|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
37-490 |
0e+00 |
|
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: 721.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 37 VLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGE 116
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKT-TARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 117 IQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLS 196
Cdd:cd07103 80 VDYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 197 ALALAQTAEEAGIPAGVFNVITADHsntAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVF 276
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSP---AEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 277 DDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVDKCELLL 356
Cdd:cd07103 237 DDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVK-KLKVGNGLDEGTDMGPLINERAVEKVEALV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 357 SDALGKGSELICGGKR-GEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQS 435
Cdd:cd07103 316 EDAVAKGAKVLTGGKRlGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 339730667 436 RLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYIC 490
Cdd:cd07103 396 RAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVS 450
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
19-493 |
0e+00 |
|
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: 599.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 19 QAYIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETEL 98
Cdd:COG1012 7 PLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAAT-PPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 99 ATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAA 178
Cdd:COG1012 86 AALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 179 LSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSAS 258
Cdd:COG1012 166 LAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGD---GSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 259 TVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKT 338
Cdd:COG1012 243 NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAK-ALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 339 TQGPLVNQKAVDKCELLLSDALGKGSELICGGKR--GEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLE 416
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRpdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339730667 417 AANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISC-AEAAFGGVKESGIGREGGAQGIDEFTNWKYICTQY 493
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
18-490 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 596.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 18 AQAYIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETE 97
Cdd:PLN02278 25 TQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKL-TASERSKILRRWYDLIIANKED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 98 LATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAA 177
Cdd:PLN02278 104 LAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 178 ALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSA 257
Cdd:PLN02278 184 ALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGD---APEIGDALLASPKVRKITFTGSTAVGKKLMAGAA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 258 STVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPK 337
Cdd:PLN02278 261 ATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQ-KLVVGDGFEEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 338 TTQGPLVNQKAVDKCELLLSDALGKGSELICGGKR-GEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLE 416
Cdd:PLN02278 340 VTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRhSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIA 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339730667 417 AANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYIC 490
Cdd:PLN02278 420 IANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVC 493
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
37-487 |
0e+00 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 563.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 37 VLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGE 116
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRAT-TAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 117 IQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLS 196
Cdd:TIGR01780 80 ILYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 197 ALALAQTAEEAGIPAGVFNVITAdhSNTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVF 276
Cdd:TIGR01780 160 ALALARLAEQAGIPKGVLNVITG--SRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 277 DDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVDKCELLL 356
Cdd:TIGR01780 238 DDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVK-KLKVGNGLDEGVTQGPLINEKAVEKVEKHI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 357 SDALGKGSELICGGKRGEHG-TSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQS 435
Cdd:TIGR01780 317 ADAVEKGAKVVTGGKRHELGgNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 339730667 436 RLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWK 487
Cdd:TIGR01780 397 RIWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
26-489 |
0e+00 |
|
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: 552.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 26 WTASEtGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKE 105
Cdd:pfam00171 1 WVDSE-SETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKT-PAAERAAILRKAADLLEERKDELAELETLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 106 QGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVvNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSA 185
Cdd:pfam00171 79 NGKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSDP-GRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 186 VVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCL 265
Cdd:pfam00171 158 VLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGS---GAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 266 ELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVN 345
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAK-KLKVGDPLDPDTDMGPLIS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 346 QKAVDKCELLLSDALGKGSELICGGKRG-EHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVG 424
Cdd:pfam00171 314 KAQLERVLKYVEDAKEEGAKLLTGGEAGlDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339730667 425 LAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAA-FGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:pfam00171 394 LAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLpFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
58-491 |
7.50e-170 |
|
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: 485.56 E-value: 7.50e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 58 EKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQ 137
Cdd:cd07078 1 DAAVAAARAAFKAWAAL-PPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 138 VVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVI 217
Cdd:cd07078 80 VIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 218 TADHSntaEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSG 297
Cdd:cd07078 160 TGDGD---EVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 298 QTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKR--GEH 375
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVK-ALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRleGGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 376 GTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGL 455
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 339730667 456 IS-CAEAAFGGVKESGIGREGGAQGIDEFTNWKYICT 491
Cdd:cd07078 396 VGaEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
19-490 |
5.48e-167 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 480.17 E-value: 5.48e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 19 QAYIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWaHTYSAKQRGAILHKWFEILVQRETEL 98
Cdd:PRK11241 12 QALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAW-RALTAKERANILRRWFNLMMEHQDDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 99 ATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAA 178
Cdd:PRK11241 91 ARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 179 LSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITAdhsNTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSAS 258
Cdd:PRK11241 171 LAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTG---SAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 259 TVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLNPKT 338
Cdd:PRK11241 248 DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAV-SKLHIGDGLEKGV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 339 TQGPLVNQKAVDKCELLLSDALGKGSELICGGKRGE-HGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEA 417
Cdd:PRK11241 327 TIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHElGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQ 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339730667 418 ANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYIC 490
Cdd:PRK11241 407 ANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMC 479
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
21-489 |
4.83e-154 |
|
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: 446.71 E-value: 4.83e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELAT 100
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERL-PAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 101 LLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALS 180
Cdd:cd07088 80 LIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 181 VGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHSNTAEiskYLCESTDVSAISFTGSTPVGKLLLAQSASTV 260
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGD---ALVAHPKVGMISLTGSTEAGQKIMEAAAENI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 261 KRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQ 340
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMK-AVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 341 GPLVNQKAVDKCELLLSDALGKGSELICGGKR--GEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAA 418
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRpeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339730667 419 NNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGlisCAEAAFG---GVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRE---NFEAMQGfhaGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
37-487 |
2.20e-147 |
|
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: 429.28 E-value: 2.20e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 37 VLNPFNNEVVDRATNCTVKDAEKAVHSALEGF-DKWAHTYSAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARG 115
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 116 EIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPL 195
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 196 SALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIV 275
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGF---GPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 276 FDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVDKCELL 355
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARAR-AIRVGDPLDPETQMGPLATERQLEKVERY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 356 LSDALGKGSELICGGKRGEH-----GTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVF 430
Cdd:cd07114 317 VARAREEGARVLTGGERPSGadlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIW 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 339730667 431 GRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWK 487
Cdd:cd07114 397 TRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
21-489 |
8.68e-145 |
|
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: 423.65 E-value: 8.68e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDK--WAHTySAKQRGAILHKWFEILVQRETEL 98
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHL-PAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 99 ATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSA--VVNRLhlhTREPIGVVALIAPWNFPTAMIARKAA 176
Cdd:cd07119 80 ARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPphVISRT---VREPVGVCGLITPWNYPLLQAAWKLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 177 AALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQS 256
Cdd:cd07119 157 PALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGS---GATVGAELAESPDVDLVSFTGGTATGRSIMRAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 257 ASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNP 336
Cdd:cd07119 234 AGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAK-KIKLGNGLDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 337 KTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKRGE-----HGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDE 411
Cdd:cd07119 313 DTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTgdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339730667 412 QEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07119 393 EEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
37-489 |
2.73e-140 |
|
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: 410.77 E-value: 2.73e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 37 VLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGE 116
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSAT-PLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 117 IQYSAAYFDWYAGearrvygQVVPSAVVN-----RLHLHtREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSG 191
Cdd:cd07106 80 VGGAVAWLRYTAS-------LDLPDEVIEdddtrRVELR-RKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 192 DTPLSALALAQTAEEAgIPAGVFNVITADHsntaEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNA 271
Cdd:cd07106 152 FTPLCTLKLGELAQEV-LPPGVLNVVSGGD----ELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGND 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 272 PLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVDK 351
Cdd:cd07106 227 AAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAK-AAVVGDGLDPGTTLGPVQNKMQYDK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 352 CELLLSDALGKGSELICGGKRGE-HGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVF 430
Cdd:cd07106 306 VKELVEDAKAKGAKVLAGGEPLDgPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVW 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 339730667 431 GRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07106 386 SSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
21-487 |
5.02e-140 |
|
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: 411.36 E-value: 5.02e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGNSFDVLNPFN-NEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELA 99
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADlEEVVGTFPLSTASDVDAAVEAAREAFPEWRKV-PAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 100 TLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAAL 179
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 180 SVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHSNTAEIskyLCESTDVSAISFTGSTPVGKLLLAQSAST 259
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEA---LVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 260 VKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKEkLVLGDGLNPKTT 339
Cdd:cd07131 238 NKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKR-LRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 340 QGPLVNQKAVDKCELLLSDALGKGSELICGGKR-----GEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEV 414
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERltgggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339730667 415 LEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLIScAEA--AFGGVKESGIG-REGGAQGIDEFTNWK 487
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIG-AEVhlPFGGVKKSGNGhREAGTTALDAFTEWK 471
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
21-489 |
1.28e-138 |
|
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: 407.27 E-value: 1.28e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELAT 100
Cdd:cd07138 2 YIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSAT-SVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 101 LLTKEQGKPLAEARgEIQYSAA--YFDWYAGEARRV-YGQVVPSAVVnrlhlhTREPIGVVALIAPWNFPTAMIARKAAA 177
Cdd:cd07138 81 AITLEMGAPITLAR-AAQVGLGigHLRAAADALKDFeFEERRGNSLV------VREPIGVCGLITPWNWPLNQIVLKVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 178 ALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSA 257
Cdd:cd07138 154 ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGD---GPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 258 STVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYIsKLAAAMKEKLVLGDGLNPK 337
Cdd:cd07138 231 DTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAE-EIAAAAAEAYVVGDPRDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 338 TTQGPLVNQKAVDKCELLLSDALGKGSELICGG----KRGEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQE 413
Cdd:cd07138 310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339730667 414 VLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLIScAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFN-PGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
56-489 |
6.47e-138 |
|
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: 404.22 E-value: 6.47e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 56 DAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVY 135
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAAT-PPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 136 GQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLS-ALALAQTAEEAGIPAGVF 214
Cdd:cd07104 80 GEILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 215 NVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFR 294
Cdd:cd07104 160 NVVPGG---GSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 295 CSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKRge 374
Cdd:cd07104 237 HQGQICMAAGRILVHESVYDEFVEKLVAKAK-ALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 375 HGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEG 454
Cdd:cd07104 314 EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQ 393
|
410 420 430
....*....|....*....|....*....|....*.
