgpVIAELGGKNPVIVSD 242
Cdd:cd07094 166 ALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRA--NAGGKR--IALELGGNAPVIVDR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 243 EADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRY-REIST 321
Cdd:cd07094 242 DADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVeRWVEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 322 QARSDGTVLTGGSvisdsdlPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSED 401
Cdd:cd07094 322 AVEAGARLLCGGE-------RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2082837691 402 ESEIEQWFDEIEAGMCYVNRkqsaTTGALVQAQPFGGWKFSG 443
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVND----SSAFRTDWMPFGGVKESG 432
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
7-447 |
6.13e-91 |
|
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: 283.83 E-value: 6.13e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMAD-VDEAI 85
Cdd:cd07092 6 TGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDeLPGAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 86 DFLEFYSREITAADGYRfdTGEPTPGqHTTNLLR-PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAH 164
Cdd:cd07092 86 DNFRFFAGAARTLEGPA--AGEYLPG-HTSMIRRePIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 165 KVMDLFEEaGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEA 244
Cdd:cd07092 163 LLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKR--VHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 245 DLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQAR 324
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 325 SDGTVLTGGSVISDsdlpDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESE 404
Cdd:cd07092 320 AHARVLTGGRRAEG----PGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2082837691 405 IEQWFDEIEAGMCYVNrkqsaTTGALVQAQPFGGWKFSGtTGK 447
Cdd:cd07092 396 AMRLSARLDFGTVWVN-----THIPLAAEMPHGGFKQSG-YGK 432
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
3-458 |
8.92e-91 |
|
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: 285.63 E-value: 8.92e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 3 SPGDTTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRK-FEFAATLSLENGKTRIEAMADV 81
Cdd:cd07123 52 MPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYELNAATMLGQGKNVWQAEIDA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 82 D-EAIDFLEF---YSREITAADgyrfdtgEPTPGQHTTNLL--RPY-GVFGVISPFNFPlAILVGMTTGALITGNTVVLK 154
Cdd:cd07123 132 AcELIDFLRFnvkYAEELYAQQ-------PLSSPAGVWNRLeyRPLeGFVYAVSPFNFT-AIGGNLAGAPALMGNVVLWK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 155 PAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAV----------GVGIERTFQELgk 224
Cdd:cd07123 204 PSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTfkslwkqigeNLDRYRTYPRI-- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 225 rgpvIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFV 304
Cdd:cd07123 282 ----VGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFM 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 305 SPLIDDEAVDRYREISTQARSDG--TVLTGGSViSDSdlpDGRYVEPTVV-TEIPHeHSLAREEHFVPFVTIH--PVSGL 379
Cdd:cd07123 358 GAVIDEKAFDRIKGYIDHAKSDPeaEIIAGGKC-DDS---VGYFVEPTVIeTTDPK-HKLMTEEIFGPVLTVYvyPDSDF 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 380 DAGIEKSND-SEFGLCAGLFSEDESEIEQWFDEIE--AGMCYVNRKqsaTTGALVQAQPFGGWKFSGTTGKfAGGYWYLQ 456
Cdd:cd07123 433 EETLELVDTtSPYALTGAIFAQDRKAIREATDALRnaAGNFYINDK---PTGAVVGQQPFGGARASGTNDK-AGSPLNLL 508
|
..
gi 2082837691 457 QF 458
Cdd:cd07123 509 RW 510
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
7-443 |
1.03e-90 |
|
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: 284.30 E-value: 1.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSS-RAELCTRVADqLRDRKFEFAATL-SLENGKT-RIEAMADVDE 83
Cdd:cd07144 32 TGEVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGEeRGELLDKLAD-LVEKNRDLLAAIeALDSGKPyHSNALGDLDE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 84 AIDFLEFYSreiTAADGYRFDTGEPTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVA 163
Cdd:cd07144 111 IIAVIRYYA---GWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 164 HKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGvgieRTFQEL--GKRGPVIAELGGKNPVIVS 241
Cdd:cd07144 188 LYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATG----RLVMKAaaQNLKAVTLECGGKSPALVF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 242 DEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEET-ENLVVGQPTDRETFVSPLIDDEAVDRYREIS 320
Cdd:cd07144 264 EDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVVGPQVSKTQYDRVLSYI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 321 TQARSDGTVLTGGSVISDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSE 400
Cdd:cd07144 344 EKGKKEGAKLVYGGEKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTK 423
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2082837691 401 DESEIEQWFDEIEAGMCYVNRKQSATTGAlvqaqPFGGWKFSG 443
Cdd:cd07144 424 DIRRAHRVARELEAGMVWINSSNDSDVGV-----PFGGFKMSG 461
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
36-463 |
5.43e-90 |
|
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: 280.95 E-value: 5.43e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFYSrEITAADGYRFDTgeptPGQHTT 115
Cdd:cd07106 35 WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYTA-SLDLPDEVIEDD----DTRRVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 116 NLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAgIPDGVLNLVTGDGPTtGQPLV 195
Cdd:cd07106 110 LRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSGGDEL-GPALT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 196 EHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYE 275
Cdd:cd07106 188 SHPDIRKISFTGSTATGKKVMASAAKTLKR--VTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 276 NIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSVISDsdlpDGRYVEPTVVTE 354
Cdd:cd07106 266 SIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGaKVLAGGEPLDG----PGYFIPPTIVDD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 355 IPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqsaTTGALVQAQ 434
Cdd:cd07106 342 PPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN-----THGALDPDA 416
|
410 420
....*....|....*....|....*....
gi 2082837691 435 PFGGWKFSGTTGKFagGYWYLQQFMREQS 463
Cdd:cd07106 417 PFGGHKQSGIGVEF--GIEGLKEYTQTQV 443
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
36-443 |
4.21e-88 |
|
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: 276.43 E-value: 4.21e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFYsreITAADGYRfdtgEPTPGQHTT 115
Cdd:cd07102 34 WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYM---ISIAEEAL----ADIRVPEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 116 NLLR-----PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTT 190
Cdd:cd07102 107 GFERyirrePLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 191 GQpLVEHEAVDGIAFTGSRAVGVGIERTFQelGKRGPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSR 270
Cdd:cd07102 187 AA-LIADPRIDHVSFTGSVAGGRAIQRAAA--GRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIER 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 271 VYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSVISDSDlPDGRYVEP 349
Cdd:cd07102 264 IYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGaRALIDGALFPEDK-AGGAYLAP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 350 TVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRkqsatTGA 429
Cdd:cd07102 343 TVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNR-----CDY 417
|
410
....*....|....
gi 2082837691 430 LVQAQPFGGWKFSG 443
Cdd:cd07102 418 LDPALAWTGVKDSG 431
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
7-459 |
4.45e-88 |
|
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: 276.69 E-value: 4.45e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAM-ADVDEAI 85
Cdd:cd07138 23 TEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARaAQVGLGI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 86 DFLEFYsreITAADGYRFDTgepTPGqHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHK 165
Cdd:cd07138 103 GHLRAA---ADALKDFEFEE---RRG-NSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAII 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 166 VMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEAD 245
Cdd:cd07138 176 LAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKR--VALELGGKSANIILDDAD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 246 LDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARS 325
Cdd:cd07138 254 LEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 326 DG-TVLTGGsvisdSDLPDGR----YVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSE 400
Cdd:cd07138 334 EGaRLVAGG-----PGRPEGLergyFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSA 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2082837691 401 DESEIEQWFDEIEAGMCYVNRkqsattGALVQAQPFGGWKFSGtTGKfAGGYWYLQQFM 459
Cdd:cd07138 409 DPERARAVARRLRAGQVHING------AAFNPGAPFGGYKQSG-NGR-EWGRYGLEEFL 459
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
7-443 |
5.40e-88 |
|
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: 276.11 E-value: 5.40e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAID 86
Cdd:cd07101 5 TGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 87 FLEFYSReiTAAdgyRFDTGEPTPG-----QHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPL 161
Cdd:cd07101 85 VARYYAR--RAE---RLLKPRRRRGaipvlTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 162 VAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHeaVDGIAFTGSRAVGvgiERTFQELGKR-GPVIAELGGKNPVIV 240
Cdd:cd07101 160 TALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATG---RVVAERAGRRlIGCSLELGGKNPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 241 SDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREIS 320
Cdd:cd07101 235 LEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 321 TQARSDG-TVLTGGSVisdsdLPD-GRYV-EPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGL 397
Cdd:cd07101 315 DDAVAKGaTVLAGGRA-----RPDlGPYFyEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2082837691 398 FSEDESEIEQWFDEIEAGMCYVNRKQSATTGALvqAQPFGGWKFSG 443
Cdd:cd07101 390 WTRDGARGRRIAARLRAGTVNVNEGYAAAWASI--DAPMGGMKDSG 433
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
36-465 |
8.00e-88 |
|
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: 274.84 E-value: 8.00e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFYSREITAADGYRFDTGEPtpGQHTT 115
Cdd:cd07105 16 WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIPSDKP--GTLAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 116 NLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVT---GDGPTTGQ 192
Cdd:cd07105 94 VVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVThspEDAPEVVE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 193 PLVEHEAVDGIAFTGSRAVGVGIERTFQELGKrgPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVY 272
Cdd:cd07105 174 ALIAHPAVRKVNFTGSTRVGRIIAETAAKHLK--PVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERII 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 273 VYENIVDSFTDRLVEETENLVVGQPTdretfVSPLIDDEAVDRYREISTQARSDGTVLTGGSVISDSdlPDGRYVEPTVV 352
Cdd:cd07105 252 VHESIADEFVEKLKAAAEKLFAGPVV-----LGSLVSAAAADRVKELVDDALSKGAKLVVGGLADES--PSGTSMPPTIL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 353 TEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqSATTGalVQ 432
Cdd:cd07105 325 DNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN---GMTVH--DE 399
|
410 420 430
....*....|....*....|....*....|....
