|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
4-475 |
0e+00 |
|
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: 806.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 4 HQNLIAGEWV-GGDGVANINPSNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELG 82
Cdd:cd07097 1 YRNYIDGEWVaGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 83 RLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPAL 162
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 163 CYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRK 242
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 243 YQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPV 322
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 323 VDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVAND 402
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAND 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 803452457 403 TPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRKASSYGPREQGKYAAEFYTNVKTAYT 475
Cdd:cd07097 401 TEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHVPFGGRKGSSYGPREQGEAALEFYTTIKTVYV 473
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-474 |
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: 590.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 1 MTL--HQNLIAGEWV---GGDGVANINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEIL 75
Cdd:COG1012 1 MTTpeYPLFIGGEWVaaaSGETFDVINPA-TGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 76 ARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPA 155
Cdd:COG1012 80 ERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 156 WKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVA 235
Cdd:COG1012 160 WKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 236 SVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKP 315
Cdd:COG1012 240 AAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 316 GTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISrDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDE 395
Cdd:COG1012 320 GTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPD-GEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 803452457 396 ALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRKASSYGpREQGKYAAEFYTNVKTAY 474
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIG-REGGREGLEEYTETKTVT 476
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
12-472 |
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: 544.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 12 WVGGDG--VANINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREE 89
Cdd:pfam00171 1 WVDSESetIEVINPA-TGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 90 GKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSvRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVV 169
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 170 LKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGG 249
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 250 KNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLN 329
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 330 QDTDYIAIGKQEGAKLAFGGEVISRDtpGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSS 409
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDN--GYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 803452457 410 GIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRKASSYGpREQGKYAAEFYTNVKT 472
Cdd:pfam00171 397 GVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFG-REGGPYGLEEYTEVKT 458
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
6-474 |
8.02e-178 |
|
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: 506.89 E-value: 8.02e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 6 NLIAGEWVGGDGVA---NINPSNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELG 82
Cdd:cd07131 1 NYIGGEWVDSASGEtfdSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 83 RLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPAL 162
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 163 CYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRK 242
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 243 YQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPV 322
Cdd:cd07131 241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 323 VDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRD--TPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVA 400
Cdd:cd07131 321 INEAQLEKVLNYNEIGKEEGATLLLGGERLTGGgyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 803452457 401 NDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRKASSYGPREQGKYAAEFYTNVKTAY 474
Cdd:cd07131 401 NDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNGHREAGTTALDAFTEWKAVY 474
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
55-472 |
3.86e-172 |
|
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: 490.95 E-value: 3.86e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEIT 134
Cdd:cd07078 14 WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPDPGELAIVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 135 REPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDS 214
Cdd:cd07078 94 REPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALASH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 215 PDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHD 294
Cdd:cd07078 174 PRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 295 RFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDtPGFYLQPALFTEATNEMR 374
Cdd:cd07078 254 EFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGG-KGYFVPPTVLTDVDPDMP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 375 ISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRKASSY 454
Cdd:cd07078 333 IAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPSAPFGGVKQSGI 412
|
410
....*....|....*...