gi 339730667 455 LISC-AEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07104 394 TVNDePHVPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
21-489 |
2.98e-137 |
|
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: 403.88 E-value: 2.98e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDK--WAHTySAKQRGAILHKWFEILVQRETEL 98
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRL-SPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 99 ATLLTKEQGKPLAEAR-GEIQYSAAYFDWYAGEARRV-YGQVVPSAVVNRLHLHtREPIGVVALIAPWNFPTAMIARKAA 176
Cdd:cd07139 81 ARLWTAENGMPISWSRrAQGPGPAALLRYYAALARDFpFEERRPGSGGGHVLVR-REPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 177 AALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsntAEISKYLCESTDVSAISFTGSTPVGKLLLAQS 256
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPAD----REVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 257 ASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLNP 336
Cdd:cd07139 236 GERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAV-AALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 337 KTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKRGEH---GTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQE 413
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGldrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDD 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339730667 414 VLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNeGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07139 395 AVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
19-487 |
4.78e-137 |
|
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: 403.51 E-value: 4.78e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 19 QAYIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFD-KWAHTYSAKQRGAILHKWFEILVQRETE 97
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFEtGWWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 98 LATLLTKEQGKPLAE-ARGEIQYSAAYFDWYAGEARRVYGQVVPSAVvNRLHLHTREPIGVVALIAPWNFPTAMIARKAA 176
Cdd:cd07091 85 LAALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIPIDG-NFLAYTRREPIGVCGQIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 177 AALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITAdHSNTAeiSKYLCESTDVSAISFTGSTPVGKLLL-AQ 255
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPG-FGPTA--GAAISSHMDVDKIAFTGSTAVGRTIMeAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 256 SASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLN 335
Cdd:cd07091 241 AKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARA-EKRVVGDPFD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 336 PKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKR-GEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEV 414
Cdd:cd07091 320 PDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERhGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339730667 415 LEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWK 487
Cdd:cd07091 400 IERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
37-490 |
7.67e-135 |
|
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: 397.32 E-value: 7.67e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 37 VLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEAR-G 115
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRM-SPAERARILHKVADLIEARADELALLESLDTGKPITLARtR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 116 EIQYSAAYFDWYAGEARRVYGQVVPSAVvNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPL 195
Cdd:cd07093 80 DIPRAAANFRFFADYILQLDGESYPQDG-GALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 196 SALALAQTAEEAGIPAGVFNVItadHSNTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIV 275
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVV---HGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 276 FDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVDKCELL 355
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAK-ALKVGDPLDPDTEVGPLISKEHLEKVLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 356 LSDALGKGSELICGGKRGEH-----GTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVF 430
Cdd:cd07093 315 VELARAEGATILTGGGRPELpdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 431 GRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYIC 490
Cdd:cd07093 395 TRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
35-489 |
5.31e-133 |
|
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: 392.46 E-value: 5.31e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 35 FDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEAR 114
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAAT-TPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 115 GEIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTP 194
Cdd:cd07150 80 FETTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 195 LSALALAQTAEEAGIPAGVFNVITAdhsNTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLI 274
Cdd:cd07150 160 VIGLKIAEIMEEAGLPKGVFNVVTG---GGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 275 VFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLNPKTTQGPLVNQKAVDKCEL 354
Cdd:cd07150 237 VLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARA-SKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 355 LLSDALGKGSELICGGKRgeHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQ 434
Cdd:cd07150 316 QVEDAVAKGAKLLTGGKY--DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 339730667 435 SRLQRVARKLEVGMVGVNEGLISC-AEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07150 394 QRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
21-487 |
2.88e-132 |
|
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: 391.23 E-value: 2.88e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGNsfDVLNPFN-NEVVDRATNCTVKDAEKAVHSALEGFDKWAhTYSAKQRGAILHKWFEILVQRETELA 99
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWR-RTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 100 TLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAAL 179
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 180 SVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHSntaEISKYLCESTDVSAISFTGSTPVGKLLLAQSAST 259
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGS---EVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 260 VKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTT 339
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTK-ALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 340 QGPLVNQKAVDKCELLLSDALGKGSELICGG---KRGEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLE 416
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGerlKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339730667 417 AANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNeglISCAE----AAFGGVKESGIG-REGGAQGIDEFTNWK 487
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVN---LPTAGvdyhVPFGGRKGSSYGpREQGEAALEFYTTIK 469
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
35-490 |
1.76e-131 |
|
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: 388.49 E-value: 1.76e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 35 FDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEAR 114
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSL-PAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 115 GEIQYSAAYFDWYAGEARRVYGQVVP-SAVV---NRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPS 190
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKRLAGETIPfDASPggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 191 GDTPLSALALAQTAEEAGIPAGVFNVITADHSntaEISKYLCESTDVSAISFTGSTPVGKLLlaQSASTVKRVCLELGGN 270
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGE---TVGDALVTDPRVRMISFTGSPAVGEAI--ARKAGLKKVTLELGSN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 271 APLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVD 350
Cdd:cd07149 235 AAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATK-KLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 351 KCELLLSDALGKGSELICGGKRgeHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVF 430
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGKR--DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339730667 431 GRDQSRLQRVARKLEVGMVGVNEglISCAEA---AFGGVKESGIGREGGAQGIDEFTNWKYIC 490
Cdd:cd07149 392 TNDLQKALKAARELEVGGVMIND--SSTFRVdhmPYGGVKESGTGREGPRYAIEEMTEIKLVC 452
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
37-489 |
2.62e-130 |
|
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: 385.83 E-value: 2.62e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 37 VLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTYSAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARG- 115
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 116 EIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHT----REPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSG 191
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGRrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 192 DTPLSALALAQTAEEAGIPAGVFNVITadhSNTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNA 271
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVT---GSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 272 PLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLNPKTTQGPLVNQKAVDK 351
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAF-EALPVGDPADPGTVMGPLISAAQRDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 352 CELLLSDALGKGSELICGGKRGEH---GTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGY 428
Cdd:cd07089 317 VEGYIARGRDEGARLVTGGGRPAGldkGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339730667 429 VFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07089 397 VWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
32-489 |
1.03e-129 |
|
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: 384.26 E-value: 1.03e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 32 GNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDK--WAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKP 109
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRL-SPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 110 LAEAR-GEIQYSAAYFDWYAGEARRVYGQVVPSAVvNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVK 188
Cdd:cd07112 80 ISDALaVDVPSAANTFRWYAEAIDKVYGEVAPTGP-DALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 189 PSGDTPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSA-STVKRVCLEL 267
Cdd:cd07112 159 PAEQSPLTALRLAELALEAGLPAGVLNVVPGF---GHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqSNLKRVWLEC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 268 GGNAPLIVFDDA-DLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKEkLVLGDGLNPKTTQGPLVNQ 346
Cdd:cd07112 236 GGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAARE-WKPGDPLDPATRMGALVSE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 347 KAVDKCELLLSDALGKGSELICGGKRG---EHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRV 423
Cdd:cd07112 315 AHFDKVLGYIESGKAEGARLVAGGKRVlteTGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVY 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339730667 424 GLAGYVFGRDQSRLQRVARKLEVGMVGVN---EGLIScaeAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07112 395 GLAASVWTSDLSRAHRVARRLRAGTVWVNcfdEGDIT---TPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
37-490 |
1.92e-127 |
|
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: 378.32 E-value: 1.92e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 37 VLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAhTYSAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARG- 115
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWS-AMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 116 EIQYSAAYFDWYAGEARRVYGQVVPsaVVNR-LHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTP 194
Cdd:cd07115 80 DVPRAADTFRYYAGWADKIEGEVIP--VRGPfLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 195 LSALALAQTAEEAGIPAGVFNVITADHSNTAEiskYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLI 274
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGA---ALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 275 VFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVDKCEL 354
Cdd:cd07115 235 VFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLAR-SLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 355 LLSDALGKGSELICGGKR-GEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRD 433
Cdd:cd07115 314 YVDVGREEGARLLTGGKRpGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 339730667 434 QSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYIC 490
Cdd:cd07115 394 LGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVW 450
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
63-490 |
2.07e-127 |
|
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: 375.03 E-value: 2.07e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 63 SALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSA 142
Cdd:cd06534 2 AARAAFKAWAAL-PPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 143 VVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHS 222
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 223 ntaEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVS 302
Cdd:cd06534 161 ---EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 303 ANRIYVHEKIHDQYISKLAaamkeklvlgdglnpkttqgplvnqkavdkcelllsdalgkgselicggkrgehgtsyepT 382
Cdd:cd06534 238 ASRLLVHESIYDEFVEKLV------------------------------------------------------------T 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 383 LITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLI-SCAEA 461
Cdd:cd06534 258 VLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEA 337
|
410 420
....*....|....*....|....*....
gi 339730667 462 AFGGVKESGIGREGGAQGIDEFTNWKYIC 490
Cdd:cd06534 338 PFGGVKNSGIGREGGPYGLEEYTRTKTVV 366
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
57-487 |
3.11e-127 |
|
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: 376.80 E-value: 3.11e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 57 AEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGEIQYSAAYFDWYA--GE---A 131
Cdd:cd07100 1 IEAALDRAHAAFLAWRKT-SFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAenAEaflA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 132 RRVYGQVVPSAVVnrlhlhTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPA 211
Cdd:cd07100 80 DEPIETDAGKAYV------RYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 212 GVFNVITADHSNTAEIskylCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMAT 291
Cdd:cd07100 154 GVFQNLLIDSDQVEAI----IADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 292 KFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLNPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGK 371
Cdd:cd07100 230 RLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAM-AALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 372 RGEH-GTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVG 450
Cdd:cd07100 309 RPDGpGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVF 388
|
410 420 430
....*....|....*....|....*....|....*..
gi 339730667 451 VNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWK 487
Cdd:cd07100 389 INGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIK 425
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
37-490 |
3.25e-127 |
|
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: 377.80 E-value: 3.25e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 37 VLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGE 116
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSAT-SGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 117 IQYSAAYFDWYAGEARRVYGQVVP----SAVVNRlhlhtREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGD 192
Cdd:cd07090 80 IDSSADCLEYYAGLAPTLSGEHVPlpggSFAYTR-----REPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 193 TPLSALALAQTAEEAGIPAGVFNVITADhsntAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAP 272
Cdd:cd07090 155 TPLTALLLAEILTEAGLPDGVFNVVQGG----GETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 273 LIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVDKC 352
Cdd:cd07090 231 LIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTK-KIRIGDPLDEDTQMGALISEEHLEKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 353 ELLLSDALGKGSELICGGKR-----GEHGTSY-EPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLA 426
Cdd:cd07090 310 LGYIESAKQEGAKVLCGGERvvpedGLENGFYvSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLA 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339730667 427 GYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYIC 490
Cdd:cd07090 390 AGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
35-489 |
1.62e-126 |
|
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: 375.92 E-value: 1.62e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 35 FDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAhTYSAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEAR 114
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMS-NLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 115 GEIQYSAAYFDWYAGEARRVYGQVVPSAVV----NRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPS 190
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPVDAYeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 191 GDTPLSALALAQTAEEAGIPAGVFNVITADHSntaEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGN 270
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGS---EVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 271 APLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVD 350
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVK-KLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 351 KCELLLSDALGKGSELICGGKRgEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVF 430
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGKR-DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 431 GRDQSRLQRVARKLEVGMVGVNE-GLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07145 395 TNDINRALKVARELEAGGVVINDsTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
24-492 |
4.92e-126 |
|
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: 375.10 E-value: 4.92e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 24 GKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLT 103
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAAT-LPQERAEILEKAAQILEERRDEIVEWLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 104 KEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGC 183
Cdd:cd07151 80 RESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 184 SAVVKPSGDTPLSA-LALAQTAEEAGIPAGVFNVITADHSntaEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKR 262
Cdd:cd07151 160 AVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGS---EIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 263 VCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGP 342
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVK-ALPYGDPSDPDTVVGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 343 LVNQKAVDKCELLLSDALGKGSELICGGKRgeHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCR 422
Cdd:cd07151 316 LINESQVDGLLDKIEQAVEEGATLLVGGEA--EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339730667 423 VGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLIS-CAEAAFGGVKESGIGREGGAQGIDEFTNWKYICTQ 492
Cdd:cd07151 394 YGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
37-489 |
2.20e-125 |
|
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: 373.11 E-value: 2.20e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 37 VLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTYSAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGE 116
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 117 IQYSAAYFDWYAGEARRVYGQVVPSAVvNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLS 196
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLGP-GYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 197 ALALAQTAEEAGIPAGVFNVITAdhsNTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVF 276
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTG---LGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 277 DDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGL-NPKTtqGPLVNQKAVDKCELL 355
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERF-RALRVGPGLeDPDL--GPLISAKQLDRVEGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 356 LSDALGKGSELICGGKRGEHGTS----YEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFG 431
Cdd:cd07109 314 VARARARGARIVAGGRIAEGAPAggyfVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWT 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 339730667 432 RDQSRLQRVARKLEVGMVGVNE-GLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07109 394 RDGDRALRVARRLRAGQVFVNNyGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
21-487 |
2.79e-125 |
|
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: 373.82 E-value: 2.79e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGnSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELAT 100
Cdd:cd07086 2 VIGGEWVGSGGE-TFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKV-PAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 101 LLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALS 180
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 181 VGCSAVVKPSGDTPLSALALAQTAEEA----GIPAGVFNVITADhsntAEISKYLCESTDVSAISFTGSTPVGKLLLAQS 256
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGG----GDGGELLVHDPRVPLVSFTGSTEVGRRVGETV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 257 ASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNP 336
Cdd:cd07086 236 ARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYK-QVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 337 KTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKR---GEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQE 413
Cdd:cd07086 315 GTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRidgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339730667 414 VLEAANNCRVGLAGYVFGRDQSRLQRV--ARKLEVGMVGVNEGLIScAEA--AFGGVKESGIGREGGAQGIDEFTNWK 487
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSG-AEIggAFGGEKETGGGRESGSDAWKQYMRRS 471
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
38-489 |
2.59e-123 |
|
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: 367.82 E-value: 2.59e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 38 LNPFNNEVVDRATNCTVKDAEKAVHSALEGFDK-WAHTYSAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGE 116
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 117 IQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLS 196
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 197 ALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVF 276
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGY---GATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 277 DDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLNPKTTQGPLVNQKAVDKCELLL 356
Cdd:cd07118 239 ADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARS-RKVRVGDPLDPETKVGAIINEAQLAKITDYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 357 SDALGKGSELICGGKRGEH--GTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQ 434
Cdd:cd07118 318 DAGRAEGATLLLGGERLASaaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 339730667 435 SRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07118 398 DTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
18-487 |
2.21e-122 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 366.51 E-value: 2.21e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 18 AQAYIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAhTYSAKQRGAILHKWFEILVQRETE 97
Cdd:PRK13252 7 QSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWA-AMTAMERSRILRRAVDILRERNDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 98 LATLLTKEQGKPLAEAR-GEIQYSAAYFDWYAGEARRVYGQVVP----SAVVNRlhlhtREPIGVVALIAPWNFPTAMIA 172
Cdd:PRK13252 86 LAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPlrggSFVYTR-----REPLGVCAGIGAWNYPIQIAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 173 RKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsntAEISKYLCESTDVSAISFTGSTPVGKLL 252
Cdd:PRK13252 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGD----GRVGAWLTEHPDIAKVSFTGGVPTGKKV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 253 LAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGD 332
Cdd:PRK13252 237 MAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERV-ERIRIGD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 333 GLNPKTTQGPLVNQKAVDKceLLLSDALGK--GSELICGGKRGEHGTS-----YEPTLITNVQSNTNIAHTEIFGPIASV 405
Cdd:PRK13252 316 PMDPATNFGPLVSFAHRDK--VLGYIEKGKaeGARLLCGGERLTEGGFangafVAPTVFTDCTDDMTIVREEIFGPVMSV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 406 QKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTN 485
Cdd:PRK13252 394 LTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQ 473
|
..