gi 2082837691 433 AQ-PFGGWKFSGtTGKFaGGYWYLQQFMREQSRT 465
Cdd:cd07105 400 PTlPHGGVKSSG-YGRF-NGKWGIDEFTETKWIT 431
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
7-443 |
2.26e-87 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 276.76 E-value: 2.26e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRieAMAdVDEAID 86
Cdd:PRK09407 41 TGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKAR--RHA-FEEVLD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 87 FL---EFYSREITAADGYRFDTGePTPG-QHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLV 162
Cdd:PRK09407 118 VAltaRYYARRAPKLLAPRRRAG-ALPVlTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 163 AHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHeaVDGIAFTGSRAVGvgieRTFQEL-GKRgpVI---AELGGKNPV 238
Cdd:PRK09407 197 ALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATG----RVLAEQaGRR--LIgfsLELGGKNPM 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 239 IVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYRE 318
Cdd:PRK09407 269 IVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 319 ISTQARSDG-TVLTGGSVisdsdLPD-GRYV-EPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCA 395
Cdd:PRK09407 349 HVDDAVAKGaTVLAGGKA-----RPDlGPLFyEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNA 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2082837691 396 GLFSEDESEIEQWFDEIEAGMCYVNRKQSATTGALvqAQPFGGWKFSG 443
Cdd:PRK09407 424 SVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSV--DAPMGGMKDSG 469
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
41-447 |
5.64e-87 |
|
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: 273.47 E-value: 5.64e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 41 PSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFYSREITAADGYRFDTGEPTPGQH--TTNLL 118
Cdd:cd07146 39 RYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEALRDDGESFSCDLTANGKArkIFTLR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 119 RPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHE 198
Cdd:cd07146 119 EPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 199 AVDGIAFTGSRAVGVGIERTfqELGKRgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIV 278
Cdd:cd07146 199 DVDLVTFTGGVAVGKAIAAT--AGYKR--QLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 279 DSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDGT-VLTGGSvisdsdlPDGRYVEPTVVTEIPH 357
Cdd:cd07146 275 DEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGArVLLGNQ-------RQGALYAPTVLDHVPP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 358 EHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRkqsaTTGALVQAQPFG 437
Cdd:cd07146 348 DAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNE----VPGFRSELSPFG 423
|
410
....*....|
gi 2082837691 438 GWKFSGTTGK 447
Cdd:cd07146 424 GVKDSGLGGK 433
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
36-449 |
5.09e-86 |
|
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: 271.13 E-value: 5.09e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFysreitAADGYRFDTGEP--TPGQH 113
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRY------AASLARTLHGDSynNLGDD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 114 TTNL-LR-PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTG 191
Cdd:cd07118 111 MLGLvLRePIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 192 QPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRV 271
Cdd:cd07118 191 QAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKK--VSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 272 YVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSVISDSdlpDGRYVEPT 350
Cdd:cd07118 269 LVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGaTLLLGGERLASA---AGLFYQPT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 351 VVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqSATTGAl 430
Cdd:cd07118 346 IFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVN---TFLDGS- 421
|
410 420
....*....|....*....|..
gi 2082837691 431 vQAQPFGGWKFSG---TTGKFA 449
Cdd:cd07118 422 -PELPFGGFKQSGigrELGRYG 442
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
36-443 |
5.83e-85 |
|
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: 268.67 E-value: 5.83e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTR-IEAMADVDEAIDFLEFYSReitAADGYRFDTGEPTPGQHT 114
Cdd:cd07139 54 WPRLSPAERAAVLRRLADALEARADELARLWTAENGMPIsWSRRAQGPGPAALLRYYAA---LARDFPFEERRPGSGGGH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 115 TNLLR-PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGpTTGQP 193
Cdd:cd07139 131 VLVRRePVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADR-EVGEY 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 194 LVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYV 273
Cdd:cd07139 210 LVRHPGVDKVSFTGSTAAGRRIAAVCGERLAR--VTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 274 YENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSVisDSDLPDGRYVEPTVV 352
Cdd:cd07139 288 PRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGaRLVTGGGR--PAGLDRGWFVEPTLF 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 353 TEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDEseieqwfdeiEAGMCYVNRKQSATTG---- 428
Cdd:cd07139 366 ADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADV----------ERGLAVARRIRTGTVGvngf 435
|
410
....*....|....*
gi 2082837691 429 ALVQAQPFGGWKFSG 443
Cdd:cd07139 436 RLDFGAPFGGFKQSG 450
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
11-463 |
1.34e-84 |
|
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: 267.57 E-value: 1.34e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 11 IGTFAVGDSSEVDDAVAAATAAQPAWE-AMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTR--IEAMAdVDEAIDF 87
Cdd:cd07089 10 IGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVmtARAMQ-VDGPIGH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 88 LEFYSREITAADGYRFDTGEPTPGQHTTNLLR--PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHK 165
Cdd:cd07089 89 LRYFADLADSFPWEFDLPVPALRGGPGRRVVRrePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 166 VMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEAD 245
Cdd:cd07089 169 LGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKR--VLLELGGKSANIVLDDAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 246 LDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARS 325
Cdd:cd07089 247 LAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 326 DG-TVLTGGSviSDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESE 404
Cdd:cd07089 327 EGaRLVTGGG--RPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDR 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2082837691 405 IEQWFDEIEAGMCYVNrkqsaTTGALVQAQPFGGWKFSGtTGKfAGGYWYLQQFMREQS 463
Cdd:cd07089 405 AYRVARRIRTGSVGIN-----GGGGYGPDAPFGGYKQSG-LGR-ENGIEGLEEFLETKS 456
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
11-456 |
4.00e-84 |
|
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: 267.05 E-value: 4.00e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 11 IGTFAVGDSSEVDDAVAAATAA--QPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKT-RIEAMADVDEAIDF 87
Cdd:cd07142 32 IAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPyEQARYAEVPLAARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 88 LEFYSreiTAADGYRFDTGEPTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVM 167
Cdd:cd07142 112 FRYYA---GWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 168 DLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGvgieRTFQELGKRG---PVIAELGGKNPVIVSDEA 244
Cdd:cd07142 189 KLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVG----KIIMQLAAKSnlkPVTLELGGKSPFIVCEDA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 245 DLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDR-YREISTQA 323
Cdd:cd07142 265 DVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKiLSYIEHGK 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 324 RSDGTVLTGGSVISDSdlpdGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDES 403
Cdd:cd07142 345 EEGATLITGGDRIGSK----GYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNID 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2082837691 404 EIEQWFDEIEAGMCYVNrkqsaTTGALVQAQPFGGWKFSGtTGKFAGGYW---YLQ 456
Cdd:cd07142 421 TANTLSRALKAGTVWVN-----CYDVFDASIPFGGYKMSG-IGREKGIYAlnnYLQ 470
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
7-443 |
7.97e-84 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 266.00 E-value: 7.97e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADvdeaid 86
Cdd:PRK13473 26 TGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALND------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 87 flefysrEITA-ADGYRF-----------DTGEPTPGqHTTNLLR-PYGVFGVISPFNFPLAILVGMTTGALITGNTVVL 153
Cdd:PRK13473 100 -------EIPAiVDVFRFfagaarclegkAAGEYLEG-HTSMIRRdPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 154 KPAEATPLVAHKVMDLFEEAgIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELG 233
Cdd:PRK13473 172 KPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKR--THLELG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 234 GKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAV 313
Cdd:PRK13473 249 GKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 314 DRYREISTQARSDG--TVLTGGSVISDsdlpDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEF 391
Cdd:PRK13473 329 DRVAGFVERAKALGhiRVVTGGEAPDG----KGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDY 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2082837691 392 GLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqsaTTGALVQAQPFGGWKFSG 443
Cdd:PRK13473 405 GLASSVWTRDVGRAHRVSARLQYGCTWVN-----THFMLVSEMPHGGQKQSG 451
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
11-443 |
4.87e-83 |
|
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: 263.44 E-value: 4.87e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 11 IGTFAVGDSSEVDDAVAAATA--AQPAWeAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFL 88
Cdd:cd07120 10 IGTYADGGVAEAEAAIAAARRafDETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 89 EFYSREITAADGYrfdTGEPTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMD 168
Cdd:cd07120 89 RYYAGLARTEAGR---MIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 169 LFEEA-GIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEADLD 247
Cdd:cd07120 166 ILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKR--LGLELGGKTPCIVFDDADLD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 248 AAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG 327
Cdd:cd07120 244 AALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 328 --TVLTGGSVisDSDLPDGRYVEPTVVtEIPHEHS-LAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESE 404
Cdd:cd07120 324 aeVVLRGGPV--TEGLAKGAFLRPTLL-EVDDPDAdIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLAR 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 2082837691 405 IEQWFDEIEAGMCYVNrkqsaTTGALVQAQPFGGWKFSG 443
Cdd:cd07120 401 AMRVARAIRAGTVWIN-----DWNKLFAEAEEGGYRQSG 434
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
3-462 |
9.07e-83 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 264.08 E-value: 9.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 3 SPGDTTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVD 82
Cdd:TIGR01238 57 NPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 83 EAIDFLEFYSREItaadgyRFDTGEPTpgqhttnlLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLV 162
Cdd:TIGR01238 137 EAVDFCRYYAKQV------RDVLGEFS--------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 163 AHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTF-QELGKRGPVIAELGGKNPVIVS 241
Cdd:TIGR01238 203 AYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLaQREDAPVPLIAETGGQNAMIVD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 242 DEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREIST 321
Cdd:TIGR01238 283 STALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 322 QARSDGTVLTGGSVISDSDLPDGRYVEPTVVtEIPHEHSLAREEhFVPFVTI--HPVSGLDAGIEKSNDSEFGLCAGLFS 399
Cdd:TIGR01238 363 HMSQTQKKIAQLTLDDSRACQHGTFVAPTLF-ELDDIAELSEEV-FGPVLHVvrYKARELDQIVDQINQTGYGLTMGVHS 440
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2082837691 400 EDESEIEQWFDEIEAGMCYVNRKQsatTGALVQAQPFGGWKFSGtTGKFAGGYWYLQQFMREQ 462
Cdd:TIGR01238 441 RIETTYRWIEKHARVGNCYVNRNQ---VGAVVGVQPFGGQGLSG-TGPKAGGPHYLYRLTQVQ 499
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
36-443 |
6.57e-82 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 261.43 E-value: 6.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFysrEITAadgYRFDTGE---PTPGq 112
Cdd:PRK09457 53 WARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAMINKIAI---SIQA---YHERTGEkrsEMAD- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 113 hTTNLLR--PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGdGPTT 190
Cdd:PRK09457 126 -GAAVLRhrPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRET 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 191 GQPLVEHEAVDGIAFTGSRAVGVGIERTFQelGKRGPVIA-ELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATS 269
Cdd:PRK09457 204 GKALAAHPDIDGLLFTGSANTGYLLHRQFA--GQPEKILAlEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCAR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 270 RVYVYENIV-DSFTDRLVEETENLVVGQP-TDRETFVSPLIDDEAVDRYreISTQARsdgTVLTGGSVISDSDLPDGR-- 345
Cdd:PRK09457 282 RLLVPQGAQgDAFLARLVAVAKRLTVGRWdAEPQPFMGAVISEQAAQGL--VAAQAQ---LLALGGKSLLEMTQLQAGtg 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 346 YVEP-----TVVTEIPHehslarEEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMcyVN 420
Cdd:PRK09457 357 LLTPgiidvTGVAELPD------EEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGI--VN 428
|
410 420
....*....|....*....|....