gi 803452457 455 GpREQGKYAAEFYTNVKT 472
Cdd:cd07078 413 G-REGGPYGLEEYTEPKT 429
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
21-472 |
1.30e-162 |
|
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: 467.29 E-value: 1.30e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 21 INPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGET 100
Cdd:cd07103 2 INPA-TGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 101 VRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCS 180
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 181 WAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDAD 260
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 261 LAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQ 340
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 341 EGAKLAFGGEVISRdtPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHAT 420
Cdd:cd07103 321 KGAKVLTGGKRLGL--GGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 803452457 421 HFKRNAEAGMVMVNLPTAGvDFHVPFGGRKASSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07103 399 RVAEALEAGMVGINTGLIS-DAEAPFGGVKESGLG-REGGKEGLEEYLETKY 448
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
6-474 |
5.50e-161 |
|
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: 464.34 E-value: 5.50e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 6 NLIAGEWVGGDG--VANINPSNTDDVVGEYArASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGR 83
Cdd:cd07086 1 GVIGGEWVGSGGetFTSRNPANGEPIARVFP-ASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 84 LLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALC 163
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 164 YGNTVVLKPAELVPGCSWAIVDILHRA----GLPKGVLNLVMGkGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEH 239
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 240 NRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHI 319
Cdd:cd07086 239 FGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 320 GPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAV 399
Cdd:cd07086 319 GPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAI 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 803452457 400 ANDTPFGLSSGIATTSLKHATHFKRNA--EAGMVMVNLPTAGVDFHVPFGGRKASSYGpREQGKYAAEFYTNVKTAY 474
Cdd:cd07086 399 NNDVPQGLSSSIFTEDLREAFRWLGPKgsDCGIVNVNIPTSGAEIGGAFGGEKETGGG-RESGSDAWKQYMRRSTCT 474
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
55-472 |
1.18e-148 |
|
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: 431.99 E-value: 1.18e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETV-RAGQIFEFFAGETLRLAGEVVPSVRPGIGVeI 133
Cdd:cd07093 35 WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIpRAAANFRFFADYILQLDGESYPQDGGALNY-V 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 134 TREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLD 213
Cdd:cd07093 114 LRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 214 SPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIH 293
Cdd:cd07093 194 HPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 294 DRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEV--ISRDTPGFYLQPALFTEATN 371
Cdd:cd07093 274 DEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGATILTGGGRpeLPDLEGGYFVEPTVITGLDN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 372 EMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGvDFHVPFGGRKA 451
Cdd:cd07093 354 DSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVR-DLRTPFGGVKA 432
|
410 420
....*....|....*....|.
gi 803452457 452 SSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07093 433 SGIG-REGGDYSLEFYTELKN 452
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
55-471 |
1.87e-146 |
|
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: 425.41 E-value: 1.87e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEIT 134
Cdd:cd07104 16 WAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILPSDVPGKESMVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 135 REPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCS-WAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLD 213
Cdd:cd07104 96 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKGVLNVVPGGGSEIGDALVE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 214 SPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIH 293
Cdd:cd07104 176 HPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 294 DRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVisrdtPGFYLQPALFTEATNEM 373
Cdd:cd07104 256 DEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY-----EGLFYQPTVLSDVTPDM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 374 RISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRKASS 453
Cdd:cd07104 331 PIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDEPHVPFGGVKASG 410
|
410
....*....|....*...
gi 803452457 454 YGpREQGKYAAEFYTNVK 471
Cdd:cd07104 411 GG-RFGGPASLEEFTEWQ 427
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
55-474 |
2.67e-143 |
|
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: 418.49 E-value: 2.67e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEIT 134
Cdd:cd07114 37 WRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 135 REPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDS 214
Cdd:cd07114 117 REPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 215 PDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHD 294
Cdd:cd07114 197 PLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 295 RFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTP--GFYLQPALFTEATNE 372
Cdd:cd07114 277 EFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGERPSGADLgaGYFFEPTILADVTND 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 373 MRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAgVDFHVPFGGRKAS 452
Cdd:cd07114 357 MRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYRA-LSPSSPFGGFKDS 435
|
410 420
....*....|....*....|..
gi 803452457 453 SYGpREQGKYAAEFYTNVKTAY 474
Cdd:cd07114 436 GIG-RENGIEAIREYTQTKSVW 456
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
55-472 |
4.10e-138 |
|
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: 405.45 E-value: 4.10e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVR-AGQIFEFFAGETLRLAGEVVPSVRPGIGVeI 133
Cdd:cd07112 42 WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAVDVPsAANTFRWYAEAIDKVYGEVAPTGPDALAL-I 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 134 TREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLD 213
Cdd:cd07112 121 TREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 214 SPDVQAITFTGSTATGKRVAVASVEHNRK-YQLEMGGKNPFVVLDDA-DLAVAVEAAVNSAFFSTGQRCTASSRIIVTEG 291
Cdd:cd07112 201 HMDVDALAFTGSTEVGRRFLEYSGQSNLKrVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHES 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 292 IHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTPGFYLQPALFTEATN 371
Cdd:cd07112 281 IKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKRVLTETGGFFVEPTVFDGVTP 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 372 EMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGvDFHVPFGGRKA 451
Cdd:cd07112 361 DMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEG-DITTPFGGFKQ 439
|
410 420
....*....|....*....|.