gi 339730667 486 WK 487
Cdd:PRK13252 474 IK 475
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
37-489 |
7.10e-120 |
|
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: 358.97 E-value: 7.10e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 37 VLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWaHTYSAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGE 116
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRW-KKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 117 IQYSAAYFDWYAGEARRVyGQVVPSAV---VNRLHLHTR-EPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGD 192
Cdd:cd07110 80 VDDVAGCFEYYADLAEQL-DAKAERAVplpSEDFKARVRrEPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 193 TPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAP 272
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGT---GDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 273 LIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLNPKTTQGPLVNQKAVDKC 352
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAA-EAIRVGDPLEEGVRLGPLVSQAQYEKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 353 ELLLSDALGKGSELICGGKRGEHGTS---YEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYV 429
Cdd:cd07110 315 LSFIARGKEEGARLLCGGRRPAHLEKgyfIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 430 FGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07110 395 ISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
21-487 |
3.47e-118 |
|
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: 355.95 E-value: 3.47e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTYSAKQRGAILHKWFEiLVQRETE-LA 99
Cdd:cd07144 11 FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGEERGELLDKLAD-LVEKNRDlLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 100 TLLTKEQGKPL-AEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVvNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAA 178
Cdd:cd07144 90 AIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSP-NKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 179 LSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITAdhsNTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSAS 258
Cdd:cd07144 169 LAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPG---YGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 259 TVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKEKLVLGDGLNPKT 338
Cdd:cd07144 246 NLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYKVGSPFDDDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 339 TQGPLVNQKAVDKCELLLSDALGKGSELICGG----KRGEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEV 414
Cdd:cd07144 326 VVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekapEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339730667 415 LEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWK 487
Cdd:cd07144 406 IKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
36-490 |
5.16e-118 |
|
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: 354.43 E-value: 5.16e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 36 DVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARG 115
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRAL-PPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 116 EIQYSAAYFDWYAGEARRVYGQVVPS----AVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSG 191
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 192 DTPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSAstVKRVCLELGGNA 271
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGE---REVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 272 PLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVDK 351
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVK-KLKVGDPLDEDTDVGPLISEEAAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 352 CELLLSDALGKGSELICGGKRgeHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFG 431
Cdd:cd07094 315 VERWVEEAVEAGARLLCGGER--DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 432 RDQSRLQRVARKLEVGMVGVNEGLISCAEA-AFGGVKESGIGREGGAQGIDEFTNWKYIC 490
Cdd:cd07094 393 RDLNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVV 452
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
37-489 |
1.68e-117 |
|
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: 353.20 E-value: 1.68e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 37 VLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPL-AEARG 115
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAAT-PARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 116 EIQYSAAYFDWYAGEARRVYGQVVPSAVvNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPL 195
Cdd:cd07108 80 EAAVLADLFRYFGGLAGELKGETLPFGP-DVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 196 SALALAQTAEEAgIPAGVFNVITADHSntaEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIV 275
Cdd:cd07108 159 AVLLLAEILAQV-LPAGVLNVITGYGE---ECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 276 FDDADLDVAVNGTMA-TKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLNPKTTQGPLVNQKAVDKCEL 354
Cdd:cd07108 235 FPDADLDDAVDGAIAgMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKL-SKLKIGDPLDEATDIGAIISEKQFAKVCG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 355 LLSDALG-KGSELICGGK-----RGEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGY 428
Cdd:cd07108 314 YIDLGLStSGATVLRGGPlpgegPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAY 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339730667 429 VFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQG-IDEFTNWKYI 489
Cdd:cd07108 394 VWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
38-490 |
3.56e-117 |
|
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: 352.03 E-value: 3.56e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 38 LNPFNNEVVDRATNCTVKDAEKAVHSALEGFDK--WAHtySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARG 115
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWAH--DPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 116 EIQYSAAYFDWYAGEARRVYGQVV-PSAvvNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTP 194
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIePEP--GSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 195 LSALALAQT-AEEAGIPAGVFNVITadhSNTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPL 273
Cdd:cd07120 158 QINAAIIRIlAEIPSLPAGVVNLFT---ESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 274 IVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLNPKTTQGPLVNQKAVDKCE 353
Cdd:cd07120 235 IVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARL-AAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 354 LLLSDALGKGSELICGGKRGEHGTS----YEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYV 429
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTEGLAkgafLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339730667 430 FGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYIC 490
Cdd:cd07120 394 WTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
19-489 |
3.06e-116 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 350.36 E-value: 3.06e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 19 QAYIGGKWTASEtGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETEL 98
Cdd:PRK13473 4 KLLINGELVAGE-GEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQT-TPKERAEALLKLADAIEENADEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 99 ATLLTKEQGKPLAEARG-EIQYSAAYFDWYAGEARRVYGQVVPSAVVNrlhlHT----REPIGVVALIAPWNFPTAMIAR 173
Cdd:PRK13473 82 ARLESLNCGKPLHLALNdEIPAIVDVFRFFAGAARCLEGKAAGEYLEG----HTsmirRDPVGVVASIAPWNYPLMMAAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 174 KAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAgIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLL 253
Cdd:PRK13473 158 KLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGR---GATVGDALVGHPKVRMVSLTGSIATGKHVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 254 AQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDG 333
Cdd:PRK13473 234 SAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVA-TLKVGDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 334 LNPKTTQGPLVNQKAVDKCELLLSDALGKG-SELICGGKRGEH-GTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDE 411
Cdd:PRK13473 313 DDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGkGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339730667 412 QEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
56-489 |
1.43e-115 |
|
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: 347.26 E-value: 1.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 56 DAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVY 135
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKT-PPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 136 GQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFN 215
Cdd:cd07105 80 GGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 216 VITADHSNTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRC 295
Cdd:cd07105 160 VVTHSPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 296 SGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDglnpkTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKR--G 373
Cdd:cd07105 240 SGQICMSTERIIVHESIADEFVEKLKAAA-EKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLAdeS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 374 EHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNE 453
Cdd:cd07105 314 PSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHING 393
|
410 420 430
....*....|....*....|....*....|....*..
gi 339730667 454 GLISC-AEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07105 394 MTVHDePTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
35-484 |
1.90e-115 |
|
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: 347.70 E-value: 1.90e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 35 FDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEAR 114
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRAL-PAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 115 GEIQYSAAYFDWYAGEARRVYGQVVP----SAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPS 190
Cdd:cd07147 80 GEVARAIDTFRIAAEEATRIYGEVLPldisARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 191 GDTPLSALALAQTAEEAGIPAGVFNVITADHsntaEISKYLCESTDVSAISFTGSTPVGKLLLAQSAStvKRVCLELGGN 270
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLPCSR----DDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 271 APLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVD 350
Cdd:cd07147 234 AAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVK-ALKTGDPKDDATDVGPMISESEAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 351 KCELLLSDALGKGSELICGGKRgeHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVF 430
Cdd:cd07147 313 RVEGWVNEAVDAGAKLLTGGKR--DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVF 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 339730667 431 GRDQSRLQRVARKLEVGMVGVNEglISCAEA---AFGGVKESGIGREGGAQGIDEFT 484
Cdd:cd07147 391 TRDLEKALRAWDELEVGGVVIND--VPTFRVdhmPYGGVKDSGIGREGVRYAIEEMT 445
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
21-493 |
1.36e-114 |
|
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: 346.35 E-value: 1.36e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTYSAKQRGAILHKWFEILVQRETELAT 100
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 101 LLTKEQGKPLAEARG-EIQYSAAYFDWYAGEARRVYGQV----VPSAVVNRLHLHT-REPIGVVALIAPWNFPTAMIARK 174
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETlapsIPSMQGERYTAFTrREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 175 AAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsntAEISKYLCESTDVSAISFTGSTPVGKLLLA 254
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGK----GAVGAQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 255 QSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKEkLVLGDGL 334
Cdd:cd07113 239 QAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSS-FQVGSPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 335 NPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKRGEhGTSY--EPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQ 412
Cdd:cd07113 318 DESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA-GEGYfvQPTLVLARSADSRLMREETFGPVVSFVPYEDEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 413 EVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYICTQ 492
Cdd:cd07113 397 ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
.
gi 339730667 493 Y 493
Cdd:cd07113 477 Y 477
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
15-493 |
7.61e-114 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 345.18 E-value: 7.61e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 15 PQGAQAYIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDK-----WAHT---YSAKQRGAILHK 86
Cdd:PLN02467 5 VPRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTtgaVRAKYLRAIAAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 87 wfeiLVQRETELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQvvPSAVVN------RLHLhTREPIGVVAL 160
Cdd:PLN02467 85 ----ITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAK--QKAPVSlpmetfKGYV-LKEPLGVVGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 161 IAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITAdhsNTAEISKYLCESTDVSAI 240
Cdd:PLN02467 158 ITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTG---LGTEAGAPLASHPGVDKI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 241 SFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKL 320
Cdd:PLN02467 235 AFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 321 AAAMKeKLVLGDGLNPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKRGEH---GTSYEPTLITNVQSNTNIAHTE 397
Cdd:PLN02467 315 VKWAK-NIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkkGFFIEPTIITDVTTSMQIWREE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 398 IFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGA 477
Cdd:PLN02467 394 VFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGE 473
|
490
....*....|....*.
gi 339730667 478 QGIDEFTNWKYIcTQY 493
Cdd:PLN02467 474 WGLENYLSVKQV-TKY 488
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
21-476 |
2.81e-113 |
|
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: 344.21 E-value: 2.81e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTasETGNSFDVLNPFN-NEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELA 99
Cdd:cd07124 36 VIGGKEV--RTEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRT-PPEERARLLLRAAALLRRRRFELA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 100 TLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSA--VVNRLHLhtrEPIGVVALIAPWNFPTAMIARKAAA 177
Cdd:cd07124 113 AWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVpgEDNRYVY---RPLGVGAVISPWNFPLAILAGMTTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 178 ALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSA 257
Cdd:cd07124 190 ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGP---GEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 258 ST------VKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLG 331
Cdd:cd07124 267 KVqpgqkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTK-ALKVG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 332 DGLNPKTTQGPLVNQKAVDKCELLLSDALGKGSeLICGGKRGEHGT-SY--EPTLITNVQSNTNIAHTEIFGPIASVQKF 408
Cdd:cd07124 346 DPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGR-LLLGGEVLELAAeGYfvQPTIFADVPPDHRLAQEEIFGPVLAVIKA 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339730667 409 RDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGlisCAEA-----AFGGVKESGIGREGG 476
Cdd:cd07124 425 KDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRK---ITGAlvgrqPFGGFKMSGTGSKAG 494
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
19-489 |
6.64e-113 |
|
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: 341.86 E-value: 6.64e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 19 QAYIGGKWTASEtGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTYSAKQRGAILHKWFEILVQRETEL 98
Cdd:cd07082 3 KYLINGEWKESS-GKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 99 ATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPS----AVVNRLHLHTREPIGVVALIAPWNFPTAMIARK 174
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGdwfpGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 175 AAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHSntaEISKYLCESTDVSAISFTGSTPVGKLLLA 254
Cdd:cd07082 162 LIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGR---EIGDPLVTHGRIDVISFTGSTEVGNRLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 255 QSAstVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGL 334
Cdd:cd07082 239 QHP--MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEV-AKLKVGMPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 335 NPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKRgEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEV 414
Cdd:cd07082 316 DNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR-EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339730667 415 LEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEgliSCAEA----AFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07082 395 IELANKSNYGLQASIFTKDINKARKLADALEVGTVNINS---KCQRGpdhfPFLGRKDSGIGTQGIGDALRSMTRRKGI 470
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
19-491 |
7.79e-113 |
|
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: 341.78 E-value: 7.79e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 19 QAYIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDK--WAHTySAKQRGAILHKWFEILVQRET 96
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRM-TGYERSRILLRFADLLEKHAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 97 ELATLLTKEQGKPLAEAR-GEIQYSAAYFDWYAGEARRVYGQVVPSAvvNRLHLHT-REPIGVVALIAPWNFPTAMIARK 174
Cdd:cd07142 84 ELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPAD--GPHHVYTlHEPIGVVGQIIPWNFPLLMFAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 175 AAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHSNT-AEISKYLcestDVSAISFTGSTPVGKLLL 253
Cdd:cd07142 162 VGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAgAAIASHM----DVDKVAFTGSTEVGKIIM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 254 -AQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKlAAAMKEKLVLGD 332
Cdd:cd07142 238 qLAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEK-AKARALKRVVGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 333 GLNPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKR-GEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDE 411
Cdd:cd07142 317 PFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRiGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 412 QEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYICT 491
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVVM 476
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
37-491 |
1.13e-112 |
|
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: 340.46 E-value: 1.13e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 37 VLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEAR-G 115
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRT-TPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 116 EIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPL 195
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 196 SALALAQTAEEaGIPAGVFNVITADHSNTAEiskYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIV 275
Cdd:cd07092 160 TTLLLAELAAE-VLPPGVVNVVCGGGASAGD---ALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 276 FDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVDKCELL 355
Cdd:cd07092 236 FDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVS-AIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 356 LsDALGKGSELICGGKRGE-HGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQ 434
Cdd:cd07092 315 V-ERAPAHARVLTGGRRAEgPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDV 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 339730667 435 SRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYICT 491
Cdd:cd07092 394 GRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
19-489 |
1.33e-112 |
|
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: 341.25 E-value: 1.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 19 QAYIGGKWTASETGNSFDVLNPFNNEVV------DRAtnctvkDAEKAVHSALEGFDK---WaHTYSAKQRGAILHKWFE 89
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKIcevqegDKA------DVDKAVKAARAAFKLgspW-RTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 90 ILVQRETELATLLTKEQGKPLAEAR-GEIQYSAAYFDWYAGEARRVYGQVVPSAvvNRLHLHTR-EPIGVVALIAPWNFP 167
Cdd:cd07141 81 LIERDRAYLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTIPMD--GDFFTYTRhEPVGVCGQIIPWNFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 168 TAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITA-DHSNTAEISKYLcestDVSAISFTGST 246
Cdd:cd07141 159 LLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHP----DIDKVAFTGST 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 247 PVGKLLL-AQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMK 325
Cdd:cd07141 235 EVGKLIQqAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 326 eKLVLGDGLNPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKR-GEHGTSYEPTLITNVQSNTNIAHTEIFGPIAS 404
Cdd:cd07141 315 -KRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRhGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 405 VQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFT 484
Cdd:cd07141 394 IFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYT 473
|
....*
gi 339730667 485 NWKYI 489
Cdd:cd07141 474 EVKTV 478
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
21-493 |
1.50e-111 |
|
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: 338.55 E-value: 1.50e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELAT 100
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKT-SVAERANILNKIADRIEENLELLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 101 LLTKEQGKPLAEARG-EIQYSAAYFDWYAGEARRVYGQVvpsAVVNR--LHLHTREPIGVVALIAPWNFPTAMIARKAAA 177
Cdd:cd07559 83 AETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSL---SEIDEdtLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 178 ALSVGCSAVVKPSGDTPLSALALAQTAEEAgIPAGVFNVITADHSntaEISKYLCESTDVSAISFTGSTPVGKLLLAQSA 257
Cdd:cd07559 160 ALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGS---EAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 258 STVKRVCLELGGNAPLIVFDDAD------LDVAVNGTMATKFRcSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLG 331
Cdd:cd07559 236 ENLIPVTLELGGKSPNIFFDDAMdadddfDDKAEEGQLGFAFN-QGEVCTCPSRALVQESIYDEFIERAVERF-EAIKVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 332 DGLNPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKRGE-----HGTSYEPTLITNVQSNTNIAHTEIFGPIASVQ 406
Cdd:cd07559 314 NPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTlggldKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 407 KFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNW 486
Cdd:cd07559 394 TFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQT 473
|
....*..