gi 2082837691 421 R-KQsaTTGAlVQAQPFGGWKFSG 443
Cdd:PRK09457 429 WnKP--LTGA-SSAAPFGGVGASG 449
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
7-443 |
1.53e-81 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 260.82 E-value: 1.53e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAA-----ATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADV 81
Cdd:PLN02467 32 TEETIGDIPAATAEDVDAAVEAarkafKRNKGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 82 DEAIDFLEFYSREITAADGYRFDTGEPTPGQHTTNLLR-PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATP 160
Cdd:PLN02467 112 DDVAGCFEYYADLAEALDAKQKAPVSLPMETFKGYVLKePLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELAS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 161 LVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKrgPVIAELGGKNPVIV 240
Cdd:PLN02467 192 VTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVK--PVSLELGGKSPIIV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 241 SDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREIS 320
Cdd:PLN02467 270 FDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 321 TQARSDG-TVLTGGSviSDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFS 399
Cdd:PLN02467 350 STAKSEGaTILCGGK--RPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVIS 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2082837691 400 EDESEIEQWFDEIEAGMCYVNRKQSattgALVQAqPFGGWKFSG 443
Cdd:PLN02467 428 NDLERCERVSEAFQAGIVWINCSQP----CFCQA-PWGGIKRSG 466
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
36-443 |
1.57e-81 |
|
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: 258.54 E-value: 1.57e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFYsreitAADGYRF--DTGEPTPGQH 113
Cdd:cd07100 15 WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYY-----AENAEAFlaDEPIETDAGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 114 TTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQp 193
Cdd:cd07100 90 AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVEA- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 194 LVEHEAVDGIAFTGS----RAVGvgiertfQELGKRG-PVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSAT 268
Cdd:cd07100 169 IIADPRVRGVTLTGSeragRAVA-------AEAGKNLkKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 269 SRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSVISdsdlPDGRYV 347
Cdd:cd07100 242 KRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGaTLLLGGKRPD----GPGAFY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 348 EPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKqSATT 427
Cdd:cd07100 318 PPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGM-VKSD 396
|
410
....*....|....*.
gi 2082837691 428 GALvqaqPFGGWKFSG 443
Cdd:cd07100 397 PRL----PFGGVKRSG 408
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
9-465 |
1.65e-81 |
|
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: 259.15 E-value: 1.65e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 9 RQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFL 88
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 89 EFYSREITAADGYRFDTGeptPGQhtTNLLR--PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPlVAHKV 166
Cdd:cd07152 82 HEAAGLPTQPQGEILPSA---PGR--LSLARrvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTP-VSGGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 167 M--DLFEEAGIPDGVLNLVTGdGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEA 244
Cdd:cd07152 156 ViaRLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKK--VSLELGGKNALIVLDDA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 245 DLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQAR 324
Cdd:cd07152 233 DLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 325 SDG-TVLTGGSVisdsdlpDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDES 403
Cdd:cd07152 313 AAGaRLEAGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVG 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2082837691 404 EIEQWFDEIEAGMCYVNrKQSATTGALVqaqPFGGWKFSGTTGKFaGGYWYLQQFMREQSRT 465
Cdd:cd07152 386 RAMALADRLRTGMLHIN-DQTVNDEPHN---PFGGMGASGNGSRF-GGPANWEEFTQWQWVT 442
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
11-443 |
1.71e-81 |
|
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: 259.10 E-value: 1.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 11 IGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEF 90
Cdd:cd07147 12 VARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 91 YSREITAADG--YRFDTGEPTPGQhtTNLLR--PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKV 166
Cdd:cd07147 92 AAEEATRIYGevLPLDISARGEGR--QGLVRrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 167 MDLFEEAGIPDGVLNLVTGDGPTTgQPLVEHEAVDGIAFTGSRAVGVGIERtfqELGKRgPVIAELGGKNPVIVSDEADL 246
Cdd:cd07147 170 GEVLAETGLPKGAFSVLPCSRDDA-DLLVTDERIKLLSFTGSPAVGWDLKA---RAGKK-KVVLELGGNAAVIVDSDADL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 247 DAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSD 326
Cdd:cd07147 245 DFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 327 G-TVLTGGSVisdsdlpDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEI 405
Cdd:cd07147 325 GaKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKA 397
|
410 420 430
....*....|....*....|....*....|....*...
gi 2082837691 406 EQWFDEIEAGMCYVNRKQSATtgalVQAQPFGGWKFSG 443
Cdd:cd07147 398 LRAWDELEVGGVVINDVPTFR----VDHMPYGGVKDSG 431
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
36-444 |
4.05e-81 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 259.62 E-value: 4.05e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFYSREitAADGYRFDTGEPTPGQHTT 115
Cdd:PLN02278 78 WSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEE--AKRVYGDIIPSPFPDRRLL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 116 NLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLV 195
Cdd:PLN02278 156 VLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 196 EHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYE 275
Cdd:PLN02278 236 ASPKVRKITFTGSTAVGKKLMAGAAATVKR--VSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 276 NIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDGT-VLTGGSVISDSdlpdGRYVEPTVVTE 354
Cdd:PLN02278 314 GIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAkVLLGGKRHSLG----GTFYEPTVLGD 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 355 IPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKQSATTGAlvqaq 434
Cdd:PLN02278 390 VTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA----- 464
|
410
....*....|
gi 2082837691 435 PFGGWKFSGT 444
Cdd:PLN02278 465 PFGGVKQSGL 474
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
41-452 |
1.16e-80 |
|
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: 258.23 E-value: 1.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 41 PSSRAELCTRVADqLRDRKFEFAATL-SLENGKTrIEAMA--DVDEAIDFLEFYSreiTAADGYRFDTGEPTPGQHTTNL 117
Cdd:cd07143 67 GSKRGRCLSKLAD-LMERNLDYLASIeALDNGKT-FGTAKrvDVQASADTFRYYG---GWADKIHGQVIETDIKKLTYTR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 118 LRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEH 197
Cdd:cd07143 142 HEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 198 EAVDGIAFTGSRAVGvgieRTFQELGKRG---PVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVY 274
Cdd:cd07143 222 MDIDKVAFTGSTLVG----RKVMEAAAKSnlkKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQ 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 275 ENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSVISDsdlpDGRYVEPTVVT 353
Cdd:cd07143 298 EGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGaTVETGGKRHGN----EGYFIEPTIFT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 354 EIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKQSATTGAlvqa 433
Cdd:cd07143 374 DVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQV---- 449
|
410
....*....|....*....
gi 2082837691 434 qPFGGWKFSGtTGKFAGGY 452
Cdd:cd07143 450 -PFGGYKQSG-IGRELGEY 466
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
36-444 |
1.73e-80 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 257.66 E-value: 1.73e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADqLRDRKFEFAATL-SLENGKT-RIEAMADVDEAIDFLEFYSreiTAADGYRFDTgEPTPGQH 113
Cdd:cd07141 63 WRTMDASERGRLLNKLAD-LIERDRAYLASLeTLDNGKPfSKSYLVDLPGAIKVLRYYA---GWADKIHGKT-IPMDGDF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 114 -TTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQ 192
Cdd:cd07141 138 fTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 193 PLVEHEAVDGIAFTGSRAVGvgieRTFQELG-----KRgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSA 267
Cdd:cd07141 218 AISSHPDIDKVAFTGSTEVG----KLIQQAAgksnlKR--VTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 268 TSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDGTVL-TGGSVISDSdlpdGRY 346
Cdd:cd07141 292 GSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLeCGGKRHGDK----GYF 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 347 VEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqsaT 426
Cdd:cd07141 368 IQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN-----C 442
|
410
....*....|....*...