gi 803452457 452 SSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07112 440 SGNG-RDKSLHALDKYTELKT 459
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
55-475 |
4.62e-137 |
|
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: 403.23 E-value: 4.62e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVeIT 134
Cdd:cd07119 53 WPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISR-TV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 135 REPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDS 214
Cdd:cd07119 132 REPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAES 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 215 PDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHD 294
Cdd:cd07119 212 PDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHD 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 295 RFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRD--TPGFYLQPALFTEATNE 372
Cdd:cd07119 292 KFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelAKGYFVEPTIFDDVDRT 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 373 MRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlptagvDFHV-----PFG 447
Cdd:cd07119 372 MRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN------DYHPyfaeaPWG 445
|
410 420
....*....|....*....|....*...
gi 803452457 448 GRKASSYGpREQGKYAAEFYTNVKTAYT 475
Cdd:cd07119 446 GYKQSGIG-RELGPTGLEEYQETKHINI 472
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
7-452 |
1.94e-136 |
|
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: 402.76 E-value: 1.94e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 7 LIAGEWVGGDGVAN-INPSNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLL 85
Cdd:cd07124 36 VIGGKEVRTEEKIEsRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 86 SREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVrPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYG 165
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMV-PGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 166 NTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRV-AVASV-----EH 239
Cdd:cd07124 195 NTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIyERAAKvqpgqKW 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 240 NRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHI 319
Cdd:cd07124 275 LKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 320 GPVVDQSQLNQDTDYIAIGKQEGaKLAFGGEVISRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAV 399
Cdd:cd07124 355 GPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEI 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 803452457 400 ANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAG--VDFHvPFGGRKAS 452
Cdd:cd07124 434 ANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGalVGRQ-PFGGFKMS 487
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
7-474 |
2.85e-135 |
|
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: 398.51 E-value: 2.85e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 7 LIAGEWV---GGDGVANINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGI--LERHAILKKTADEILARKDEL 81
Cdd:cd07091 7 FINNEFVdsvSGKTFPTINPA-TEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMdpRERGRLLNKLADLIERDRDEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 82 GRLLSREEGKTLAEG----IGETVRAgqiFEFFAGETLRLAGEVVPSVRPGIGVEItREPAGVVGIITPWNFPIAIPAWK 157
Cdd:cd07091 86 AALESLDNGKPLEESakgdVALSIKC---LRYYAGWADKIQGKTIPIDGNFLAYTR-REPIGVCGQIIPWNFPLLMLAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 158 IAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASV 237
Cdd:cd07091 162 LAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 238 EHN-RKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPG 316
Cdd:cd07091 242 KSNlKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 317 THIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVIsrDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEA 396
Cdd:cd07091 322 TFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERH--GSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 397 LAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlptAGVDFH--VPFGGRKASSYGpREQGKYAAEFYTNVKTAY 474
Cdd:cd07091 400 IERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN---TYNVFDaaVPFGGFKQSGFG-RELGEEGLEEYTQVKAVT 475
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
22-471 |
3.62e-135 |
|
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: 397.47 E-value: 3.62e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 22 NPsNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETV 101
Cdd:cd07150 5 NP-ADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 102 RAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSW 181
Cdd:cd07150 84 FTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 182 AIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADL 261
Cdd:cd07150 164 KIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 262 AVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQE 341
Cdd:cd07150 244 DYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 342 GAKLAFGGEVisrdtPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATH 421
Cdd:cd07150 324 GAKLLTGGKY-----DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFK 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 803452457 422 FKRNAEAGMVMVNLPTAGVDFHVPFGGRKASSYGpREQGKYAAEFYTNVK 471
Cdd:cd07150 399 LAERLESGMVHINDPTILDEAHVPFGGVKASGFG-REGGEWSMEEFTELK 447
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
20-472 |
7.03e-135 |
|
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: 396.81 E-value: 7.03e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 20 NINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGE 99