gi 339730667 487 KYICTQY 493
Cdd:cd07559 474 KNILVSY 480
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
21-487 |
5.47e-111 |
|
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: 337.19 E-value: 5.47e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFD-KWAHTYSAKQRGAILHKWFEILVQRETELA 99
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWGLKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 100 TLLTKEQGKP-LAEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVvNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAA 178
Cdd:cd07143 90 SIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIETDI-KKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 179 LSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHSNT-AEISKYLcestDVSAISFTGSTPVG-KLLLAQS 256
Cdd:cd07143 169 LAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHM----DIDKVAFTGSTLVGrKVMEAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 257 ASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNP 336
Cdd:cd07143 245 KSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAK-KLKVGDPFAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 337 KTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKR-GEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVL 415
Cdd:cd07143 324 DTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRhGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339730667 416 EAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWK 487
Cdd:cd07143 404 KRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIK 475
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
21-491 |
1.10e-108 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 331.79 E-value: 1.10e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFD--KWAHTySAKQRGAILHKWFEILVQRETEL 98
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRM-SGFERGRIMMKFADLIEEHIEEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 99 ATLLTKEQGKPLAEARG-EIQYSAAYFDWYAGEARRVYGQVVpsAVVNRLHLHT-REPIGVVALIAPWNFPTAMIARKAA 176
Cdd:PLN02766 103 AALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETL--KMSRQLQGYTlKEPIGVVGHIIPWNFPSTMFFMKVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 177 AALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHSNT-AEISKYLcestDVSAISFTGSTPVGKLLL-A 254
Cdd:PLN02766 181 PALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAgAAIASHM----DVDKVSFTGSTEVGRKIMqA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 255 QSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGL 334
Cdd:PLN02766 257 AATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAK-DWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 335 NPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKR-GEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQE 413
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPcGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339730667 414 VLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYICT 491
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVT 493
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
38-489 |
1.18e-107 |
|
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: 327.64 E-value: 1.18e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 38 LNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGEI 117
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAAL-GVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 118 QYSAAYFDWYAGEARRVYG-QVVPSAVVNRLHLHT--REPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTP 194
Cdd:cd07099 80 LLALEAIDWAARNAPRVLApRKVPTGLLMPNKKATveYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 195 LSALALAQTAEEAGIPAGVFNVITADhsntAEISKYLCESTdVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLI 274
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGD----GATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 275 VFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLNPKTTQGPLVNQKAVDKCEL 354
Cdd:cd07099 235 VLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKA-RALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 355 LLSDALGKGSELICGGKRGE-HGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRD 433
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNgGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 339730667 434 QSRLQRVARKLEVGMVGVNEGL--ISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLltAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
21-489 |
1.88e-107 |
|
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: 327.87 E-value: 1.88e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELAT 100
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKT-TVAERANILNKIADIIDENKELLAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 101 LLTKEQGKPLAEARG-EIQYSAAYFDWYAGEARRVYGQVVpsaVVNR--LHLHTREPIGVVALIAPWNFPTAMIARKAAA 177
Cdd:cd07117 83 VETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSAN---MIDEdtLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 178 ALSVGCSAVVKPSGDTPLSALALAQTAEEAgIPAGVFNVITADHSNTAEiskYLCESTDVSAISFTGSTPVGKLLLAQSA 257
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGE---YLLNHPGLDKLAFTGSTEVGRDVAIAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 258 STVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLNPK 337
Cdd:cd07117 236 KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKF-ENVKVGNPLDPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 338 TTQGPLVNQKAVDKCELLLSDALGKGSELICGGKR-----GEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQ 412
Cdd:cd07117 315 TQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRltengLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTED 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339730667 413 EVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07117 395 EVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
37-489 |
4.30e-105 |
|
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: 321.25 E-value: 4.30e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 37 VLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGE 116
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRAT-TPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 117 IQYSAAYFDWYAGEARRVYGQVVPSAVVNrLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLS 196
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKGETIPVGGRN-LHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 197 ALALAQTAEEAgIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVF 276
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGD---GATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 277 DDADLDVAVNGTMA-TKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLNPKTTQGPLVNQKAVDKCELL 355
Cdd:cd07107 235 PDADPEAAADAAVAgMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERV-AAIKVGDPTDPATTMGPLVSRQQYDRVMHY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 356 LSDALGKGSELICGGKR-----GEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVF 430
Cdd:cd07107 314 IDSAKREGARLVTGGGRpegpaLEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIW 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 339730667 431 GRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07107 394 TNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
37-487 |
2.54e-104 |
|
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: 318.92 E-value: 2.54e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 37 VLNPFNNEVVDratncTV-KDAEKAVHSALEGFDKWAHTYSAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARG 115
Cdd:cd07146 3 VRNPYTGEVVG-----TVpAGTEEALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 116 EIQYSAAYFDWYAGEARRVYGQVVPSAVVN----RLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSG 191
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFSCDLTAngkaRKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 192 DTPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSAstVKRVCLELGGNA 271
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGE---PGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 272 PLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVDK 351
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSA-ALVVGDPMDPATDMGTVIDEEAAIQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 352 CELLLSDALGKGSELICGGKRgeHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFG 431
Cdd:cd07146 312 IENRVEEAIAQGARVLLGNQR--QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 339730667 432 RDQSRLQRVARKLEVGMVGVNEGLISCAE-AAFGGVKESGIG-REGGAQGIDEFTNWK 487
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGgKEGVREAMKEMTNVK 447
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
56-489 |
1.44e-103 |
|
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: 316.93 E-value: 1.44e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 56 DAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVY 135
Cdd:cd07152 14 DVDRAAARAAAAQRAWAAT-PPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 136 GQVVPSAVvNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSA-LALAQTAEEAGIPAGVF 214
Cdd:cd07152 93 GEILPSAP-GRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 215 NVITADhsntAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFR 294
Cdd:cd07152 172 HVLPGG----ADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 295 CSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKRge 374
Cdd:cd07152 248 HQGQICMAAGRHLVHESVADAYTAKLAAKAK-HLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTY-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 375 HGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEG 454
Cdd:cd07152 325 DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ 404
|
410 420 430
....*....|....*....|....*....|....*..
gi 339730667 455 LISC-AEAAFGGVKESGIG-REGGAQGIDEFTNWKYI 489
Cdd:cd07152 405 TVNDePHNPFGGMGASGNGsRFGGPANWEEFTQWQWV 441
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
19-493 |
3.95e-103 |
|
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: 317.13 E-value: 3.95e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 19 QAYIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDK-WAHTYSAKQRGAILHKWFEILVQRETE 97
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgEWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 98 LATLLTKEQGKPLAEA-RGEIQYSAAYFDWYAGEARRVYGQVVP--SAVVNR-LHLHTREPIGVVALIAPWNFPTAMIAR 173
Cdd:cd07140 87 LATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRnLTLTKREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 174 KAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHSNtaeISKYLCESTDVSAISFTGSTPVGKLLL 253
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSL---VGQRLSDHPDVRKLGFTGSTPIGKHIM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 254 AQSA-STVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGD 332
Cdd:cd07140 244 KSCAvSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVK-KMKIGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 333 GLNPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKRGEH-GTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDE 411
Cdd:cd07140 323 PLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRpGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 412 --QEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07140 403 dvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
....
gi 339730667 490 CTQY 493
Cdd:cd07140 483 TIEY 486
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
4-483 |
1.03e-100 |
|
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: 310.87 E-value: 1.03e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 4 LSQFKRSYSLlpqgaqaYIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAhTYSAKQRGAI 83
Cdd:cd07111 15 LDAHDRSFGH-------FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWS-ALPGHVRARH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 84 LHKWFEILVQRETELATLLTKEQGKPLAEAR-GEIQYSAAYFDWYAGEArrvygQVVPSAvvnrlhLHTREPIGVVALIA 162
Cdd:cd07111 87 LYRIARHIQKHQRLFAVLESLDNGKPIRESRdCDIPLVARHFYHHAGWA-----QLLDTE------LAGWKPVGVVGQIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 163 PWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsntAEISKYLCESTDVSAISF 242
Cdd:cd07111 156 PWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGN----GSFGSALANHPGVDKVAF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 243 TGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAA 322
Cdd:cd07111 232 TGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 323 AMKeKLVLGDGLNPKTTQGPLVNQKAVDKCELLLSDALGKGSELI-CGGKRGEHGTSYEPTLITNVQSNTNIAHTEIFGP 401
Cdd:cd07111 312 RMS-HLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFqPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 402 IASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGID 481
Cdd:cd07111 391 VLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLY 470
|
..
gi 339730667 482 EF 483
Cdd:cd07111 471 EY 472
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
19-491 |
2.70e-100 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 311.36 E-value: 2.70e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 19 QAYIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDK--WAHTySAKQRGAILHKWFEILVQRET 96
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKM-TAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 97 ELATLLTKEQGKPLAEARG-EIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLH-LHtrEPIGVVALIAPWNFPTAMIARK 174
Cdd:PLN02466 138 ELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPADGPHHVQtLH--EPIGVAGQIIPWNFPLLMFAWK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 175 AAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITAdHSNTAEISkyLCESTDVSAISFTGSTPVGKLLLA 254
Cdd:PLN02466 216 VGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSG-FGPTAGAA--LASHMDVDKLAFTGSTDTGKIVLE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 255 QSA-STVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKlAAAMKEKLVLGDG 333
Cdd:PLN02466 293 LAAkSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK-AKARALKRVVGDP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 334 LNPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKR-GEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQ 412
Cdd:PLN02466 372 FKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRfGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLD 451
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339730667 413 EVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYICT 491
Cdd:PLN02466 452 EVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 530
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
28-492 |
4.87e-99 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 307.58 E-value: 4.87e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 28 ASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQG 107
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAAT-PVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 108 KPLAEARGEIQYSAAYFDWYAGEA------RRVYGqVVPSAVVNRlhlHTREPIGVVALIAPWNFPTAMIARKAAAALSV 181
Cdd:PRK09407 106 KARRHAFEEVLDVALTARYYARRApkllapRRRAG-ALPVLTKTT---ELRQPKGVVGVISPWNYPLTLAVSDAIPALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 182 GCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHSntaEISKYLCESTDVsaISFTGSTPVGKLLLAQSASTVK 261
Cdd:PRK09407 182 GNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGP---VVGTALVDNADY--LMFTGSTATGRVLAEQAGRRLI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 262 RVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTTQG 341
Cdd:PRK09407 257 GFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVR-AMRLGAGYDYSADMG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 342 PLVNQKAVDKCELLLSDALGKGSELICGGK-RGEHGTS-YEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAAN 419
Cdd:PRK09407 336 SLISEAQLETVSAHVDDAVAKGATVLAGGKaRPDLGPLfYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERAN 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339730667 420 NCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISC---AEAAFGGVKESGIGREGGAQGIDEFTNWKYICTQ 492
Cdd:PRK09407 416 DTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAwgsVDAPMGGMKDSGLGRRHGAEGLLKYTESQTIATQ 491
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
40-484 |
1.65e-98 |
|
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: 304.23 E-value: 1.65e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 40 PFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGEIQY 119
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAAR-PFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 120 SAAYFDWYAGEARRVY-----GQVVPSAVVNRlhlHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTP 194
Cdd:cd07101 82 VAIVARYYARRAERLLkprrrRGAIPVLTRTT---VNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 195 LSALALAQTAEEAGIPAGVFNVITADHSntaEISKYLCESTDVsaISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLI 274
Cdd:cd07101 159 LTALWAVELLIEAGLPRDLWQVVTGPGS---EVGGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 275 VFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLNPKTTQGPLVNQKAVDKCEL 354
Cdd:cd07101 234 VLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVART-RALRLGAALDYGPDMGSLISQAQLDRVTA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 355 LLSDALGKGSELICGGK-RGEHGTS-YEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGR 432
Cdd:cd07101 313 HVDDAVAKGATVLAGGRaRPDLGPYfYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 339730667 433 DQSRLQRVARKLEVGMVGVNEGLISC---AEAAFGGVKESGIGREGGAQGIDEFT 484
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNEGYAAAwasIDAPMGGMKDSGLGRRHGAEGLLKYT 447
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
93-493 |
9.28e-95 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 293.18 E-value: 9.28e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 93 QRETELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIA 172
Cdd:PRK10090 10 ERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPFFLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 173 RKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHSntaEISKYLCESTDVSAISFTGSTPVGKLL 252
Cdd:PRK10090 90 RKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGE---TVGQELAGNPKVAMVSMTGSVSAGEKI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 253 LAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGD 332
Cdd:PRK10090 167 MAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ-AVQFGN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 333 GL-NPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKR-GEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRD 410
Cdd:PRK10090 246 PAeRNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAvEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 411 EQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYIC 490
Cdd:PRK10090 326 LEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVVY 405
|
...
gi 339730667 491 TQY 493
Cdd:PRK10090 406 LQS 408
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
21-489 |
1.02e-94 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 295.65 E-value: 1.02e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDK--WAHTYSAkQRGAILHKWFEILVQRETEL 98
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPA-KRKAVLNKLADLMEAHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 99 ATLLTKEQGKPLAEA-RGEIQYSAAYFDWYAGEARRVYGQVVPSAVvNRLHLHTREPIGVVALIAPWNFPTAMIARKAAA 177
Cdd:PRK09847 102 ALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSS-HELAMIVREPVGVIAAIVPWNFPLLLTCWKLGP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 178 ALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITA-DHsntaEISKYLCESTDVSAISFTGSTPVGKLLLAQS 256
Cdd:PRK09847 181 ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGH----EAGQALSRHNDIDAIAFTGSTRTGKQLLKDA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 257 A-STVKRVCLELGGNAPLIVFDDA-DLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKEkLVLGDGL 334
Cdd:PRK09847 257 GdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQN-WQPGHPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 335 NPKTTQGPLVNQKAVDKCELLLSDALGKGsELICGGKRGEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEV 414
Cdd:PRK09847 336 DPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339730667 415 LEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:PRK09847 415 LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
19-493 |
4.45e-94 |
|
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: 293.65 E-value: 4.45e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 19 QAYIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETEL 98
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSAT-PVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 99 ATLLTKEQGKPLAEARGEIQY---------SAAYFDwyAGEarrvYGQVVPSAVVNRLhlhTREPIGVVALIAPWNFPTA 169
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRglevvefacSIPHLL--KGE----YLENVARGIDTYS---YRQPLGVVAGITPFNFPAM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 170 MIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHsntaEISKYLCESTDVSAISFTGSTPVG 249
Cdd:cd07085 152 IPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGK----EAVNALLDHPDIKAVSFVGSTPVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 250 KLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLV 329
Cdd:cd07085 228 EYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAK-KLK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 330 LGDGLNPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGkRGEHGTSYE------PTLITNVQSNTNIAHTEIFGPIA 403
Cdd:cd07085 307 VGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDG-RGVKVPGYEngnfvgPTILDNVTPDMKIYKEEIFGPVL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 404 SVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGL-ISCAEAAFGGVKESGIGREG--GAQGI 480
Cdd:cd07085 386 SIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIpVPLAFFSFGGWKGSFFGDLHfyGKDGV 465
|
490
....*....|...