gi 2082837691 427 TGALVQAQPFGGWKFSGT 444
Cdd:cd07141 443 YNVVSPQAPFGGYKMSGN 460
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
36-443 |
2.59e-79 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 254.81 E-value: 2.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEA-MADVDEAIDFLEFYSREITAADGYRFDTGEptpGQHT 114
Cdd:PRK13252 60 WAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETsVVDIVTGADVLEYYAGLAPALEGEQIPLRG---GSFV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 115 TNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTtGQPL 194
Cdd:PRK13252 137 YTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 195 VEHEAVDGIAFTGSraVGVGIERTFQELGKRGPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVY 274
Cdd:PRK13252 216 TEHPDIAKVSFTGG--VPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 275 ENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSVISDSDLPDGRYVEPTVVT 353
Cdd:PRK13252 294 KSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGaRLLCGGERLTEGGFANGAFVAPTVFT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 354 EIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqsaTTGALVQA 433
Cdd:PRK13252 374 DCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWIN-----TWGESPAE 448
|
410
....*....|
gi 2082837691 434 QPFGGWKFSG 443
Cdd:PRK13252 449 MPVGGYKQSG 458
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
44-465 |
4.70e-79 |
|
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: 253.67 E-value: 4.70e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 44 RAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEF---YSREItaaDGYRFdtgePT--PGQHTTNLL 118
Cdd:cd07130 58 RGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEVQEMIDICDFavgLSRQL---YGLTI----PSerPGHRMMEQW 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 119 RPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEA----GIPDGVLNLVTGDGpTTGQPL 194
Cdd:cd07130 131 NPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGA-DVGEAL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 195 VEHEAVDGIAFTGSRAVG--VGiertfQELGKR-GPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRV 271
Cdd:cd07130 210 VKDPRVPLVSFTGSTAVGrqVG-----QAVAARfGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 272 YVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSD-GTVLTGGSVISDsdlpDGRYVEPT 350
Cdd:cd07130 285 IVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQgGTVLFGGKVIDG----PGNYVEPT 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 351 VVtEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEI--EAGMCYVNrkqSATTG 428
Cdd:cd07130 361 IV-EGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVN---IGTSG 436
|
410 420 430
....*....|....*....|....*....|....*...
gi 2082837691 429 ALVQAqPFGGWKFSGtTGKFAGG-YWylQQFMREQSRT 465
Cdd:cd07130 437 AEIGG-AFGGEKETG-GGRESGSdAW--KQYMRRSTCT 470
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
50-462 |
1.11e-78 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 250.81 E-value: 1.11e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 50 RVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEF-------YSREITAADgyrfdtgepTPGQHTTNLLRPYG 122
Cdd:PRK10090 3 KIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYmaewarrYEGEIIQSD---------RPGENILLFKRALG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 123 VFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDG 202
Cdd:PRK10090 74 VTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 203 IAFTGSRAVGVGI-ERTFQELGKrgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSF 281
Cdd:PRK10090 154 VSMTGSVSAGEKImAAAAKNITK---VCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 282 TDRLVEETENLVVGQPTDRETF-VSPLIDDEAVDRYREISTQARSDG-TVLTGGSVISDsdlpDGRYVEPTVVTEIPHEH 359
Cdd:PRK10090 231 VNRLGEAMQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGaRVALGGKAVEG----KGYYYPPTLLLDVRQEM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 360 SLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKQsattgaLVQAQPF-GG 438
Cdd:PRK10090 307 SIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINREN------FEAMQGFhAG 380
|
410 420
....*....|....*....|....
gi 2082837691 439 WKFSGTTGkfAGGYWYLQQFMREQ 462
Cdd:PRK10090 381 WRKSGIGG--ADGKHGLHEYLQTQ 402
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
17-443 |
1.79e-78 |
|
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: 252.32 E-value: 1.79e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 17 GDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTrIEAMADVDEAIDFLEFYSREIT 96
Cdd:cd07111 56 AEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKP-IRESRDCDIPLVARHFYHHAGW 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 97 AAdgyRFDTGEPTPGqhttnllrPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIP 176
Cdd:cd07111 135 AQ---LLDTELAGWK--------PVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 177 DGVLNLVTGDGpTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEADLDAAVNGVMKG 256
Cdd:cd07111 204 PGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKK--LSLELGGKSPFIVFDDADLDSAVEGIVDA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 257 AFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDGTVLtggsVI 336
Cdd:cd07111 281 IWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADV----FQ 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 337 SDSDLP-DGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAG 415
Cdd:cd07111 357 PGADLPsKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAG 436
|
410 420
....*....|....*....|....*...
gi 2082837691 416 MCYVNrkqsaTTGALVQAQPFGGWKFSG 443
Cdd:cd07111 437 VVWIN-----GHNLFDAAAGFGGYRESG 459
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
7-442 |
8.69e-78 |
|
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: 250.51 E-value: 8.69e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAID 86
Cdd:cd07085 25 TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVLRGLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 87 FLEF-----------YSREITaadgyrfdtgeptPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKP 155
Cdd:cd07085 105 VVEFacsiphllkgeYLENVA-------------RGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 156 AEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTgQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGK 235
Cdd:cd07085 172 SERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR--VQALGGAK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 236 NPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDR 315
Cdd:cd07085 249 NHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKER 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 316 YREISTQARSDG-TVLTGGSVISDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLC 394
Cdd:cd07085 329 IEGLIESGVEEGaKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNG 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2082837691 395 AGLFSEDESEIEQWFDEIEAGMCYVNRKQSATTGALvqaqPFGGWKFS 442
Cdd:cd07085 409 AAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFF----SFGGWKGS 452
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
36-443 |
1.93e-77 |
|
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: 249.57 E-value: 1.93e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAM-ADVDEAIDFLEFYSREITAADGYRFDTGEPTPGQHt 114
Cdd:cd07559 54 WGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLaADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYH- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 115 tnLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAgIPDGVLNLVTGDGPTTGQPL 194
Cdd:cd07559 133 --FHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 195 VEHEAVDGIAFTGSRAVGVGIERTFQElgKRGPVIAELGGKNPVIVSDEAD------LDAAVNGVMKGAFSfAGQKCSAT 268
Cdd:cd07559 210 ASHPRIAKLAFTGSTTVGRLIMQYAAE--NLIPVTLELGGKSPNIFFDDAMdadddfDDKAEEGQLGFAFN-QGEVCTCP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 269 SRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDR---YREISTQarSDGTVLTGGSVISDSDLPDGR 345
Cdd:cd07559 287 SRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKilsYVDIGKE--EGAEVLTGGERLTLGGLDKGY 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 346 YVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKQSA 425
Cdd:cd07559 365 FYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQY 444
|
410
....*....|....*...
gi 2082837691 426 TTGAlvqaqPFGGWKFSG 443
Cdd:cd07559 445 PAHA-----PFGGYKKSG 457
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
11-443 |
2.92e-77 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 249.74 E-value: 2.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 11 IGTFAVGDSSEVDDAVAAATAA--QPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKT-RIEAMADVDEAIDF 87
Cdd:PLN02766 49 IARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLfALGKAVDIPAAAGL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 88 LEFYSreiTAADGYRFDTGEPTPGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVM 167
Cdd:PLN02766 129 LRYYA---GAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 168 DLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGvgieRTFQELGKRG---PVIAELGGKNPVIVSDEA 244
Cdd:PLN02766 206 HLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVG----RKIMQAAATSnlkQVSLELGGKSPLLIFDDA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 245 DLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQAR 324
Cdd:PLN02766 282 DVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGK 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 325 SDG-TVLTGGSVISDSdlpdGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDES 403
Cdd:PLN02766 362 REGaTLLTGGKPCGDK----GYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLD 437
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2082837691 404 EIEQWFDEIEAGMCYVNrkqsaTTGALVQAQPFGGWKFSG 443
Cdd:PLN02766 438 VANTVSRSIRAGTIWVN-----CYFAFDPDCPFGGYKMSG 472
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
7-448 |
7.98e-77 |
|
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: 247.74 E-value: 7.98e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAA-QPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKT-RIEAMADVDEA 84
Cdd:cd07113 24 TEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSiHLSRAFEVGQS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 85 IDFLEFYSREITAADGYRFDTGEPTPG--QHTTNLLR-PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPL 161
Cdd:cd07113 104 ANFLRYFAGWATKINGETLAPSIPSMQgeRYTAFTRRePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 162 VAHKVMDLFEEAGIPDGVLNLVTGDGpTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVS 241
Cdd:cd07113 184 TLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTR--VTLELGGKNAAAFL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 242 DEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREIST 321
Cdd:cd07113 261 KDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 322 QARSDG-TVLTGGSVISDsdlpDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSE 400
Cdd:cd07113 341 DARAEGdEIVRGGEALAG----EGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTN 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2082837691 401 DESEIEQWFDEIEAGMCYVNRKQsattgALVQAQPFGGWKFSGTTGKF 448
Cdd:cd07113 417 NLSKALRYIPRIEAGTVWVNMHT-----FLDPAVPFGGMKQSGIGREF 459
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
13-443 |
4.82e-73 |
|
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: 238.12 E-value: 4.82e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 13 TFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGK-TRIEAMADVDEAIDFLEFY 91
Cdd:cd07117 31 EITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKpIRETRAVDIPLAADHFRYF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 92 SREITAADGYRFDTGEptpgqHTTNLLR--PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDL 169
Cdd:cd07117 111 AGVIRAEEGSANMIDE-----DTLSIVLrePIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 170 FEEAgIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQElgKRGPVIAELGGKNPVIVSDEADLDAA 249
Cdd:cd07117 186 IQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK--KLIPATLELGGKSANIIFDDANWDKA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 250 VNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDR---YREISTQarSD 326
Cdd:cd07117 263 LEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKilsYVDIAKE--EG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 327 GTVLTGGSVISDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIE 406
Cdd:cd07117 341 AKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRAL 420
|
410 420 430
....*....|....*....|....*....|....*..