Cdd:cd07115 1 TLNPA-TGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 100 TV-RAGQIFEFFAGETLRLAGEVVPsVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPG 178
Cdd:cd07115 80 DVpRAADTFRYYAGWADKIEGEVIP-VRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 179 CSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDD 258
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 259 ADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIG 338
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 339 KQEGAKLAFGGEviSRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKH 418
Cdd:cd07115 319 REEGARLLTGGK--RPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 803452457 419 ATHFKRNAEAGMVMVNLPTAgVDFHVPFGGRKASSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNR-FDPGSPFGGYKQSGFG-REMGREALDEYTEVKS 448
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
8-472 |
9.08e-134 |
|
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: 394.18 E-value: 9.08e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 8 IAGEWV---GGDGVANINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRL 84
Cdd:cd07138 3 IDGAWVapaGTETIDVINPA-TEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 85 LSREEG--KTLAEGIgeTVRAGQIFeffAGETLRLAGEVVPSVRPGiGVEITREPAGVVGIITPWNFPIAIPAWKIAPAL 162
Cdd:cd07138 82 ITLEMGapITLARAA--QVGLGIGH---LRAAADALKDFEFEERRG-NSLVVREPIGVCGLITPWNWPLNQIVLKVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 163 CYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRK 242
Cdd:cd07138 156 AAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 243 YQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPV 322
Cdd:cd07138 236 VALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 323 VDQSQLNQDTDYIAIGKQEGAKLAFGGEvisrDTP-----GFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEAL 397
Cdd:cd07138 316 ASAAQFDRVQGYIQKGIEEGARLVAGGP----GRPeglerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAI 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 803452457 398 AVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlpTAGVDFHVPFGGRKASSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07138 392 AIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN--GAAFNPGAPFGGYKQSGNG-REWGRYGLEEFLEVKS 463
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
5-471 |
1.74e-133 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 394.83 E-value: 1.74e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 5 QNLIAGEWVG---GDGVANINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDEL 81
Cdd:PLN02278 26 QGLIGGKWTDaydGKTFPVYNPA-TGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 82 GRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPA 161
Cdd:PLN02278 105 AQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 162 LCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNR 241
Cdd:PLN02278 185 LAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 242 KYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGP 321
Cdd:PLN02278 265 RVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 322 VVDQSQLNQDTDYIAIGKQEGAKLAFGGeviSRDTPG--FYlQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAV 399
Cdd:PLN02278 345 LINEAAVQKVESHVQDAVSKGAKVLLGG---KRHSLGgtFY-EPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAI 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 803452457 400 ANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVN---LPTAgvdfHVPFGGRKASSYGpREQGKYAAEFYTNVK 471
Cdd:PLN02278 421 ANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNeglISTE----VAPFGGVKQSGLG-REGSKYGIDEYLEIK 490
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
8-474 |
1.95e-133 |
|
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: 393.55 E-value: 1.95e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 8 IAGEWV---GGDGVANINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRL 84
Cdd:cd07088 2 INGEFVpssSGETIDVLNPA-TGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 85 LSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCY 164
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 165 GNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQ 244
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 245 LEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVD 324
Cdd:cd07088 241 LELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 325 QSQLNQDTDYIAIGKQEGAKLAFGGEVISRDtPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTP 404
Cdd:cd07088 321 EAALDKVEEMVERAVEAGATLLTGGKRPEGE-KGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 803452457 405 FGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGV--DFHvpfGGRKASSYGPrEQGKYAAEFYTNVKTAY 474
Cdd:cd07088 400 YGLTSYIYTENLNTAMRATNELEFGETYINRENFEAmqGFH---AGWKKSGLGG-ADGKHGLEEYLQTKVVY 467
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
5-472 |
1.52e-131 |
|
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: 389.18 E-value: 1.52e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 5 QNLIAGEWVGGDGVANI---NPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDEL 81
Cdd:cd07085 2 KLFINGEWVESKTTEWLdvyNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 82 GRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPA 161
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 162 LCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVgQAMLDSPDVQAITFTGSTATGKRVAVASVEHNR 241
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYERAAANGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 242 KYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGP 321
Cdd:cd07085 240 RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 322 VVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRD--TPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAV 399