gi 339730667 481 DEFTNWKYICTQY 493
Cdd:cd07085 466 RFYTQTKTVTSRW 478
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
5-470 |
1.33e-92 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 290.68 E-value: 1.33e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 5 SQFKRSYSLLpqgaqayIGGKWTasETGNSFDVLNPFN-NEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAI 83
Cdd:PRK03137 31 KELGQDYPLI-------IGGERI--TTEDKIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKW-SPEDRARI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 84 LHKWFEILVQRETELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRvYGQVVPsaVVNRLHLHTR---EPIGVVAL 160
Cdd:PRK03137 101 LLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLK-LADGKP--VESRPGEHNRyfyIPLGVGVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 161 IAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAI 240
Cdd:PRK03137 178 ISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGS---GSEVGDYLVDHPKTRFI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 241 SFTGSTPVGKLLLAQSAST------VKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHD 314
Cdd:PRK03137 255 TFTGSREVGLRIYERAAKVqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 315 QYISKlAAAMKEKLVLGDGLNPkTTQGPLVNQKAVDKceLLLSDALGKGS-ELICGGKRGEHGTSY-EPTLITNVQSNTN 392
Cdd:PRK03137 335 EVLEK-VVELTKELTVGNPEDN-AYMGPVINQASFDK--IMSYIEIGKEEgRLVLGGEGDDSKGYFiQPTIFADVDPKAR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 393 IAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGlisCAEA-----AFGGVK 467
Cdd:PRK03137 411 IMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRG---CTGAivgyhPFGGFN 487
|
...
gi 339730667 468 ESG 470
Cdd:PRK03137 488 MSG 490
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
31-491 |
4.04e-92 |
|
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: 288.04 E-value: 4.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 31 TGNSFDVLNPFNNEVVDRAtnctVKDAEKAvhsalegFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPL 110
Cdd:cd07098 5 TGQHLGSVPADTPEDVDEA----IAAARAA-------QREWAKT-SFAERRKVLRSLLKYILENQEEICRVACRDTGKTM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 111 AEAR-GEIQYSAAYFDWYAGEARRVygqVVPSAV-VNRLHLHTR-----EPIGVVALIAPWNFPTAMIARKAAAALSVGC 183
Cdd:cd07098 73 VDASlGEILVTCEKIRWTLKHGEKA---LRPESRpGGLLMFYKRarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 184 SAVVKPSGDTPLSA---LALAQTA-EEAGIPAGVFNVITAdhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSAST 259
Cdd:cd07098 150 AIVVKVSEQVAWSSgffLSIIREClAACGHDPDLVQLVTC----LPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAES 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 260 VKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDGLNPKTT 339
Cdd:cd07098 226 LTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQ-ALRQGPPLDGDVD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 340 QGPLVNQKAVDKCELLLSDALGKGSELICGGKRGEH-----GTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEV 414
Cdd:cd07098 305 VGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHpeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEA 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339730667 415 LEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLIS--CAEAAFGGVKESGIGREGGAQGIDEFTNWKYICT 491
Cdd:cd07098 385 VEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
38-484 |
2.59e-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: 277.59 E-value: 2.59e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 38 LNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGEI 117
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAV-PLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 118 QYSAAYFDWYAGEARRVygqVVPSAVVNRLHLH---TREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTP 194
Cdd:cd07102 80 RGMLERARYMISIAEEA---LADIRVPEKDGFEryiRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 195 LSALALAQTAEEAGIPAGVFNVITADHSNTAEiskyLCESTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLI 274
Cdd:cd07102 157 LCGERFAAAFAEAGLPEGVFQVLHLSHETSAA----LIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 275 VFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKEkLVLGDGLNPKTTQGPLVNQKAVDKCEL 354
Cdd:cd07102 233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKG-YKLGDPLDPSTTLGPVVSARAADFVRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 355 LLSDALGKGSELICGGKRG----EHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVF 430
Cdd:cd07102 312 QIADAIAKGARALIDGALFpedkAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVW 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 339730667 431 GRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFT 484
Cdd:cd07102 392 TKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLT 445
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
21-476 |
1.63e-85 |
|
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: 271.00 E-value: 1.63e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASetGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELAT 100
Cdd:cd07130 2 VYDGEWGGG--GGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDV-PAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 101 LLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALS 180
Cdd:cd07130 79 LVSLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 181 VGCSAVVKPSGDTPLSALA----LAQTAEEAGIPAGVFNVITADhsntAEISKYLCESTDVSAISFTGSTPVGKLLLAQS 256
Cdd:cd07130 159 CGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCGG----ADVGEALVKDPRVPLVSFTGSTAVGRQVGQAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 257 ASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMatkFRC---SGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGDG 333
Cdd:cd07130 235 AARFGRSLLELGGNNAIIVMEDADLDLAVRAVL---FAAvgtAGQRCTTTRRLIVHESIYDEVLERLKKAYK-QVRIGDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 334 LNPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKRGEHGTSY-EPTLITnVQSNTNIAHTEIFGPIASVQKFRDEQ 412
Cdd:cd07130 311 LDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYvEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLE 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339730667 413 EVLEAANNCRVGLAGYVFGRDQSRLQRV--ARKLEVGMVGVNEGlISCAE--AAFGGVKESGIGREGG 476
Cdd:cd07130 390 EAIAWNNEVPQGLSSSIFTTDLRNAFRWlgPKGSDCGIVNVNIG-TSGAEigGAFGGEKETGGGRESG 456
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
38-487 |
1.85e-83 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 265.57 E-value: 1.85e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 38 LNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGEI 117
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRET-NIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 118 QYSAAYFDWYAgEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSA 197
Cdd:PRK13968 91 AKSANLCDWYA-EHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 198 LALAQTAEEAGIPAGVFNVITADHSNTAEISKylceSTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFD 277
Cdd:PRK13968 170 QLIAQVFKDAGIPQGVYGWLNADNDGVSQMIN----DSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 278 DADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKEkLVLGDGLNPKTTQGPLVNQKAVDKCELLLS 357
Cdd:PRK13968 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAA-LKMGDPRDEENALGPMARFDLRDELHHQVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 358 DALGKGSELICGGKR--GEhGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQS 435
Cdd:PRK13968 325 ATLAEGARLLLGGEKiaGA-GNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDET 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 339730667 436 RLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTN----WK 487
Cdd:PRK13968 404 QARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNiqtvWK 459
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
38-487 |
1.19e-82 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 263.14 E-value: 1.19e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 38 LNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGEI 117
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTT-TFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 118 QYSAAYFDWYAGEARRVYG-QVVPSAVVNRLHLHTR-EPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPL 195
Cdd:PRK09406 85 LKCAKGFRYYAEHAEALLAdEPADAAAVGASRAYVRyQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 196 SALALAQTAEEAGIPAGVFNVITADHSNTAEISKylceSTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIV 275
Cdd:PRK09406 165 TALYLADLFRRAGFPDGCFQTLLVGSGAVEAILR----DPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 276 FDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKEkLVLGDGLNPKTTQGPLVNQKAVDKCELL 355
Cdd:PRK09406 241 MPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAA-LRVGDPTDPDTDVGPLATEQGRDEVEKQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 356 LSDALGKGSELICGGKRGEH-GTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQ 434
Cdd:PRK09406 320 VDDAVAAGATILCGGKRPDGpGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 339730667 435 SRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTNWK 487
Cdd:PRK09406 400 AEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIK 452
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
21-493 |
8.73e-82 |
|
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: 261.62 E-value: 8.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELAT 100
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKT-SVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 101 LLTKEQGKPLAEARG-EIQYSAAYFDWYAGEARRVYGQVvpSAV-VNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAA 178
Cdd:cd07116 83 AETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSI--SEIdENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 179 LSVGCSAVVKPSGDTPLSALALAQTAEEAgIPAGVFNVItadHSNTAEISKYLCESTDVSAISFTGSTPVGKLLLAQSAS 258
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVV---NGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 259 TVKRVCLELGGNAPLIVF------DDADLDVAVNGTMATKFRcSGQTCVSANRIYVHEKIHDQYIsKLAAAMKEKLVLGD 332
Cdd:cd07116 237 NIIPVTLELGGKSPNIFFadvmdaDDAFFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDRFM-ERALERVKAIKQGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 333 GLNPKTTQGPLVNQKAVDKceLLLSDALGK--GSELICGGKRGE-----HGTSYEPTLITNvQSNTNIAHTEIFGPIASV 405
Cdd:cd07116 315 PLDTETMIGAQASLEQLEK--ILSYIDIGKeeGAEVLTGGERNElggllGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 406 QKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAAFGGVKESGIGREGGAQGIDEFTN 485
Cdd:cd07116 392 TTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQ 471
|
....*...
gi 339730667 486 WKYICTQY 493
Cdd:cd07116 472 TKNLLVSY 479
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
21-476 |
2.86e-81 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 261.34 E-value: 2.86e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTasETGNSFDVLNPFN-NEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELA 99
Cdd:TIGR01237 36 VINGERV--ETENKIVSINPCDkSEVVGTVSKASQEHAEHALQAAAKAFEAWKKT-DPEERAAILFKAAAIVRRRRHEFS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 100 TLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAAL 179
Cdd:TIGR01237 113 ALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 180 SVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHSntaEISKYLCESTDVSAISFTGSTPVGKLLLAQSAST 259
Cdd:TIGR01237 193 VTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGS---EVGDYLVDHPKTSLITFTGSREVGTRIFERAAKV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 260 ------VKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAmKEKLVLGDG 333
Cdd:TIGR01237 270 qpgqkhLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEI-TESLKVGPP 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 334 LNPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKRGEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQE 413
Cdd:TIGR01237 349 DSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDE 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339730667 414 VLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEgliSCAEA-----AFGGVKESGIGREGG 476
Cdd:TIGR01237 429 ALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNR---NITGAivgyqPFGGFKMSGTDSKAG 493
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
36-489 |
2.13e-78 |
|
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: 252.34 E-value: 2.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 36 DVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTYSAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARG 115
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 116 EIQYSAAYFDWYAGEARRVYGQVVP----SAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSG 191
Cdd:cd07148 82 EVTRAIDGVELAADELGQLGGREIPmgltPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 192 DTPLSALALAQTAEEAGIPAGVFNVITADhSNTAEiskYLCESTDVSAISFTGSTPVGKLLLAQSASTVkRVCLELGGNA 271
Cdd:cd07148 162 ATPLSCLAFVDLLHEAGLPEGWCQAVPCE-NAVAE---KLVTDPRVAFFSFIGSARVGWMLRSKLAPGT-RCALEHGGAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 272 PLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLNPKTTQGPLVNQKAVDK 351
Cdd:cd07148 237 PVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAA-EKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 352 CELLLSDALGKGSELICGGKR-GEhgTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVF 430
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGKRlSD--TTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339730667 431 GRDQSRLQRVARKLEVGMVGVNEgliscaEAA-------FGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07148 394 TKDLDVALKAVRRLDATAVMVND------HTAfrvdwmpFAGRRQSGYGTGGIPYTMHDMTQEKMA 453
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
56-486 |
1.95e-67 |
|
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: 222.92 E-value: 1.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 56 DAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGE-------IQYSAAYFDWYA 128
Cdd:cd07095 1 QVDAAVAAARAAFPGWAAL-SLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEvaamagkIDISIKAYHERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 129 GEaRRVYGQVVPSAVVNRlhlhtrePIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAG 208
Cdd:cd07095 80 GE-RATPMAQGRAVLRHR-------PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 209 IPAGVFNVITADhsntAEISKYLCESTDVSAISFTGSTPVGKLLLAQSASTV-KRVCLELGGNAPLIVFDDADLDVAVNG 287
Cdd:cd07095 152 LPPGVLNLVQGG----RETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPgKILALEMGGNNPLVVWDVADIDAAAYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 288 TMATKFRCSGQTCVSANRIYVHEK-IHDQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVDKCELLLSDALGKGSEL 366
Cdd:cd07095 228 IVQSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAK-RLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 367 ICGGKRGEHGTSY-EPTLItNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLE 445
Cdd:cd07095 307 LLAMERLVAGTAFlSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIR 385
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 339730667 446 VGMVGVNEGLISCAEAA-FGGVKESGIGREGGAQGIDeFTNW 486
Cdd:cd07095 386 AGIVNWNRPTTGASSTApFGGVGLSGNHRPSAYYAAD-YCAY 426
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
73-491 |
2.99e-65 |
|
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: 217.01 E-value: 2.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 73 HTYSAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEA--------RGEIQYSAAYFDWYAgEARRVYgqvVP---- 140
Cdd:cd07087 15 KTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAylteiavvLGEIDHALKHLKKWM-KPRRVS---VPlllq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 141 --SAVVnrlhlhTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAgIPAGVFNVIT 218
Cdd:cd07087 91 paKAYV------IPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 219 ADhsntAEISKYLC-ESTDVsaISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSG 297
Cdd:cd07087 164 GG----VEVATALLaEPFDH--IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 298 QTCVSANRIYVHEKIHDQYISKLAAAMKEKLvlgdGLNPKTTQ--GPLVNQKAVDKCELLLSDalgkgSELICGGKRGEH 375
Cdd:cd07087 238 QTCIAPDYVLVHESIKDELIEELKKAIKEFY----GEDPKESPdyGRIINERHFDRLASLLDD-----GKVVIGGQVDKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 376 GTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGL 455
Cdd:cd07087 309 ERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVL 388
|
410 420 430
....*....|....*....|....*....|....*...
gi 339730667 456 ISCA--EAAFGGVKESGIGREGGAQGIDEFTNWKYICT 491
Cdd:cd07087 389 LHAAipNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
21-489 |
1.51e-64 |
|
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: 217.06 E-value: 1.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTasETGNSFDVLNPFN-NEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELA 99
Cdd:cd07083 22 VIGGEWV--DTKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDW-PQEDRARLLLKAADLLRRRRRELI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 100 TLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVV----PSAVVNRLHLhtrEPIGVVALIAPWNFPTAMIARKA 175
Cdd:cd07083 99 ATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVevvpYPGEDNESFY---VGLGAGVVISPWNFPVAIFTGMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 176 AAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGKLLLAQ 255
Cdd:cd07083 176 VAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGV---GEEVGAYLTEHERIRGINFTGSLETGKKIYEA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 256 SA------STVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLV 329
Cdd:cd07083 253 AArlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRA-ERLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 330 LGDGLNPKTTQGPLVNQKAVDKCELLLSDALGKGsELICGGKRGE-HGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKF 408
Cdd:cd07083 332 VGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEgEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 409 RDEQ--EVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISC--AEAAFGGVKESGIG-REGGAQGIDEF 483
Cdd:cd07083 411 KDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGAlvGVQPFGGFKLSGTNaKTGGPHYLRRF 490
|
....*.