gi 2082837691 407 QWFDEIEAGMCYVNRKQSATTGAlvqaqPFGGWKFSG 443
Cdd:cd07117 421 RVARAVETGRVWVNTYNQIPAGA-----PFGGYKKSG 452
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
4-456 |
9.84e-70 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 241.03 E-value: 9.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 4 PGDTTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDE 83
Cdd:PRK11809 666 PADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVRE 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 84 AIDFLEFYSREItaADGYRFDTgeptpgqHttnllRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVA 163
Cdd:PRK11809 746 AVDFLRYYAGQV--RDDFDNDT-------H-----RPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIA 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 164 HKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTF-QELGKRG---PVIAELGGKNPVI 239
Cdd:PRK11809 812 AQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLaGRLDPQGrpiPLIAETGGQNAMI 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 240 VSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEA---VDRY 316
Cdd:PRK11809 892 VDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAkanIERH 971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 317 REistQARSDGTVLTGGSVISDSDLPDGRYVEPTVVtEIPHEHSLAREE-----HFVPFvtihPVSGLDAGIEKSNDSEF 391
Cdd:PRK11809 972 IQ---AMRAKGRPVFQAARENSEDWQSGTFVPPTLI-ELDSFDELKREVfgpvlHVVRY----NRNQLDELIEQINASGY 1043
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2082837691 392 GLCAGLFSEDESEIEQWFDEIEAGMCYVNRKqsaTTGALVQAQPFGGWKFSGTTGKfAGGYWYLQ 456
Cdd:PRK11809 1044 GLTLGVHTRIDETIAQVTGSAHVGNLYVNRN---MVGAVVGVQPFGGEGLSGTGPK-AGGPLYLY 1104
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
36-443 |
1.00e-69 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 229.69 E-value: 1.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAM-ADVDEAIDFLEFYSREITAADGYRFDTGEPTPGQHT 114
Cdd:cd07140 61 WGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNRNL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 115 TNLLR-PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQP 193
Cdd:cd07140 141 TLTKRePIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 194 LVEHEAVDGIAFTGSRAVGVGIERTFQE--LGKrgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRV 271
Cdd:cd07140 221 LSDHPDVRKLGFTGSTPIGKHIMKSCAVsnLKK---VSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 272 YVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSVIsdsDLPdGRYVEPT 350
Cdd:cd07140 298 FVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGaTLVYGGKQV---DRP-GFFFEPT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 351 VVTEIPHEHSLAREEHFVPFVTIHPVSG--LDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKQSATTg 428
Cdd:cd07140 374 VFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDV- 452
|
410
....*....|....*
gi 2082837691 429 alvqAQPFGGWKFSG 443
Cdd:cd07140 453 ----AAPFGGFKQSG 463
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
36-456 |
5.08e-69 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 229.31 E-value: 5.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAM-ADVDEAIDFLEFYSreiTAADGYRFDTGePTPGQHT 114
Cdd:PLN02466 113 WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAkAELPMFARLFRYYA---GWADKIHGLTV-PADGPHH 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 115 TNLL-RPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQP 193
Cdd:PLN02466 189 VQTLhEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 194 LVEHEAVDGIAFTGSRAVGvgieRTFQELGKRG---PVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSR 270
Cdd:PLN02466 269 LASHMDVDKLAFTGSTDTG----KIVLELAAKSnlkPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSR 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 271 VYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDR-YREISTQARSDGTVLTGGSVISDSdlpdGRYVEP 349
Cdd:PLN02466 345 TFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKiLRYIKSGVESGATLECGGDRFGSK----GYYIQP 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 350 TVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqsaTTGA 429
Cdd:PLN02466 421 TVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVN-----CFDV 495
|
410 420 430
....*....|....*....|....*....|
gi 2082837691 430 LVQAQPFGGWKFSGtTGKFAGGYW---YLQ 456
Cdd:PLN02466 496 FDAAIPFGGYKMSG-IGREKGIYSlnnYLQ 524
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
36-443 |
7.00e-67 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 222.09 E-value: 7.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFYSREitaadGYRFdTGEPTPGQHTT 115
Cdd:PRK11241 64 WRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEE-----GKRI-YGDTIPGHQAD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 116 NLL----RPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTG 191
Cdd:PRK11241 138 KRLivikQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 192 QPLVEHEAVDGIAFTGSRAVGVGI-ERTFQELGKrgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSR 270
Cdd:PRK11241 218 GELTSNPLVRKLSFTGSTEIGRQLmEQCAKDIKK---VSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANR 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 271 VYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSvisdSDLPDGRYVEP 349
Cdd:PRK11241 295 LYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGaRVVCGGK----AHELGGNFFQP 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 350 TVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqsatTGA 429
Cdd:PRK11241 371 TILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGIN------TGI 444
|
410
....*....|....*
gi 2082837691 430 LV-QAQPFGGWKFSG 443
Cdd:PRK11241 445 ISnEVAPFGGIKASG 459
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
7-450 |
9.73e-65 |
|
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: 216.01 E-value: 9.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADvdeaid 86
Cdd:cd07098 5 TGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLG------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 87 flefysrEI-TAADGYRF--DTGEPT--PGQHTTNLL----------RPYGVFGVISPFNFPLAILVGMTTGALITGNTV 151
Cdd:cd07098 79 -------EIlVTCEKIRWtlKHGEKAlrPESRPGGLLmfykrarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 152 VLKPAE----ATPLVAHKVMDLFEEAGIPDGVLNLVTGdGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQElgKRGP 227
Cdd:cd07098 152 VVKVSEqvawSSGFFLSIIRECLAACGHDPDLVQLVTC-LPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAE--SLTP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 228 VIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPL 307
Cdd:cd07098 229 VVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 308 IDDEAVDRYREISTQARSDG-TVLTGGSVISDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKS 386
Cdd:cd07098 309 ISPARFDRLEELVADAVEKGaRLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2082837691 387 NDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKQSATtgaLVQAQPFGGWKFSGtTGKFAG 450
Cdd:cd07098 389 NSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNY---YVQQLPFGGVKGSG-FGRFAG 448
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
36-443 |
5.47e-60 |
|
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: 203.84 E-value: 5.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAM-ADVDEAIDFLEFYSREITAADGYRFDTGEPTPGQHt 114
Cdd:cd07116 54 WGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLaADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYH- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 115 tnLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAgIPDGVLNLVTGDGPTTGQPL 194
Cdd:cd07116 133 --FHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 195 VEHEAVDGIAFTGSRAVGVGIERTFQElgKRGPVIAELGGKNP------VIVSDEADLDAAVNGVMKGAFSfAGQKCSAT 268
Cdd:cd07116 210 ASSKRIAKVAFTGETTTGRLIMQYASE--NIIPVTLELGGKSPniffadVMDADDAFFDKALEGFVMFALN-QGEVCTCP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 269 SRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDR---YREIstqARSDG-TVLTGGSVISDSDLPDG 344
Cdd:cd07116 287 SRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKilsYIDI---GKEEGaEVLTGGERNELGGLLGG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 345 RYVEPTVVTEiPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKQS 424
Cdd:cd07116 364 GYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHL 442
|
410
....*....|....*....
gi 2082837691 425 ATTGAlvqaqPFGGWKFSG 443
Cdd:cd07116 443 YPAHA-----AFGGYKQSG 456
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
36-443 |
7.30e-58 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 198.58 E-value: 7.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGK-TRIEAMADVDEAIDFLEFYSREITAADGyrfdTGEPTPGQHT 114
Cdd:PRK09847 75 WSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKpIRHSLRDDIPGAARAIRWYAEAIDKVYG----EVATTSSHEL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 115 TNLLR-PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQP 193
Cdd:PRK09847 151 AMIVRePVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 194 LVEHEAVDGIAFTGSRAVGvgiERTFQELG----KRgpVIAELGGKNPVIV-SDEADLDAAVNGVMKGAFSFAGQKCSAT 268
Cdd:PRK09847 231 LSRHNDIDAIAFTGSTRTG---KQLLKDAGdsnmKR--VWLEAGGKSANIVfADCPDLQQAASATAAGIFYNQGQVCIAG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 269 SRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDGTVLTGGsviSDSDLPdgRYVE 348
Cdd:PRK09847 306 TRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDG---RNAGLA--AAIG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 349 PTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKQSATTG 428
Cdd:PRK09847 381 PTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT 460
|
410
....*....|....*
gi 2082837691 429 AlvqaqPFGGWKFSG 443
Cdd:PRK09847 461 V-----PFGGYKQSG 470
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
7-443 |
9.04e-58 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 197.27 E-value: 9.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAID 86
Cdd:PRK09406 10 TGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 87 FLEFYsreitAADGYRFDTGEPTPGQH---TTNLLR--PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPL 161
Cdd:PRK09406 90 GFRYY-----AEHAEALLADEPADAAAvgaSRAYVRyqPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 162 VAHKVMDLFEEAGIPDGVLNLVtgdgpttgqpLVEHEAVDGI---------AFTGSRAVGVGIERTFQELGKrgPVIAEL 232
Cdd:PRK09406 165 TALYLADLFRRAGFPDGCFQTL----------LVGSGAVEAIlrdprvaaaTLTGSEPAGRAVAAIAGDEIK--KTVLEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 233 GGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEA 312
Cdd:PRK09406 233 GGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 313 VDRYREISTQARSDG-TVLTGGsvisdsDLPDGR--YVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDS 389
Cdd:PRK09406 313 RDEVEKQVDDAVAAGaTILCGG------KRPDGPgwFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANAT 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2082837691 390 EFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrKQSATTGALvqaqPFGGWKFSG 443
Cdd:PRK09406 387 TFGLGSNAWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPEL----PFGGVKRSG 435
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
41-443 |
2.87e-57 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 196.10 E-value: 2.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 41 PSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFYSREITAADGYRFDTG--EPTPGQHTTNLL 118
Cdd:cd07148 43 AHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREIPMGltPASAGRIAFTTR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 119 RPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTtGQPLVEHE 198
Cdd:cd07148 123 EPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAV-AEKLVTDP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 199 AVDGIAFTGSRAVGVGIeRTFQELGKRgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIV 278
Cdd:cd07148 202 RVAFFSFIGSARVGWML-RSKLAPGTR--CALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 279 DSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDG-TVLTGGSVISDSDLpdgryvEPTVVTEIPH 357
Cdd:cd07148 279 DDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGaRLLCGGKRLSDTTY------APTVLLDPPR 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 358 EHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKqsatTGALVQAQPFG 437
Cdd:cd07148 353 DAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDH----TAFRVDWMPFA 428
|
....*.