Cdd:cd07085 320 VISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPgyENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 803452457 400 ANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPT-AGVDFHvPFGGRKASSYGPRE-QGKYAAEFYTNVKT 472
Cdd:cd07085 400 INANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIpVPLAFF-SFGGWKGSFFGDLHfYGKDGVRFYTQTKT 473
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
55-472 |
1.05e-130 |
|
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: 382.73 E-value: 1.05e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEIT 134
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGEAYVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 135 REPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDS 214
Cdd:cd06534 90 REPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLSH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 215 PDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHD 294
Cdd:cd06534 170 PRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 295 RFVaamgERIKGLVVDDalkpgthigpvvdqsqlnqdtdyiaigkqegaklafggevisrdtpgfylqpalfteaTNEMR 374
Cdd:cd06534 250 EFV----EKLVTVLVDV----------------------------------------------------------DPDMP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 375 ISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRKASSY 454
Cdd:cd06534 268 IAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFGGVKNSGI 347
|
410
....*....|....*...
gi 803452457 455 GpREQGKYAAEFYTNVKT 472
Cdd:cd06534 348 G-REGGPYGLEEYTRTKT 364
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
10-471 |
2.92e-130 |
|
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: 385.50 E-value: 2.92e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 10 GEWVGGDG---VANINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLS 86
Cdd:cd07151 1 GEWRDGTSertIDVLNPY-TGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 87 REEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGN 166
Cdd:cd07151 80 RESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 167 TVVLKPAELVPGCSWAIV-DILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQL 245
Cdd:cd07151 160 AVVLKPASDTPITGGLLLaKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 246 EMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQ 325
Cdd:cd07151 240 ELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 326 SQLNQDTDYIAIGKQEGAKLAFGGEVisrdtPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPF 405
Cdd:cd07151 320 SQVDGLLDKIEQAVEEGATLLVGGEA-----EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEY 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 803452457 406 GLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRKASSYGpREQGKYAAEFYTNVK 471
Cdd:cd07151 395 GLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLG-RFNGEWALEEFTTDK 459
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
55-472 |
4.18e-130 |
|
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: 384.77 E-value: 4.18e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEIT 134
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 135 REPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDS 214
Cdd:cd07118 117 REPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 215 PDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHD 294
Cdd:cd07118 197 PDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIAD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 295 RFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRdTPGFYLQPALFTEATNEMR 374
Cdd:cd07118 277 AFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLAS-AAGLFYQPTIFTDVTPDMA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 375 ISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDfHVPFGGRKASSY 454
Cdd:cd07118 356 IAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP-ELPFGGFKQSGI 434
|
410
....*....|....*...
gi 803452457 455 GpREQGKYAAEFYTNVKT 472
Cdd:cd07118 435 G-RELGRYGVEEYTELKT 451
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
7-472 |
5.97e-129 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 383.00 E-value: 5.97e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 7 LIAGEWV---GGDGVANINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGR 83
Cdd:TIGR02299 4 FIDGEFVpseSGETFETLSPA-TNEVLGSVARGGAADVDRAAKAAKEAFKRWAELKAAERKRYLHKIADLIEQHADEIAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 84 LLSREEGKTLAEGIGETVRAGQIFEFFAGE-TLRLAGEVVPSvrPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPAL 162
Cdd:TIGR02299 83 LECLDCGQPLRQTRQQVIRAAENFRFFADKcEEAMDGRTYPV--DTHLNYTVRVPVGPVGLITPWNAPFMLSTWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 163 CYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRK 242
Cdd:TIGR02299 161 AFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMRNGADTLKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 243 YQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPV 322
Cdd:TIGR02299 241 FSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPETEVGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 323 VDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTP-----GFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEAL 397
Cdd:TIGR02299 321 IHPEHLAKVLGYVEAAEKEGATILVGGERAPTFRGedlgrGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFKDEEEAI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 398 AVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVN------LPTagvdfhvPFGGRKASSYGpREQGKYAAEFYTNVK 471
Cdd:TIGR02299 401 EKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNsqnvrhLPT-------PFGGVKASGIG-REGGTYSFDFYTETK 472
|
.