gi 339730667 484 TNWKYI 489
Cdd:cd07083 491 LEMKAV 496
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
74-485 |
6.26e-64 |
|
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: 213.63 E-value: 6.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 74 TYSAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEAR--------GEIQYSAAYFD-WYAGeaRRVygqvvPSAVV 144
Cdd:cd07134 16 ASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlteilpvlSEINHAIKHLKkWMKP--KRV-----RTPLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 145 N---RLHLHTrEPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFnVITADh 221
Cdd:cd07134 89 LfgtKSKIRY-EPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEGD- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 222 sntAEISKYLCEsTDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCV 301
Cdd:cd07134 166 ---AEVAQALLE-LPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 302 SANRIYVHEKIHDQYISKLAAAMKEklVLGDGL----NPKTTQgpLVNQKAVDKCELLLSDALGKGSELICGGKRGEHGT 377
Cdd:cd07134 242 APDYVFVHESVKDAFVEHLKAEIEK--FYGKDAarkaSPDLAR--IVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 378 SYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLIS 457
Cdd:cd07134 318 YIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLH 397
|
410 420 430
....*....|....*....|....*....|
gi 339730667 458 CAEA--AFGGVKESGIGREGGAQGIDEFTN 485
Cdd:cd07134 398 FLNPnlPFGGVNNSGIGSYHGVYGFKAFSH 427
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
1-491 |
1.29e-62 |
|
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: 212.44 E-value: 1.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 1 MNRLSQFKRSYSLLPQGAQAYIGGKWTAS--------ETGNSFDVLNPFNNE-VVDRATNCTVKDAEKAVHSALEGFDKW 71
Cdd:cd07125 6 VNRIFDLEVPLEALADALKAFDEKEWEAIpiingeetETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 72 AHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVV---PSAVVNRLH 148
Cdd:cd07125 86 SAT-PVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPElpgPTGELNGLE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 149 LHTRepiGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHSntaEIS 228
Cdd:cd07125 165 LHGR---GVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGE---EIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 229 KYLCESTDVSAISFTGSTPVGKLLL-AQSASTVKRVCL--ELGG-NApLIVFDDADLDVAVNGTMATKFRCSGQTCvSAN 304
Cdd:cd07125 239 EALVAHPRIDGVIFTGSTETAKLINrALAERDGPILPLiaETGGkNA-MIVDSTALPEQAVKDVVQSAFGSAGQRC-SAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 305 RI-YVHEKIHDQYISKLAAAMKEkLVLGDGLNPKTTQGPLVNQKAVDKCELLlsDALGKGSE-LICGGKRGEH-GTSYEP 381
Cdd:cd07125 317 RLlYLQEEIAERFIEMLKGAMAS-LKVGDPWDLSTDVGPLIDKPAGKLLRAH--TELMRGEAwLIAPAPLDDGnGYFVAP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 382 TLITNVQSNTNiaHTEIFGPIASVQKFRDEQ--EVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLIsca 459
Cdd:cd07125 394 GIIEIVGIFDL--TTEVFGPILHVIRFKAEDldEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNIT--- 468
|
490 500 510
....*....|....*....|....*....|....*....
gi 339730667 460 eAA------FGGVKESGIGRE-GGAQGIDEFTNWKYICT 491
Cdd:cd07125 469 -GAivgrqpFGGWGLSGTGPKaGGPNYLLRFGNEKTVSL 506
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
21-487 |
2.83e-61 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 208.46 E-value: 2.83e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTYSAKqRGAILHKWFEILVQRETELAT 100
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWK-RAELLHKAAAILKEHKAPIAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 101 LLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQ-------VVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIAR 173
Cdd:PLN00412 98 CLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEgkflvsdSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 174 KAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHSntaEISKYLCESTDVSAISFTGSTPvgKLLL 253
Cdd:PLN00412 178 KIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGS---EIGDFLTMHPGVNCISFTGGDT--GIAI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 254 AQSASTVKrVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKeKLVLGdg 333
Cdd:PLN00412 253 SKKAGMVP-LQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVA-KLTVG-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 334 lNPK--TTQGPLVNQKAVDKCELLLSDALGKGSELICGGKRgeHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDE 411
Cdd:PLN00412 329 -PPEddCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR--EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 412 QEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEgliscAEA------AFGGVKESGIGREGGAQGIDEFTN 485
Cdd:PLN00412 406 EEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINS-----APArgpdhfPFQGLKDSGIGSQGITNSINMMTK 480
|
..
gi 339730667 486 WK 487
Cdd:PLN00412 481 VK 482
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
152-484 |
1.78e-60 |
|
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: 204.76 E-value: 1.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 152 REPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAgIPAGVFNVITADhsnTAEISKYL 231
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGG---VPETTALL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 232 CESTDvsAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEK 311
Cdd:cd07135 182 EQKFD--KIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 312 IHDQYISKLAAAMKEklVLGDGLNPKTTQGPLVNQKAVDKCELLLSDALGKgseLICGGKRGEHGTSYEPTLITNVQSNT 391
Cdd:cd07135 260 VYDEFVEELKKVLDE--FYPGGANASPDYTRIVNPRHFNRLKSLLDTTKGK---VVIGGEMDEATRFIPPTIVSDVSWDD 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 392 NIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLI--SCAEAAFGGVKES 469
Cdd:cd07135 335 SLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvGVDNAPFGGVGDS 414
|
330
....*....|....*
gi 339730667 470 GIGREGGAQGIDEFT 484
Cdd:cd07135 415 GYGAYHGKYGFDTFT 429
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
74-490 |
5.89e-58 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 199.48 E-value: 5.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 74 TYSAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEA--------RGEIQYSAAYFDWYAgeaRRVYgqvVPSAVVN 145
Cdd:PTZ00381 25 TRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETkmtevlltVAEIEHLLKHLDEYL---KPEK---VDTVGVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 146 RL---HLHtREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAgIPAGVFNVITADHS 222
Cdd:PTZ00381 99 GPgksYII-PEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 223 NTAEISKylcESTDVsaISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVS 302
Cdd:PTZ00381 177 VTTELLK---EPFDH--IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 303 ANRIYVHEKIHDQYISKLAAAMKEKLvlgdGLNPKTTQ--GPLVNQKAVDKCELLLSDalgKGSELICGGKRGEHGTSYE 380
Cdd:PTZ00381 252 PDYVLVHRSIKDKFIEALKEAIKEFF----GEDPKKSEdySRIVNEFHTKRLAELIKD---HGGKVVYGGEVDIENKYVA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 381 PTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAE 460
Cdd:PTZ00381 325 PTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLN 404
|
410 420 430
....*....|....*....|....*....|..
gi 339730667 461 AA--FGGVKESGIGREGGAQGIDEFTNWKYIC 490
Cdd:PTZ00381 405 PNlpFGGVGNSGMGAYHGKYGFDTFSHPKPVL 436
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
6-477 |
5.29e-56 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 194.67 E-value: 5.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 6 QFKRSYSLLPQGAQAYIGGKWTASetGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILH 85
Cdd:PLN02315 9 EFLSEIGLSSRNLGCYVGGEWRAN--GPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQV-PAPKRGEIVR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 86 KWFEILVQRETELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTREPIGVVALIAPWN 165
Cdd:PLN02315 86 QIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 166 FPTAMIARKAAAALSVGCSAVVKPSGDTPLSALAL----AQTAEEAGIPAGVFNVITADhsntAEISKYLCESTDVSAIS 241
Cdd:PLN02315 166 FPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCGG----AEIGEAIAKDTRIPLVS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 242 FTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLA 321
Cdd:PLN02315 242 FTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 322 AAMKEkLVLGDGLNPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKRGEHGTSY-EPTlITNVQSNTNIAHTEIFG 400
Cdd:PLN02315 322 TVYKQ-VKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFvQPT-IVEISPDADVVKEELFG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 401 PIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKL--EVGMVGVNEGlISCAE--AAFGGVKESGIGREGG 476
Cdd:PLN02315 400 PVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLgsDCGIVNVNIP-TNGAEigGAFGGEKATGGGREAG 478
|
.
gi 339730667 477 A 477
Cdd:PLN02315 479 S 479
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
21-470 |
1.00e-55 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 193.25 E-value: 1.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTASeTGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELAT 100
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARL-SFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 101 LLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSAVVNRLHLHTRePIGVVALIAPWNFPTAMIARKAAAALS 180
Cdd:PRK09457 82 VIARETGKPLWEAATEVTAMINKIAISIQAYHERTGEKRSEMADGAAVLRHR-PHGVVAVFGPYNFPGHLPNGHIVPALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 181 VGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsntAEISKYLCESTDVSAISFTGSTPVGKLLLAQSAS-T 259
Cdd:PRK09457 161 AGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGG----RETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGqP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 260 VKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIH-DQYISKLAAAMKeKLVLGD-GLNPK 337
Cdd:PRK09457 237 EKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAK-RLTVGRwDAEPQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 338 TTQGPLVNQKAVDKCELLLSDALGKGSELICGGKRGEHGTSY-EPTLI--TNVqsnTNIAHTEIFGPIASVQKFRDEQEV 414
Cdd:PRK09457 316 PFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLlTPGIIdvTGV---AELPDEEYFGPLLQVVRYDDFDEA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 339730667 415 LEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAA-FGGVKESG 470
Cdd:PRK09457 393 IRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASSAApFGGVGASG 449
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
14-493 |
5.34e-54 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 191.50 E-value: 5.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 14 LPQGAQAYIGGKWTASETGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGFDKWAHT-YSAKQRgaILHKWFEILV 92
Cdd:PLN02419 110 MPPRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTpITTRQR--VMLKFQELIR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 93 QRETELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVVPSaVVNRLHLHT-REPIGVVALIAPWNFPTAMI 171
Cdd:PLN02419 188 KNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPN-VSNGVDTYSiREPLGVCAGICPFNFPAMIP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 172 ARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVItadhSNTAEISKYLCESTDVSAISFTGSTPVGKL 251
Cdd:PLN02419 267 LWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIV----HGTNDTVNAICDDEDIRAVSFVGSNTAGMH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 252 LLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVS-ANRIYVHE-KIHDQYISKLAAAMKeklv 329
Cdd:PLN02419 343 IYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMAlSTVVFVGDaKSWEDKLVERAKALK---- 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 330 LGDGLNPKTTQGPLVNQKAVDKCELLLSDALGKGSELICGGKR-----GEHGTSYEPTLITNVQSNTNIAHTEIFGPIAS 404
Cdd:PLN02419 419 VTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLV 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 405 VQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGL-ISCAEAAFGGVKESGIGREG--GAQGID 481
Cdd:PLN02419 499 CMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIpVPLPFFSFTGNKASFAGDLNfyGKAGVD 578
|
490
....*....|..
gi 339730667 482 EFTNWKYICTQY 493
Cdd:PLN02419 579 FFTQIKLVTQKQ 590
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
152-489 |
7.25e-50 |
|
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: 176.54 E-value: 7.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 152 REPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAgIPAGVFNVITADhsntAEISKYL 231
Cdd:cd07136 98 YEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGG----VEENQEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 232 CEStDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEK 311
Cdd:cd07136 173 LDQ-KFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 312 IHDQYIsklaAAMKEKLVLGDGLNPKTTQ--GPLVNQKAVDKCELLLsdalgKGSELICGGKRGEHGTSYEPTLITNVQS 389
Cdd:cd07136 252 VKEKFI----KELKEEIKKFYGEDPLESPdyGRIINEKHFDRLAGLL-----DNGKIVFGGNTDRETLYIEPTILDNVTW 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 390 NTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCA--EAAFGGVK 467
Cdd:cd07136 323 DDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLAnpYLPFGGVG 402
|
330 340
....*....|....*....|..
gi 339730667 468 ESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07136 403 NSGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
151-487 |
4.04e-49 |
|
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: 174.21 E-value: 4.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 151 TREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAgIPAGVFNVITADhsntAEISKy 230
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTGG----ADVAA- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 231 lcestdvsAIS--------FTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVS 302
Cdd:cd07133 172 --------AFSslpfdhllFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 303 ANRIYVHEKIHDQYISKLAAAMKEklVLGDGL-NPKTTqgPLVNQKAVDKCELLLSDALGKGSELICGGKRGEHGTS--- 378
Cdd:cd07133 244 PDYVLVPEDKLEEFVAAAKAAVAK--MYPTLAdNPDYT--SIINERHYARLQGLLEDARAKGARVIELNPAGEDFAAtrk 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 379 YEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGL--I 456
Cdd:cd07133 320 LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLlhV 399
|
330 340 350
....*....|....*....|....*....|.
gi 339730667 457 SCAEAAFGGVKESGIGREGGAQGIDEFTNWK 487
Cdd:cd07133 400 AQDDLPFGGVGASGMGAYHGKEGFLTFSHAK 430
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
19-452 |
3.07e-47 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 175.77 E-value: 3.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 19 QAYIGGKWTA----SETGNSFDVLNPFNNE-VVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQ 93
Cdd:PRK11904 544 AAFLEKQWQAgpiiNGEGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPAWSRT-PVEERAAILERAADLLEA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 94 RETELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVV----PSAVVNRLHLHTRepiGVVALIAPWNFPTA 169
Cdd:PRK11904 623 NRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEklpgPTGESNELRLHGR---GVFVCISPWNFPLA 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 170 MIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVG 249
Cdd:PRK11904 700 IFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGD---GATVGAALTADPRIAGVAFTGSTETA 776
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 250 KLL---LAQSASTVkrVCL--ELGG-NApLIVFDDADLDVAVNGTMATKFRCSGQTCvSANRI-YVHEKIHDQYISKLAA 322
Cdd:PRK11904 777 RIInrtLAARDGPI--VPLiaETGGqNA-MIVDSTALPEQVVDDVVTSAFRSAGQRC-SALRVlFVQEDIADRVIEMLKG 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 323 AMKEkLVLGDGLNPKTTQGPLVNQKAVDKcelLLS--DALGKGSELICGGKRG---EHGTSYEPTL--ITNVQSNTNiah 395
Cdd:PRK11904 853 AMAE-LKVGDPRLLSTDVGPVIDAEAKAN---LDAhiERMKREARLLAQLPLPagtENGHFVAPTAfeIDSISQLER--- 925
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 339730667 396 tEIFGPIASVQKFRDEQ--EVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVN 452
Cdd:PRK11904 926 -EVFGPILHVIRYKASDldKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
74-489 |
7.96e-46 |
|
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: 165.28 E-value: 7.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 74 TYSAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEA-RGEIQY--SAAYF------DWYAGEARRVYGQVVPS--A 142
Cdd:cd07137 17 TRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVlvSSCKLaikelkKWMAPEKVKTPLTTFPAkaE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 143 VVNrlhlhtrEPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAgIPAGVFNVItadHS 222
Cdd:cd07137 97 IVS-------EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVI---EG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 223 NTAEISKYLCESTDvsAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRC-SGQTCV 301
Cdd:cd07137 166 GVPETTALLEQKWD--KIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 302 SANRIYVHEkihdQYISKLAAAMKEKLVLGDGLNPKTTQ--GPLVNQKAVDKCELLLSDAlGKGSELICGGKRGEHGTSY 379
Cdd:cd07137 244 APDYVLVEE----SFAPTLIDALKNTLEKFFGENPKESKdlSRIVNSHHFQRLSRLLDDP-SVADKIVHGGERDEKNLYI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 380 EPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLI--S 457
Cdd:cd07137 319 EPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVqyA 398
|
410 420 430
....*....|....*....|....*....|..