gi 2082837691 438 GWKFSG 443
Cdd:cd07148 429 GRRQSG 434
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
7-443 |
2.67e-53 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 185.45 E-value: 2.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 7 TTRQIGTFAVGDSSEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAID 86
Cdd:PRK13968 16 TGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSAN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 87 FLEFYsreitAADGYRFDTGEPT--PGQHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAH 164
Cdd:PRK13968 96 LCDWY-----AEHGPAMLKAEPTlvENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 165 KVMDLFEEAGIPDGVLNLVTGDGPTTGQpLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEA 244
Cdd:PRK13968 171 LIAQVFKDAGIPQGVYGWLNADNDGVSQ-MINDSRIAAVTVTGSVRAGAAIGAQAGAALKK--CVLELGGSDPFIVLNDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 245 DLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQAR 324
Cdd:PRK13968 248 DLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 325 SDG-TVLTGGSVISDSdlpdGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDES 403
Cdd:PRK13968 328 AEGaRLLLGGEKIAGA----GNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDET 403
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2082837691 404 EIEQWFDEIEAGMCYVNrKQSATTGALVqaqpFGGWKFSG 443
Cdd:PRK13968 404 QARQMAARLECGGVFIN-GYCASDARVA----FGGVKKSG 438
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
36-465 |
2.79e-53 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 186.58 E-value: 2.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEF---YSREITaadgyrfdtGEPTPGQ 112
Cdd:PLN02315 72 WMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFavgLSRQLN---------GSIIPSE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 113 HTTNLL----RPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVA----HKVMDLFEEAGIPDGVLNLVT 184
Cdd:PLN02315 143 RPNHMMmevwNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITiamtKLVAEVLEKNNLPGAIFTSFC 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 185 GdGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTFQElgKRGPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQK 264
Cdd:PLN02315 223 G-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNA--RFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 265 CSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYRE-ISTQARSDGTVLTGGSVISdsdlPD 343
Cdd:PLN02315 300 CTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKgIEIIKSQGGKILTGGSAIE----SE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 344 GRYVEPTVVtEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEI--EAGMCYVNr 421
Cdd:PLN02315 376 GNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLgsDCGIVNVN- 453
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2082837691 422 kqSATTGALVqAQPFGGWKFSGtTGKFAGG-YWylQQFMREQSRT 465
Cdd:PLN02315 454 --IPTNGAEI-GGAFGGEKATG-GGREAGSdSW--KQYMRRSTCT 492
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
120-438 |
1.50e-50 |
|
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: 177.33 E-value: 1.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 120 PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAgIPDGVLNLVTGDGPTTGQPLVEHea 199
Cdd:cd07087 100 PLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVATALLAEP-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 200 VDGIAFTGSRAVGVGIER------TfqelgkrgPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYV 273
Cdd:cd07087 177 FDHIFFTGSPAVGKIVMEaaakhlT--------PVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 274 YENIVDSFTDRLVEETENLVVGQPTDRETFvSPLIDDEAVDRYREISTqarsDGTVLTGGSVIsdsdlPDGRYVEPTVVT 353
Cdd:cd07087 249 HESIKDELIEELKKAIKEFYGEDPKESPDY-GRIINERHFDRLASLLD----DGKVVIGGQVD-----KEERYIAPTILD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 354 EIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqSATTGALVQA 433
Cdd:cd07087 319 DVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVN---DVLLHAAIPN 395
|
....*
gi 2082837691 434 QPFGG 438
Cdd:cd07087 396 LPFGG 400
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
20-420 |
8.97e-49 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 174.17 E-value: 8.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 20 SEVDDAVAAATAAQPAWEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFysreiTAAD 99
Cdd:PLN00412 53 EEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISY-----TAEE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 100 GYR------FDTGEPTPGQHTTNLLR----PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDL 169
Cdd:PLN00412 128 GVRilgegkFLVSDSFPGNERNKYCLtskiPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHC 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 170 FEEAGIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAvGVGIERtfqelgKRG--PVIAELGGKNPVIVSDEADLD 247
Cdd:PLN00412 208 FHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGDT-GIAISK------KAGmvPLQMELGGKDACIVLEDADLD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 248 AAVNGVMKGAFSFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDrETFVSPLIDDEAVDRYREISTQARSDG 327
Cdd:PLN00412 281 LAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 328 TVLTggsvisDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQ 407
Cdd:PLN00412 360 ATFC------QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAIL 433
|
410
....*....|...
gi 2082837691 408 WFDEIEAGMCYVN 420
Cdd:PLN00412 434 ISDAMETGTVQIN 446
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
119-448 |
3.43e-48 |
|
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: 171.25 E-value: 3.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 119 RPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAgIPDGVLNLVTGDGPTTGQpLVEHE 198
Cdd:cd07135 107 EPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTA-LLEQK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 199 aVDGIAFTGSRAVGVGI-ERTFQELGkrgPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENI 277
Cdd:cd07135 185 -FDKIFYTGSGRVGRIIaEAAAKHLT---PVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 278 VDSFTDRLVEETENLVVGQPTDRETFvSPLIDDEAVDRYReiSTQARSDGTVLTGGSVISDSdlpdgRYVEPTVVTEIPH 357
Cdd:cd07135 261 YDEFVEELKKVLDEFYPGGANASPDY-TRIVNPRHFNRLK--SLLDTTKGKVVIGGEMDEAT-----RFIPPTIVSDVSW 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 358 EHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkQSATTGALVQAqPFG 437
Cdd:cd07135 333 DDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVIN--DTLIHVGVDNA-PFG 409
|
330
....*....|....
gi 2082837691 438 GWKFSGT---TGKF 448
Cdd:cd07135 410 GVGDSGYgayHGKY 423
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
120-463 |
4.65e-46 |
|
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: 165.48 E-value: 4.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 120 PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVlNLVTGDgPTTGQPLVEhEA 199
Cdd:cd07134 100 PKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-AVFEGD-AEVAQALLE-LP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 200 VDGIAFTGSRAVG-VGIERTFQELGkrgPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIV 278
Cdd:cd07134 177 FDHIFFTGSPAVGkIVMAAAAKHLA---SVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 279 DSFTDRLVEETENLVVGQPTDREtfvSP----LIDDEAVDRYREISTQARSDG-TVLTGGsvisDSDlPDGRYVEPTVVT 353
Cdd:cd07134 254 DAFVEHLKAEIEKFYGKDAARKA---SPdlarIVNDRHFDRLKGLLDDAVAKGaKVEFGG----QFD-AAQRYIAPTVLT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 354 EIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqsattGALVQA 433
Cdd:cd07134 326 NVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN-------DVVLHF 398
|
330 340 350
....*....|....*....|....*....|....
gi 2082837691 434 Q----PFGGWKFSGtTGKfAGGYWYLQQFMREQS 463
Cdd:cd07134 399 LnpnlPFGGVNNSG-IGS-YHGVYGFKAFSHERA 430
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
36-450 |
1.02e-42 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 159.53 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMADVDEAIDFLEFysreitAADGYRFDTGEPTP----G 111
Cdd:PLN02419 167 WRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEH------ACGMATLQMGEYLPnvsnG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 112 QHTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTg 191
Cdd:PLN02419 241 VDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 192 QPLVEHEAVDGIAFTGSRAVGVGIERTFQELGKRgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRV 271
Cdd:PLN02419 320 NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKR--IQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTV 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 272 yVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDGT-VLTGGSVISDSDLPDGRYVEPT 350
Cdd:PLN02419 398 -VFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAkLLLDGRDIVVPGYEKGNFIGPT 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 351 VVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRKQSAttgal 430
Cdd:PLN02419 477 ILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPV----- 551
|
410 420
....*....|....*....|
gi 2082837691 431 vqaqPFGGWKFSGTTGKFAG 450
Cdd:PLN02419 552 ----PLPFFSFTGNKASFAG 567
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
36-438 |
2.53e-41 |
|
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: 152.78 E-value: 2.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAmADVDEAIDFLEFYSREItAADGYRFDTGE---PTPGQ 112
Cdd:cd07084 15 ARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAFVI-YSYRIPHEPGNhlgQGLKQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 113 HTTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGI-PDGVLNLVTGDGpTTG 191
Cdd:cd07084 93 QSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLINGDG-KTM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 192 QPLVEHEAVDGIAFTGSRAVGvgieRTFQELGKRGPVIAELGGKNPVIVSDEAD-LDAAVNGVMKGAFSFAGQKCSATSR 270
Cdd:cd07084 172 QALLLHPNPKMVLFTGSSRVA----EKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 271 VYVYENivDSfTDRLVEETENLvVGQPTDRETFVSPLIDDEAVDRyreISTQARSDGTVLTGGSVISDSDLPDGRY--VE 348
Cdd:cd07084 248 LFVPEN--WS-KTPLVEKLKAL-LARRKLEDLLLGPVQTFTTLAM---IAHMENLLGSVLLFSGKELKNHSIPSIYgaCV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 349 PT----VVTEIPHEHSLAREEHFVPF--VTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIE-AGMCYVNR 421
Cdd:cd07084 321 ASalfvPIDEILKTYELVTEEIFGPFaiVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWvAGRTYAIL 400
|
410
....*....|....*..