gi 803452457 472 T 472
Cdd:TIGR02299 473 N 473
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
55-472 |
1.50e-128 |
|
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: 379.50 E-value: 1.50e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFA--GETLrLAGEVVPSvrPGIGVE 132
Cdd:cd07100 15 WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAenAEAF-LADEPIET--DAGKAY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 133 ITREPAGVVGIITPWNFPIaipaWKI----APALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVG 208
Cdd:cd07100 92 VRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 209 QaMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIV 288
Cdd:cd07100 168 A-IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 289 TEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVIsrDTPGFYLQPALFTE 368
Cdd:cd07100 247 HEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRP--DGPGAFYPPTVLTD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 369 ATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAgVDFHVPFGG 448
Cdd:cd07100 325 VTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVK-SDPRLPFGG 403
|
410 420
....*....|....*....|....
gi 803452457 449 RKASSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07100 404 VKRSGYG-RELGRFGIREFVNIKT 426
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
8-471 |
3.25e-124 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 369.91 E-value: 3.25e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 8 IAGEWV---GGDGVANINPSNtDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRL 84
Cdd:TIGR01804 2 IDGEYVedsAGTTREIINPAN-GEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 85 LSREEGKTLAEGI-GETVRAGQIFEFFAGETLRLAGEVVPSVRPGIgVEITREPAGVVGIITPWNFPIAIPAWKIAPALC 163
Cdd:TIGR01804 81 ETLDTGKTLQETIvADMDSGADVFEFFAGLAPALNGEIIPLGGPSF-AYTIREPLGVCVGIGAWNYPLQIASWKIAPALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 164 YGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKY 243
Cdd:TIGR01804 160 AGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 244 QLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVV 323
Cdd:TIGR01804 240 TMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 324 DQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTP--GFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVAN 401
Cdd:TIGR01804 320 SAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARAN 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 803452457 402 DTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlptagvDFH-----VPFGGRKASSYGpREQGKYAAEFYTNVK 471
Cdd:TIGR01804 400 DTEYGLAGGVFTADLGRAHRVADQLEAGTVWIN------TYNlypaeAPFGGYKQSGIG-RENGKAALAHYTEVK 467
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
21-471 |
7.81e-123 |
|
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: 365.91 E-value: 7.81e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 21 INPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGET 100
Cdd:cd07110 2 INPA-TEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 101 VRAGQIFEFFAGETLRL---AGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVP 177
Cdd:cd07110 81 DDVAGCFEYYADLAEQLdakAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 178 GCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLD 257
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 258 DADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAI 337
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 338 GKQEGAKLAFGGEVISRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLK 417
Cdd:cd07110 321 GKEEGARLLCGGRRPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 803452457 418 HATHFKRNAEAGMVMVNLPTAgVDFHVPFGGRKASSYGpREQGKYAAEFYTNVK 471
Cdd:cd07110 401 RCDRVAEALEAGIVWINCSQP-CFPQAPWGGYKRSGIG-RELGEWGLDNYLEVK 452
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
55-474 |
7.27e-122 |
|
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: 363.55 E-value: 7.27e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPsVRPGIGVEIT 134
Cdd:cd07090 35 WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLEYYAGLAPTLSGEHVP-LPGGSFAYTR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 135 REPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVvGQAMLDS 214
Cdd:cd07090 114 REPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 215 PDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHD 294
Cdd:cd07090 193 PDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 295 RFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTP---GFYLQPALFTEATN 371
Cdd:cd07090 273 EFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGAKVLCGGERVVPEDGlenGFYVSPCVLTDCTD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 372 EMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVN----LPTagvdfHVPFG 447
Cdd:cd07090 353 DMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINtyniSPV-----EVPFG 427
|
410 420
....*....|....*....|....*..