gi 339730667 458 CAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:cd07137 399 IDTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
20-470 |
3.85e-43 |
|
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: 160.06 E-value: 3.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 20 AYIGGKwtASETGNSFDVLNPFN-NEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILV---QRE 95
Cdd:cd07123 35 LVIGGK--EVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARM-PFEDRAAIFLKAADLLSgkyRYE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 96 TELATLLTkeQGKPLAEArgEIQySAA----YFDWYAGEARRVYGQ---VVPSAVVNRLHLHTREpiGVVALIAPWNFpT 168
Cdd:cd07123 112 LNAATMLG--QGKNVWQA--EID-AACelidFLRFNVKYAEELYAQqplSSPAGVWNRLEYRPLE--GFVYAVSPFNF-T 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 169 AMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPV 248
Cdd:cd07123 184 AIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGD---GPVVGDTVLASPHLAGLHFTGSTPT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 249 GKLLLAQSAS------TVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAA 322
Cdd:cd07123 261 FKSLWKQIGEnldryrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 323 AMKEkLVLGDGLNPKTTQGPLVNQKAVDKcellLSDALGK-----GSELICGGKrGEHGTSY--EPTLITNVQSNTNIAH 395
Cdd:cd07123 341 ELKE-IKMGDPDDFSNFMGAVIDEKAFDR----IKGYIDHaksdpEAEIIAGGK-CDDSVGYfvEPTVIETTDPKHKLMT 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 396 TEIFGPIASVQKFRDEQ--EVLEAANNC-RVGLAGYVFGRDQSRLQRVARKLE--VGMVGVNE---GLIsCAEAAFGGVK 467
Cdd:cd07123 415 EEIFGPVLTVYVYPDSDfeETLELVDTTsPYALTGAIFAQDRKAIREATDALRnaAGNFYINDkptGAV-VGQQPFGGAR 493
|
...
gi 339730667 468 ESG 470
Cdd:cd07123 494 ASG 496
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
18-488 |
1.53e-40 |
|
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: 152.37 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 18 AQAYIGGKWTASetGNSFDVLNPFN-NEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRET 96
Cdd:TIGR01238 38 AAPIIGHSYKAD--GEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNAT-PAKERAAKLDRLADLLELHMP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 97 ELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQvvpsavvnrlhlHTREPIGVVALIAPWNFPTAMIARKAA 176
Cdd:TIGR01238 115 ELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGE------------FSVESRGVFVCISPWNFPLAIFTGQIS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 177 AALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITAdhsNTAEISKYLCESTDVSAISFTGSTPVGKLL---L 253
Cdd:TIGR01238 183 AALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPG---RGADVGAALTSDPRIAGVAFTGSTEVAQLInqtL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 254 AQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIYVHEKIHDQYISKLAAAMKEkLVLGDG 333
Cdd:TIGR01238 260 AQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQE-LKVGVP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 334 LNPKTTQGPLVNQKAVDKCELLLSDALGKG---SELICGGKRG-EHGTSYEPTLITnvQSNTNIAHTEIFGPIASVQKFR 409
Cdd:TIGR01238 339 HLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDDSRAcQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 410 DEQ--EVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAA--FGGVKESGIG-REGGAQGIDEFT 484
Cdd:TIGR01238 417 AREldQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVqpFGGQGLSGTGpKAGGPHYLYRLT 496
|
....
gi 339730667 485 NWKY 488
Cdd:TIGR01238 497 QVQY 500
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
152-484 |
2.66e-40 |
|
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: 150.45 E-value: 2.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 152 REPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTaeeagIPAGV----FNVITADHSNTAEI 227
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLdkecYPVVLGGVEETTEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 228 skyLCESTDVsaISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCVSANRIY 307
Cdd:cd07132 173 ---LKQRFDY--IFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 308 VHEKIHDQYISKLAAAMKEKLvlgdGLNPKTTQ--GPLVNQKAVDKCELLLSdalgkGSELICGGkRGEHGTSY-EPTLI 384
Cdd:cd07132 248 CTPEVQEKFVEALKKTLKEFY----GEDPKESPdyGRIINDRHFQRLKKLLS-----GGKVAIGG-QTDEKERYiAPTVL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 385 TNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGL--ISCAEAA 462
Cdd:cd07132 318 TDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTImhYTLDSLP 397
|
330 340
....*....|....*....|..
gi 339730667 463 FGGVKESGIGREGGAQGIDEFT 484
Cdd:cd07132 398 FGGVGNSGMGAYHGKYSFDTFS 419
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
18-452 |
1.44e-39 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 153.17 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 18 AQAYIGGKwtaSETGNSFDVLNPFN-NEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRET 96
Cdd:COG4230 558 AAPLIAGE---AASGEARPVRNPADhSDVVGTVVEATAADVEAALAAAQAAFPAWSAT-PVEERAAILERAADLLEAHRA 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 97 ELATLLTKEQGKPLAEARGEIQ-------YsaayfdwYAGEARRVYGqvvpsavvnrlHLHTREPIGVVALIAPWNFPTA 169
Cdd:COG4230 634 ELMALLVREAGKTLPDAIAEVReavdfcrY-------YAAQARRLFA-----------APTVLRGRGVFVCISPWNFPLA 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 170 MIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVG 249
Cdd:COG4230 696 IFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGD---GETVGAALVADPRIAGVAFTGSTETA 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 250 KLL---LAQS--------ASTvkrvclelGG-NApLIVfdD--ADLDVAVNGTMATKFRCSGQTCvSANRI-YVHEKIHD 314
Cdd:COG4230 773 RLInrtLAARdgpivpliAET--------GGqNA-MIV--DssALPEQVVDDVLASAFDSAGQRC-SALRVlCVQEDIAD 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 315 QYISKLAAAMKEkLVLGDGLNPKTTQGPLVNQKAVDKcelLLS--DALGKGSELICGGKRGE---HGTSYEPTLITnVQS 389
Cdd:COG4230 841 RVLEMLKGAMAE-LRVGDPADLSTDVGPVIDAEARAN---LEAhiERMRAEGRLVHQLPLPEecaNGTFVAPTLIE-IDS 915
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 390 ntnIAH--TEIFGPIASVQKFRDEQ--EVLEAANNCRVGLAgyvFG---RDQSRLQRVARKLEVGMVGVN 452
Cdd:COG4230 916 ---ISDleREVFGPVLHVVRYKADEldKVIDAINATGYGLT---LGvhsRIDETIDRVAARARVGNVYVN 979
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
19-472 |
4.77e-39 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 151.56 E-value: 4.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 19 QAYIGGKWTA-------SETGNSFDVLNPFN-NEVVDRATNCTVKDAEKAVHSALEGFDKWAHTySAKQRGAILHKWFEI 90
Cdd:PRK11905 546 NAFAAKTWHAapllaggDVDGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFPEWSAT-PAAERAAILERAADL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 91 LVQRETELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGQVvpsavvnrlhlhTREPIGVVALIAPWNFPTAM 170
Cdd:PRK11905 625 MEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGP------------GHKPLGPVVCISPWNFPLAI 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 171 IARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADhsnTAEISKYLCESTDVSAISFTGSTPVGK 250
Cdd:PRK11905 693 FTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGD---GRTVGAALVADPRIAGVMFTGSTEVAR 769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 251 LLLAQSASTVKR-VCL--ELGG-NApLIVFDDADLDVAVNGTMATKFRCSGQTCvSANRI-YVHEKIHDQYISKLAAAMK 325
Cdd:PRK11905 770 LIQRTLAKRSGPpVPLiaETGGqNA-MIVDSSALPEQVVADVIASAFDSAGQRC-SALRVlCLQEDVADRVLTMLKGAMD 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 326 EkLVLGDGLNPKTTQGPLVNQKAVDK----CELLlsDALGKGSELICGGKRGEHGTSYEPTLItnvqSNTNIAH--TEIF 399
Cdd:PRK11905 848 E-LRIGDPWRLSTDVGPVIDAEAQANieahIEAM--RAAGRLVHQLPLPAETEKGTFVAPTLI----EIDSISDleREVF 920
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 400 GPIASVQKFRDEQ--EVLEAANNCRVGLagyVFG---RDQSRLQRVARKLEVGMVGVNEGLIscaeAA------FGGVKE 468
Cdd:PRK11905 921 GPVLHVVRFKADEldRVIDDINATGYGL---TFGlhsRIDETIAHVTSRIRAGNIYVNRNII----GAvvgvqpFGGEGL 993
|
....
gi 339730667 469 SGIG 472
Cdd:PRK11905 994 SGTG 997
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
74-489 |
2.18e-36 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 140.63 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 74 TYSAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEA-RGEI---QYSAAYF-----DWYAGEARRV-------YGQ 137
Cdd:PLN02203 24 TRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyRDEVgvlTKSANLAlsnlkKWMAPKKAKLplvafpaTAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 138 VVPsavvnrlhlhtrEPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTaeeagIP----AGV 213
Cdd:PLN02203 104 VVP------------EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAAN-----IPkyldSKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 214 FNVITADhsntAEISKYLCEStDVSAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIV--FDDA-DLDVAVNGTMA 290
Cdd:PLN02203 167 VKVIEGG----PAVGEQLLQH-KWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 291 TKF-RCSGQTCVSANRIYVHEKihdqYISKLAAAMKEKLVLGDGLNPKTTQG--PLVNQKAVDKCELLLSDALGKGSeLI 367
Cdd:PLN02203 242 GKWgSCAGQACIAIDYVLVEER----FAPILIELLKSTIKKFFGENPRESKSmaRILNKKHFQRLSNLLKDPRVAAS-IV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 368 CGGKRGEHGTSYEPTLITNVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVG 447
Cdd:PLN02203 317 HGGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSG 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 339730667 448 MVGVNEGLI--SCAEAAFGGVKESGIGREGGAQGIDEFTNWKYI 489
Cdd:PLN02203 397 SVTFNDAIIqyACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
153-489 |
3.58e-35 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 137.10 E-value: 3.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 153 EPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITAdhsnTAEISKYLC 232
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGA----VTETTALLE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 233 ESTDvsAISFTGSTPVGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRC-SGQTCVSANRIYVHEk 311
Cdd:PLN02174 187 QKWD--KIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYILTTK- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 312 ihdQYISKLAAAMKEKLVLGDGLNPKTTQ--GPLVNQKAVDKCELLLsDALGKGSELICGGKRGEHGTSYEPTLITNVQS 389
Cdd:PLN02174 264 ---EYAPKVIDAMKKELETFYGKNPMESKdmSRIVNSTHFDRLSKLL-DEKEVSDKIVYGGEKDRENLKIAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 390 NTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCA--EAAFGGVK 467
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTLPFGGVG 419
|
330 340
....*....|....*....|..
gi 339730667 468 ESGIGREGGAQGIDEFTNWKYI 489
Cdd:PLN02174 420 ESGMGAYHGKFSFDAFSHKKAV 441
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
18-476 |
6.61e-29 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 121.23 E-value: 6.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 18 AQAYIGGkwtASETGNSFDVLNPFN-NEVVDRATNCTVKDAEKAVHSALEGFDKWAHTYSAkQRGAILHKWFEILVQRET 96
Cdd:PRK11809 647 AAPMLED---PVAAGEMSPVINPADpRDIVGYVREATPAEVEQALESAVNAAPIWFATPPA-ERAAILERAADLMEAQMQ 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 97 ELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVYGqvvpsavvNRLHlhtrEPIGVVALIAPWNFPTAMIARKAA 176
Cdd:PRK11809 723 TLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFD--------NDTH----RPLGPVVCISPWNFPLAIFTGQVA 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 177 AALSVGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVF-----------NVITADHSntaeiskylcestdVSAISFTGS 245
Cdd:PRK11809 791 AALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVqllpgrgetvgAALVADAR--------------VRGVMFTGS 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 246 TPVGKLL---LAQSASTVKR---VCLELGGNAPLIVFDDADLDVAVNGTMATKFRCSGQTCvSANRIY-VHEKIHDQYIS 318
Cdd:PRK11809 857 TEVARLLqrnLAGRLDPQGRpipLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRC-SALRVLcLQDDVADRTLK 935
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 319 KLAAAMKEkLVLGdglNPK---TTQGPLVNQKAVDKCELLLSDALGKGSEL----ICGGKRGEHGTSYEPTLITnvQSNT 391
Cdd:PRK11809 936 MLRGAMAE-CRMG---NPDrlsTDIGPVIDAEAKANIERHIQAMRAKGRPVfqaaRENSEDWQSGTFVPPTLIE--LDSF 1009
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 392 NIAHTEIFGPIASVQKFRDEQ--EVLEAANNCRVGLAGYVFGRDQSRLQRVARKLEVGMVGVNEGLISCAEAA--FGGVK 467
Cdd:PRK11809 1010 DELKREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVqpFGGEG 1089
|
....*....