gi 2082837691 422 KQSaTTGALVQAQPFGG 438
Cdd:cd07084 401 RGR-TGVAPNQNHGGGP 416
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
120-415 |
1.02e-39 |
|
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: 148.42 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 120 PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAgIPDGVLNLVTGDGPTTGQPLveHEA 199
Cdd:cd07136 100 PYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELL--DQK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 200 VDGIAFTGSRAVG-VGIERTFQELGkrgPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIV 278
Cdd:cd07136 177 FDYIFFTGSVRVGkIVMEAAAKHLT---PVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 279 DSFTDRLVEETENLVVGQPTDRETFVSpLIDDEAVDRYREIStqarSDGTVLTGGsvisDSDlPDGRYVEPTVVTEIPHE 358
Cdd:cd07136 254 EKFIKELKEEIKKFYGEDPLESPDYGR-IINEKHFDRLAGLL----DNGKIVFGG----NTD-RETLYIEPTILDNVTWD 323
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 359 HSLAREEHFVPfvtIHPV---SGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAG 415
Cdd:cd07136 324 DPVMQEEIFGP---ILPVltyDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFG 380
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
120-443 |
1.65e-38 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 145.94 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 120 PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAgIPDGVLNLVTGDGPTTGQPLVEHea 199
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTELLKEP-- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 200 VDGIAFTGSRAVGVGIERTFQElgKRGPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENIVD 279
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQAAAE--NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKD 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 280 SFTDRLVEETENLvVGQPTDRETFVSPLIDDEAVDRYREISTQarSDGTVLTGGSV-ISDsdlpdgRYVEPTVVTEIPHE 358
Cdd:PTZ00381 264 KFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKD--HGGKVVYGGEVdIEN------KYVAPTIIVNPDLD 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 359 HSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqSATTGALVQAQPFGG 438
Cdd:PTZ00381 335 SPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN---DCVFHLLNPNLPFGG 411
|
....*
gi 2082837691 439 WKFSG 443
Cdd:PTZ00381 412 VGNSG 416
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
120-438 |
6.79e-37 |
|
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: 140.31 E-value: 6.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 120 PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDgVLNLVTGDGPT----TGQPLv 195
Cdd:cd07133 101 PLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTGGADVaaafSSLPF- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 196 eheavDGIAFTGSRAVGVGIER------TfqelgkrgPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATS 269
Cdd:cd07133 179 -----DHLLFTGSTAVGRHVMRaaaenlT--------PVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 270 RVYVYENIVDSFTDRLVEETENLvVGQPTDRETFVSpLIDDEAVDRYREISTQARSdgtvlTGGSVIS----DSDLPDGR 345
Cdd:cd07133 246 YVLVPEDKLEEFVAAAKAAVAKM-YPTLADNPDYTS-IINERHYARLQGLLEDARA-----KGARVIElnpaGEDFAATR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 346 YVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAG-MCyVNrkqs 424
Cdd:cd07133 319 KLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGgVT-IN---- 393
|
330
....*....|....*...
gi 2082837691 425 attGALVQA----QPFGG 438
Cdd:cd07133 394 ---DTLLHVaqddLPFGG 408
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
38-407 |
4.05e-36 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 139.71 E-value: 4.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 38 AMDPSSRAELCTRVADQLRDRKFEFAAtLSLENGKTRIEAMADVDEAIDFLEFYS----REITAADGYRFDTGEPTP--- 110
Cdd:cd07128 55 ALTFHERAAMLKALAKYLMERKEDLYA-LSAATGATRRDSWIDIDGGIGTLFAYAslgrRELPNAHFLVEGDVEPLSkdg 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 111 ---GQHttnLLRP-YGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGI-PDGVLNLVTG 185
Cdd:cd07128 134 tfvGQH---ILTPrRGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 186 DgptTGqPLVEH-EAVDGIAFTGSRAVGVGIeRTFQELGKRG-PVIAELGGKNPVIVS-----DEADLDAAVNGVMKGAF 258
Cdd:cd07128 211 S---VG-DLLDHlGEQDVVAFTGSAATAAKL-RAHPNIVARSiRFNAEADSLNAAILGpdatpGTPEFDLFVKEVAREMT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 259 SFAGQKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDGTVLTGG---SV 335
Cdd:cd07128 286 VKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGpdrFE 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2082837691 336 ISDSDLPDGRYVEPTV-VTEIPHEHSLARE-EHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQ 407
Cdd:cd07128 366 VVGADAEKGAFFPPTLlLCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARE 439
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
120-449 |
3.51e-33 |
|
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: 130.22 E-value: 3.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 120 PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAgIPDGVLNLVTGdGPTTGQPLVEHEA 199
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLEQKW 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 200 vDGIAFTGSRAVG-VGIERTFQELgkrGPVIAELGGKNPVIVSDEADLDAAVNGVMKGAF-SFAGQKCSATSRVYVYENI 277
Cdd:cd07137 179 -DKIFFTGSPRVGrIIMAAAAKHL---TPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESF 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 278 VDSFTDRLVEETENLvVGQPTDRETFVSPLIDDEAVDRYREISTQARSDGTVLTGGSVISDSdlpdgRYVEPTVVTEIPH 357
Cdd:cd07137 255 APTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKN-----LYIEPTILLDPPL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 358 EHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqSATTGALVQAQPFG 437
Cdd:cd07137 329 DSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFN---DTVVQYAIDTLPFG 405
|
330
....*....|....*
gi 2082837691 438 GWKFSGTT---GKFA 449
Cdd:cd07137 406 GVGESGFGayhGKFS 420
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
120-452 |
9.08e-33 |
|
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: 129.26 E-value: 9.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 120 PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLfeeagIPDGVLN----LVTGDGPTTGQpLV 195
Cdd:cd07132 100 PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLDKecypVVLGGVEETTE-LL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 196 EHEaVDGIAFTGSRAVGVGIER------TfqelgkrgPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATS 269
Cdd:cd07132 174 KQR-FDYIFYTGSTSVGKIVMQaaakhlT--------PVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 270 RVYVYENIVDSFTDRLVEETENLVVGQPTDRETFvSPLIDDEAVDRYREIstqaRSDGTVLTGGSViSDSDlpdgRYVEP 349
Cdd:cd07132 245 YVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDY-GRIINDRHFQRLKKL----LSGGKVAIGGQT-DEKE----RYIAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 350 TVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNRK--QSATT 427
Cdd:cd07132 315 TVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTimHYTLD 394
|
330 340
....*....|....*....|....*
gi 2082837691 428 GAlvqaqPFGGWKFSGtTGKFAGGY 452
Cdd:cd07132 395 SL-----PFGGVGNSG-MGAYHGKY 413
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
46-429 |
7.52e-26 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 109.89 E-value: 7.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 46 ELCTRVADQLRDRKFE--FAATLSLENGKTRIEAMADVDEAIDFLEFYSreitaADGYRFDT-GEPTPGQH---TTNLLR 119
Cdd:cd07126 66 DVSHRVAHELRKPEVEdfFARLIQRVAPKSDAQALGEVVVTRKFLENFA-----GDQVRFLArSFNVPGDHqgqQSSGYR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 120 -PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPTTGQPLVEHE 198
Cdd:cd07126 141 wPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEAN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 199 AvDGIAFTGSRAVGvgiERTFQELgkRGPVIAELGGKNPVIVS-DEADLDAAVNGVMKGAFSFAGQKCSATSRVYVYENI 277
Cdd:cd07126 221 P-RMTLFTGSSKVA---ERLALEL--HGKVKLEDAGFDWKILGpDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENW 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 278 VDS-FTDRLVE-----ETENLVVGqPTdrETFVSPLIDDEaVDRYREISTqARsdgtVLTGGSVISDSDLPD--GRYvEP 349
Cdd:cd07126 295 VQAgILDKLKAlaeqrKLEDLTIG-PV--LTWTTERILDH-VDKLLAIPG-AK----VLFGGKPLTNHSIPSiyGAY-EP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 350 TVV------TEIPHEHSLAREEHFVPF--VTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNR 421
Cdd:cd07126 365 TAVfvpleeIAIEENFELVTTEVFGPFqvVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTYAGI 444
|
....*...
gi 2082837691 422 KqSATTGA 429
Cdd:cd07126 445 R-ARTTGA 451
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
120-452 |
1.35e-24 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 105.96 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 120 PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHkvmdlFEEAGIP---DGVLNLVTGDGPTTGQPLVE 196
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA-----FLAANIPkylDSKAVKVIEGGPAVGEQLLQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 197 HEAvDGIAFTGSRAVG-VGIERTFQELgkrGPVIAELGGKNPVIV---SDEADLDAAVNGVMKGAFSF-AGQKCSATSRV 271
Cdd:PLN02203 183 HKW-DKIFFTGSPRVGrIIMTAAAKHL---TPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQACIAIDYV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 272 YVYENIVDSFTDRLVEETENLVVGQPTDRETfVSPLIDDEAVDRYREISTQARSDGTVLTGGSVisDsdlPDGRYVEPTV 351
Cdd:PLN02203 259 LVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLKDPRVAASIVHGGSI--D---EKKLFIEPTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 352 VTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqsattGALV 431
Cdd:PLN02203 333 LLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFN-------DAII 405
|
330 340
....*....|....*....|....*
gi 2082837691 432 Q----AQPFGGWKFSGtTGKFAGGY 452
Cdd:PLN02203 406 QyacdSLPFGGVGESG-FGRYHGKY 429
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
36-370 |
2.27e-23 |
|
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: 102.23 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENG--KTRIE-----------AMADVDEAIDFLEfysREITAADgyr 102
Cdd:cd07129 15 YRALSPARRAAFLEAIADEIEALGDELVARAHAETGlpEARLQgelgrttgqlrLFADLVREGSWLD---ARIDPAD--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 103 fDTGEPTPGQHTTNLLRPYGVFGVISPFNFPLAILV--GMTTGALITGNTVVLKPAEATP----LVAHKVMDLFEEAGIP 176
Cdd:cd07129 89 -PDRQPLPRPDLRRMLVPLGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKAHPAHPgtseLVARAIRAALRATGLP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 177 DGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGvgieRTFQELG-KRG---PVIAELGGKNPVIVSDEAdLDAAVNG 252
Cdd:cd07129 168 AGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGG----RALFDAAaARPepiPFYAELGSVNPVFILPGA-LAERGEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 253 VMKG-AFSF---AGQKCSATSRVYVyenIVDSFTDRLVEETENLVVGQPTdretfvSPLIDDEAVDRYREISTQARSDGT 328
Cdd:cd07129 243 IAQGfVGSLtlgAGQFCTNPGLVLV---PAGPAGDAFIAALAEALAAAPA------QTMLTPGIAEAYRQGVEALAAAPG 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2082837691 329 VLTggsVISDSDLPDGRYVEPTVVT---EIPHEHSLAREEHFVPF 370
Cdd:cd07129 314 VRV---LAGGAAAEGGNQAAPTLFKvdaAAFLADPALQEEVFGPA 355
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
44-402 |
3.24e-23 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 102.48 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 44 RAELCTRVADQL---RDRKFEFAatlsLEN-GKTRIEAMADVDEAIDFLEFYSREITAADGYRFDT-GEPTP-------- 110
Cdd:PRK11903 65 RAALLAAIVKVLqanRDAYYDIA----TANsGTTRNDSAVDIDGGIFTLGYYAKLGAALGDARLLRdGEAVQlgkdpafq 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 111 GQHTTNLLRPYGVFgvISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGI-PDGVLNLVTGdgpt 189
Cdd:PRK11903 141 GQHVLVPTRGVALF--INAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCG---- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 190 TGQPLVEH-EAVDGIAFTGSRAVGVGIeRTFQELGKRGP-VIAELGGKN-----PVIVSDEADLDAAVNGVMKGAFSFAG 262
Cdd:PRK11903 215 SSAGLLDHlQPFDVVSFTGSAETAAVL-RSHPAVVQRSVrVNVEADSLNsallgPDAAPGSEAFDLFVKEVVREMTVKSG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 263 QKCSATSRVYVYENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVDRYREISTQARSDGTVLTGGSVISDSDLP 342
Cdd:PRK11903 294 QKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGFALVDAD 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2082837691 343 DGR--YVEPTV-VTEIPHEHSLARE-EHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDE 402
Cdd:PRK11903 374 PAVaaCVGPTLlGASDPDAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDA 437
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
120-449 |
5.17e-21 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 95.50 E-value: 5.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 120 PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEAGIPDGVLNLvtgDGPTTGQPLVEHEA 199
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVV---EGAVTETTALLEQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 200 VDGIAFTGSRAVGVGIertFQELGKR-GPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSF-AGQKCSATSRVYVYENI 277
Cdd:PLN02174 189 WDKIFYTGSSKIGRVI---MAAAAKHlTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYILTTKEY 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 278 VDSFTDRLVEETENLVVGQPTDRETfVSPLIDDEAVDRYREISTQARSDGTVLTGGsvisDSDLPDGRyVEPTVVTEIPH 357
Cdd:PLN02174 266 APKVIDAMKKELETFYGKNPMESKD-MSRIVNSTHFDRLSKLLDEKEVSDKIVYGG----EKDRENLK-IAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 358 EHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLCAGLFSEDESEIEQWFDEIEAGMCYVNrkqSATTGALVQAQPFG 437
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVN---DIAVHLALHTLPFG 416
|
330
....*....|....*
gi 2082837691 438 GWKFSGTT---GKFA 449
Cdd:PLN02174 417 GVGESGMGayhGKFS 431
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
36-410 |
8.13e-17 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 82.91 E-value: 8.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 36 WEAMDPSSRAELCTRVADQLRDRKFEFAATLSLENGKTRIEAMAD-----VDEAIDFLEFYSRE---ITAADGYRFDTGE 107
Cdd:cd07127 100 WRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFQAggphaQDRGLEAVAYAWREmsrIPPTAEWEKPQGK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 108 PTPGQHT-TNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPL-------VAHKVMdlfEEAGI-PDG 178
Cdd:cd07127 180 HDPLAMEkTFTVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILplaitvqVAREVL---AEAGFdPNL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 179 VLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVGVGIERTfqelGKRGPVIAELGGKNPVIVSDEADLDAAVNGVmkgAF 258
Cdd:cd07127 257 VTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEAN----ARQAQVYTEKAGVNTVVVDSTDDLKAMLRNL---AF 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 259 SFA---GQKCSATSRVYVYENIV---------DSFTDRLVEETENLvVGQPTDRETFVSPLIDDEAVDRYreisTQARSD 326
Cdd:cd07127 330 SLSlysGQMCTTPQNIYVPRDGIqtddgrksfDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARI----AEARQL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 327 GTVLTGGSVISDSDLPDGRYVEPTVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDS--EFG-LCAGLFSEDES 403
Cdd:cd07127 405 GEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESvrEHGaMTVGVYSTDPE 484
|
....*..
gi 2082837691 404 EIEQWFD 410
Cdd:cd07127 485 VVERVQE 491
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
75-324 |
3.09e-13 |
|
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: 71.10 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 75 IEAMADVDEAIDFLEFYSREITAADGYRFDTGEPTPGQhTTNLLRPYGVFGVISPFNFPLAIlVGMTTGALITGNTVVLK 154
Cdd:cd07077 56 IAMMGCSESKLYKNIDTERGITASVGHIQDVLLPDNGE-TYVRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFR 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 155 PAEATPLVAHKVMDLFEEA---GIPDGVLNLVTGDGPTTGQPLVEHEAVDGIAFTGSRAVgvgiERTFQELGKRGPVIAE 231
Cdd:cd07077 134 PHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDA----VDAAVKHSPHIPVIGF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 232 LGGKNPVIVSDEADLDAAVNGVMKGAFsFAGQKCSATSRVYV----YENIVDSFTDRLVEETENLVVG-QPTDRETFVSP 306
Cdd:cd07077 210 GAGNSPVVVDETADEERASGSVHDSKF-FDQNACASEQNLYVvddvLDPLYEEFKLKLVVEGLKVPQEtKPLSKETTPSF 288
|
250
....*....|....*...
gi 2082837691 307 liDDEAVDRYREISTQAR 324
Cdd:cd07077 289 --DDEALESMTPLECQFR 304
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
120-393 |
4.31e-12 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 67.65 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 120 PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEA----GIPDGVLNLVTGDGPTTGQPLV 195
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAiaeaGGPDNLVVTVEEPTIETTNELM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 196 EHEAVDGIAFTGsravGVGIERTFQELGKRgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAfSFAGQ-KCSATSRVYVY 274
Cdd:cd07121 177 AHPDINLLVVTG----GPAVVKAALSSGKK--AIGAGAGNPPVVVDETADIEKAARDIVQGA-SFDNNlPCIAEKEVIAV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 275 ENIVDSFTDRLVEETENLVVGQPTDRETFVSPLIDDEAVdryreISTQ--ARSDGTVLTGGSVISDSDLpdgryvePTVV 352
Cdd:cd07121 250 DSVADYLIAAMQRNGAYVLNDEQAEQLLEVVLLTNKGAT-----PNKKwvGKDASKILKAAGIEVPADI-------RLII 317
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2082837691 353 TEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGL 393
Cdd:cd07121 318 VETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGN 358
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
120-394 |
2.03e-11 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 65.69 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 120 PYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKPAEATPLVAHKVMDLFEEA----GIPDGVLNLVTGDGPTTGQPLV 195
Cdd:PRK15398 129 PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAivaaGGPENLVVTVAEPTIETAQRLM 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 196 EHEAVDGIAFTGsravGVGIERTFQELGKRgpVIAELGGKNPVIVSDEADLDAAVNGVMKGAfSFAGQ-KCSATSRVYVY 274
Cdd:PRK15398 209 KHPGIALLVVTG----GPAVVKAAMKSGKK--AIGAGAGNPPVVVDETADIEKAARDIVKGA-SFDNNlPCIAEKEVIVV 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 275 ENIVDSFTDRLVEETENLVVGQPTDRETFVSpLIDDEAVDR------YREISTQArsdgtvltGGSVISDSDLpdgryve 348
Cdd:PRK15398 282 DSVADELMRLMEKNGAVLLTAEQAEKLQKVV-LKNGGTVNKkwvgkdAAKILEAA--------GINVPKDTRL------- 345
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2082837691 349 ptVVTEIPHEHSLAREEHFVPFVTIHPVSGLDAGIEKSNDSEFGLC 394
Cdd:PRK15398 346 --LIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNR 389
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
114-450 |
1.38e-10 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 63.05 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 114 TTNLLRPYGVFGVISPFNFPLAILVGMTTGALITGNTVVLKP----AEATPLVAHKVMDLFEEAGIPDGVLNLVTGDGPT 189
Cdd:cd07081 89 TLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 190 TGQPLVEHEAVDGIAFTGsravGVGIERTFQELGKrgPVIAELGGKNPVIVSDEADLDAAVNGVMKGAFSFAGQKCSATS 269
Cdd:cd07081 169 LAQRLMKFPGIGLLLATG----GPAVVKAAYSSGK--PAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 270 RVYVYENIVDSFTDRLVEETENLVVGQPTDRetfVSPLI-DDEAVDryREISTQARSDGTVLTGGSVISDSDLpdgRYVE 348
Cdd:cd07081 243 SVIVVDSVYDEVMRLFEGQGAYKLTAEELQQ---VQPVIlKNGDVN--RDIVGQDAYKIAAAAGLKVPQETRI---LIGE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2082837691 349 PTVVTeiphEHSLAREEHFVPFVTIHPVSGLDAGIEKS----NDSEFGLCAGLFSEDESEIE---QWFDEIEAGMCYVNr 421
Cdd:cd07081 315 VTSLA----EHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKAIEnmnQFANAMKTSRFVKN- 389
|
330 340 350
....*....|....*....|....*....|
gi 2082837691 422 kQSATTGALVQAQPFGGW-KFSGTTGKFAG 450
Cdd:cd07081 390 -GPCSQGGLGDLYNFRGWpSMTLGCGTWGG 418
|
|
| |