gi 339730667 468 ESGIGREGG 476
Cdd:PRK11809 1090 LSGTGPKAG 1098
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
72-446 |
1.65e-27 |
|
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: 114.64 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 72 AHTYSAKQRGAILHKWFEILVQRETELATLLTKEQGKP--LAE--ARGEIQYSAAYFDWYAGEARRVYGQVVPSAVVNRL 147
Cdd:cd07084 15 ARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGwmFAEniCGDQVQLRARAFVIYSYRIPHEPGNHLGQGLKQQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 148 HlHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGI-PAGVFNVITADHSNTAE 226
Cdd:cd07084 95 H-GYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLINGDGKTMQA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 227 iskyLCESTDVSAISFTGSTPVGKLLLAQSASTvkRVCLELGGNAPLIVFDDAD-LDVAVNGTMATKFRCSGQTCVSANR 305
Cdd:cd07084 174 ----LLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 306 IYVHE-----KIHDQYISKLAAAMKEKLVLGDGLNPkTTQGPLVNQKAVDKCELLLSdalgkGSELICGGKRGEHGTSYE 380
Cdd:cd07084 248 LFVPEnwsktPLVEKLKALLARRKLEDLLLGPVQTF-TTLAMIAHMENLLGSVLLFS-----GKELKNHSIPSIYGACVA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339730667 381 PTLITNVQSN--TNIAHT-EIFGPIASVQKFRDEQE--VLEAANNCRVGLAGYVFGRDQSRLQRVARKLEV 446
Cdd:cd07084 322 SALFVPIDEIlkTYELVTeEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPIFLQELIGNLWV 392
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
21-440 |
1.19e-22 |
|
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: 100.65 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 21 YIGGKWTasETGNSFDVLNPFN---------------NEVVDRATNCtvkdAEKAVHSALEGFDKWAhTYsakqrGAILH 85
Cdd:cd07126 2 LVAGKWK--GASNYTTLLDPLNgdkfisvpdtdedeiNEFVDSLRQC----PKSGLHNPLKNPERYL-LY-----GDVSH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 86 KWFEILVQRETE--LATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVY--GQVVPSAVVNRLHLHTREPIGVVALI 161
Cdd:cd07126 70 RVAHELRKPEVEdfFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLarSFNVPGDHQGQQSSGYRWPYGPVAII 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 162 APWNFPTAMIARKAAAALSVGCSAVVKpsGDTPLSALA--LAQTAEEAGIPAGVFNVItadHSNTAEISKYLCEStDVSA 239
Cdd:cd07126 150 TPFNFPLEIPALQLMGALFMGNKPLLK--VDSKVSVVMeqFLRLLHLCGMPATDVDLI---HSDGPTMNKILLEA-NPRM 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 240 ISFTGSTPVGklllaqsastvKRVCLELGGNaplIVFDDADLDVAVNGTMATKF------------RCSGQTCVSANRIY 307
Cdd:cd07126 224 TLFTGSSKVA-----------ERLALELHGK---VKLEDAGFDWKILGPDVSDVdyvawqcdqdayACSGQKCSAQSILF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 308 VHEKIHDQYISKLAAAMKEKLVLGDglnpkTTQGPLV---NQKAVDKCELLLsdALgKGSELICGGKRGEHGT------S 378
Cdd:cd07126 290 AHENWVQAGILDKLKALAEQRKLED-----LTIGPVLtwtTERILDHVDKLL--AI-PGAKVLFGGKPLTNHSipsiygA 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 379 YEPTLI------TNVQSNTNIAHTEIFGPIASVQKFRDEQE--VLEAANNCRVGLAGYVFGRDQSRLQRV 440
Cdd:cd07126 362 YEPTAVfvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEV 431
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
58-419 |
1.15e-18 |
|
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: 88.37 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 58 EKAVHSALEGFDKWAHTySAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARR--VY 135
Cdd:cd07129 2 DAAAAAAAAAFESYRAL-SPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgsWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 136 GQVVPSAVVNRLHL---HTRE---PIGVVALIAPWNFP---------TAMIarkaaaaLSVGCSAVVK--PS--GDTPLS 196
Cdd:cd07129 81 DARIDPADPDRQPLprpDLRRmlvPLGPVAVFGASNFPlafsvaggdTASA-------LAAGCPVVVKahPAhpGTSELV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 197 ALALAQTAEEAGIPAGVFNVItadHSNTAEISKYLCESTDVSAISFTGSTPVGKLL--LAQSASTVKRVCLELGGNAPLI 274
Cdd:cd07129 154 ARAIRAALRATGLPAGVFSLL---QGGGREVGVALVKHPAIKAVGFTGSRRGGRALfdAAAARPEPIPFYAELGSVNPVF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 275 VFDDAdldVAVNG-TMATKFRCS-----GQTCVSANRIYVHEKIH-DQYISKLAAAMKEK--LVLgdgLNPKTTQGplvN 345
Cdd:cd07129 231 ILPGA---LAERGeAIAQGFVGSltlgaGQFCTNPGLVLVPAGPAgDAFIAALAEALAAApaQTM---LTPGIAEA---Y 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339730667 346 QKAVDKcelLLSDAlgkGSELICGGKRGEHGTSYEPTLITnVQSNTNIA----HTEIFGPIASVQKFRDEQEVLEAAN 419
Cdd:cd07129 302 RQGVEA---LAAAP---GVRVLAGGAAAEGGNQAAPTLFK-VDAAAFLAdpalQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
19-448 |
2.45e-16 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 81.55 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 19 QAYIGGKWTASeTGNSFDVLNPFNNEVVDRATNCTVKDAEKAVHSALEGfdkwahtysakqrGAILHKWfeILVQRetel 98
Cdd:cd07128 2 QSYVAGQWHAG-TGDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKG-------------GPALRAL--TFHER---- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 99 ATLLtKEQGKPLAEARGEIqYSAAY----------FD---------WYAGEARR--VYGQVVPSAVVNRL---------H 148
Cdd:cd07128 62 AAML-KALAKYLMERKEDL-YALSAatgatrrdswIDidggigtlfAYASLGRRelPNAHFLVEGDVEPLskdgtfvgqH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 149 LHTrePIGVVAL-IAPWNFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGI-PAGVFNVITADhsnTAE 226
Cdd:cd07128 140 ILT--PRRGVAVhINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 227 ISKYLcESTDVsaISFTGSTPVGKLLLAQSASTVK--RVCLE--------LGgnaPLIVFDDADLDVAVNGT---MATKf 293
Cdd:cd07128 215 LLDHL-GEQDV--VAFTGSAATAAKLRAHPNIVARsiRFNAEadslnaaiLG---PDATPGTPEFDLFVKEVareMTVK- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 294 rcSGQTCVSANRIYVHEKIHDQYISKLAAAMkEKLVLGDGLNPKTTQGPLVNQK----AVDKCELLLSDAL----GKGSE 365
Cdd:cd07128 288 --AGQKCTAIRRAFVPEARVDAVIEALKARL-AKVVVGDPRLEGVRMGPLVSREqredVRAAVATLLAEAEvvfgGPDRF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 366 LICGGKRGEhGTSYEPTLIT--NVQSNTNIAHTEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSrlqrVARK 443
Cdd:cd07128 365 EVVGADAEK-GAFFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPA----FARE 439
|
....*
gi 339730667 444 LEVGM 448
Cdd:cd07128 440 LVLGA 444
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
19-441 |
5.60e-13 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 70.89 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 19 QAYIGGKWTASeTGNSFDVLNPFNNEVVDRaTNCTVKDAEKAVHSALE--GFDKWAHTYsaKQRGAILHKWFEILVQRET 96
Cdd:PRK11903 6 ANYVAGRWQAG-SGAGTPLFDPVTGEELVR-VSATGLDLAAAFAFAREqgGAALRALTY--AQRAALLAAIVKVLQANRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 97 ELATLLTKEQGKPLAEAR----GEIQYSAAYFDWYA--GEAR-RVYGQVV-----PSAVVNRLHLHTRepiGVVALIAPW 164
Cdd:PRK11903 82 AYYDIATANSGTTRNDSAvdidGGIFTLGYYAKLGAalGDARlLRDGEAVqlgkdPAFQGQHVLVPTR---GVALFINAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 165 NFPTAMIARKAAAALSVGCSAVVKPSGDTPLSALALAQTAEEAGI-PAGVFNVITAdhsNTAEISKYLcESTDVsaISFT 243
Cdd:PRK11903 159 NFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCG---SSAGLLDHL-QPFDV--VSFT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 244 GSTPVGKLLLAQSASTVK--RVCLELGG-NAPLIVFDDA------DLDVA-VNGTMATKfrcSGQTCVSANRIYVHEKIH 313
Cdd:PRK11903 233 GSAETAAVLRSHPAVVQRsvRVNVEADSlNSALLGPDAApgseafDLFVKeVVREMTVK---SGQKCTAIRRIFVPEALY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 314 DQYISKLAAAMKeKLVLGDGLNPKTTQGPLVNQKAVDKCELLLsDALGKGSELICGGKRGEH-------GTSYEPTLI-T 385
Cdd:PRK11903 310 DAVAEALAARLA-KTTVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGGFALvdadpavAACVGPTLLgA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 339730667 386 NVQSNTNIAH-TEIFGPIASVQKFRDEQEVLEAANNCRVGLAGYVFGRDQSRLQRVA 441
Cdd:PRK11903 388 SDPDAATAVHdVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAA 444
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
92-418 |
5.47e-07 |
|
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: 52.10 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 92 VQRETELATLLTKEQGKPLAEARG--EIQYSAAYFDWYAGEAR--RVYGQVVPSAVVNRLHLHTRepiGVVALIAPWNFP 167
Cdd:cd07127 130 VMHTTGQAFMMAFQAGGPHAQDRGleAVAYAWREMSRIPPTAEweKPQGKHDPLAMEKTFTVVPR---GVALVIGCSTFP 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 168 TAMIARKAAAALSVGCSAVVKPSgdtPLSALALAQTAE-------EAGIPAGVfnVITADHSNTAEISKYLCESTDVSAI 240
Cdd:cd07127 207 TWNGYPGLFASLATGNPVIVKPH---PAAILPLAITVQvarevlaEAGFDPNL--VTLAADTPEEPIAQTLATRPEVRII 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 241 SFTGSTPVGKLLlaQSASTVKRVCLELGGNAPLIVfDDADLDVAVNGTMATKFRC-SGQTCVSANRIYV---------HE 310
Cdd:cd07127 282 DFTGSNAFGDWL--EANARQAQVYTEKAGVNTVVV-DSTDDLKAMLRNLAFSLSLySGQMCTTPQNIYVprdgiqtddGR 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 311 KIHDQYISKLAAAMkEKLvLGDGLNPKTTQGPLVNQKAVDKcellLSDALGKGSELICGGKRG----EHGTSYEPTLITN 386
Cdd:cd07127 359 KSFDEVAADLAAAI-DGL-LADPARAAALLGAIQSPDTLAR----IAEARQLGEVLLASEAVAhpefPDARVRTPLLLKL 432
|
330 340 350
....*....|....*....|....*....|..
gi 339730667 387 VQSNTNIAHTEIFGPIASVQKFRDEQEVLEAA 418
Cdd:cd07127 433 DASDEAAYAEERFGPIAFVVATDSTDHSIELA 464
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
56-315 |
2.75e-06 |
|
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: 49.57 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 56 DAEKAVHSALEGFDkwahTYSAKQRGAILHKWFEILVQRETELATLLTKEQGKPLAEARGEIQYSAAYFDWYAGEARRVY 135
Cdd:cd07081 3 DAVAAAKVAQQGLS----CKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKDEKTC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 136 GqvVPSAVVNRLHLHTREPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKP----SGDTPLSALALAQTAEEAGIPA 211
Cdd:cd07081 79 G--VLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 212 gvfNVITADHSNTAEISKYLCESTDVSAISFTGstpvGKLLLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMAT 291
Cdd:cd07081 157 ---NLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKS 229
|
250 260
....*....|....*....|....
gi 339730667 292 KFRCSGQTCVSANRIYVHEKIHDQ 315
Cdd:cd07081 230 KTFDNGVICASEQSVIVVDSVYDE 253
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
153-323 |
1.05e-05 |
|
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: 47.60 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 153 EPIGVVALIAPWNFPTAMIARKAAAALSvGCSAVVKPSGDTPLSALALAQTAEEAGIPAGVFNVITADHSNTAEISKYLC 232
Cdd:cd07077 99 FPIGVTMHILPSTNPLSGITSALRGIAT-RNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILVLYVPHPSDELAEELL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 233 ESTDVSAISFTGSTPVGKllLAQSASTVKRVCLELGGNAPLIVFDDADLDVAVNGTMATKFRcSGQTCVSANRIYVHEKI 312
Cdd:cd07077 178 SHPKIDLIVATGGRDAVD--AAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFF-DQNACASEQNLYVVDDV 254
|
170
....*....|....*
gi 339730667 313 HD----QYISKLAAA 323
Cdd:cd07077 255 LDplyeEFKLKLVVE 269
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
153-466 |
1.01e-04 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, 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: 143440 [Multi-domain] Cd Length: 436 Bit Score: 44.79 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 153 EPIGVVALIAPWNFPTAMIARKAAAALSVGCSAVVKPS----GDTPLSALALAQTAEEAGIPAGVFNVITadhSNTAEIS 228
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHprakKCSIEAAKIMREAAVAAGAPEGLIQWIE---EPSIELT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 229 KYLCESTDVSAISFTGSTPVGKLllAQSASTVKrvcleLG---GNAPLIVFDDADLDVAVNGTMATK-FRCsGQTCVSAN 304
Cdd:cd07122 171 QELMKHPDVDLILATGGPGMVKA--AYSSGKPA-----IGvgpGNVPAYIDETADIKRAVKDIILSKtFDN-GTICASEQ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 305 RIYVHEKIHDQYISKLAAA------MKEKLVLGDGLNPKttqGPLVNQKAVDKCELLLSDALG----KGSELICGgkrge 374
Cdd:cd07122 243 SVIVDDEIYDEVRAELKRRgayflnEEEKEKLEKALFDD---GGTLNPDIVGKSAQKIAELAGievpEDTKVLVA----- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339730667 375 hgtsyeptLITNVQSNTNIAHtEIFGPIASVQKFRDEQEVLEAANNC-RVGLAGY---VFGRDQSRLQRVARKLEVGMVG 450
Cdd:cd07122 315 --------EETGVGPEEPLSR-EKLSPVLAFYRAEDFEEALEKARELlEYGGAGHtavIHSNDEEVIEEFALRMPVSRIL 385
|
330
....*....|....*.
gi 339730667 451 VNEGliscaeAAFGGV 466
Cdd:cd07122 386 VNTP------SSLGGI 395
|
|
| |