gi 803452457 448 GRKASSYGpREQGKYAAEFYTNVKTAY 474
Cdd:cd07090 428 GYKQSGFG-RENGTAALEHYTQLKTVY 453
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
8-474 |
3.90e-121 |
|
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: 362.28 E-value: 3.90e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 8 IAGEWV---GGDGVANINPSnTDDVVGEYARASAEDAKAAIAAAKAA--FPAWSRSGILERHAILKKTADEILARKDELG 82
Cdd:cd07139 3 IGGRWVapsGSETIDVVSPA-TEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 83 RLLSREEGKTLA-EGIGETVRAGQIFEFFAGETLRLA-GEVVPSVRPGIGVeITREPAGVVGIITPWNFPIAIPAWKIAP 160
Cdd:cd07139 82 RLWTAENGMPISwSRRAQGPGPAALLRYYAALARDFPfEERRPGSGGGHVL-VRREPVGVVAAIVPWNAPLFLAALKIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 161 ALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGkGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHN 240
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 241 RKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIG 320
Cdd:cd07139 240 ARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 321 PVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVA 400
Cdd:cd07139 320 PLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 803452457 401 NDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlpTAGVDFHVPFGGRKASSYGpREQGKYAAEFYTNVKTAY 474
Cdd:cd07139 400 NDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN--GFRLDFGAPFGGFKQSGIG-REGGPEGLDAYLETKSIY 470
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
21-472 |
4.51e-121 |
|
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: 361.68 E-value: 4.51e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 21 INPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTL-AEGIGE 99
Cdd:cd07108 2 INPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 100 TVRAGQIFEFFAGETLRLAGEVVPsVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGC 179
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 180 SWAIVDILHRAgLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDA 259
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 260 DLAVAVEAAVNSAFFS-TGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIG 338
Cdd:cd07108 239 DLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 339 KQE-GAKLAFGGE--VISRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTS 415
Cdd:cd07108 319 LSTsGATVLRGGPlpGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 803452457 416 LKHATHFKRNAEAGMVMVNlPTAGVDFHVPFGGRKASSYGPREQGKYAAEFYTNVKT 472
Cdd:cd07108 399 LGRALRAAHALEAGWVQVN-QGGGQQPGQSYGGFKQSGLGREASLEGMLEHFTQKKT 454
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
21-472 |
1.83e-120 |
|
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: 359.53 E-value: 1.83e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 21 INPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGET 100
Cdd:cd07106 2 INPA-TGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 101 VRAGQIFEFFAgeTLRLAGEVVPSVRPGIgVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCS 180
Cdd:cd07106 81 GGAVAWLRYTA--SLDLPDEVIEDDDTRR-VELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 181 WAIVDILHRAgLPKGVLNLVMGKGSVvGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDAD 260
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 261 LAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQ 340
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 341 EGAKLAFGGEVisRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHAT 420
Cdd:cd07106 316 KGAKVLAGGEP--LDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 803452457 421 HFKRNAEAGMVMVNLPtAGVDFHVPFGGRKASSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07106 394 AVARRLEAGTVWINTH-GALDPDAPFGGHKQSGIG-VEFGIEGLKEYTQTQV 443
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
62-472 |
1.96e-120 |
|
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: 359.99 E-value: 1.96e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 62 ERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVP-SVRPG----IGVEItRE 136
Cdd:cd07149 44 ERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEEAKRLAGETIPfDASPGgegrIGFTI-RE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 137 PAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPD 216
Cdd:cd07149 123 PIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 217 VQAITFTGSTATGKRVAVASVEhnRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRF 296
Cdd:cd07149 203 VRMISFTGSPAVGEAIARKAGL--KKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 297 VAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVIsrdtpGFYLQPALFTEATNEMRIS 376
Cdd:cd07149 281 LERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEEAVEGGARLLTGGKRD-----GAILEPTVLTDVPPDMKVV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 377 REEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVN-LPTAGVDfHVPFGGRKASSYG 455
Cdd:cd07149 356 CEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINdSSTFRVD-HMPYGGVKESGTG 434
|
410
....*....|....*..
gi 803452457 456 pREQGKYAAEFYTNVKT 472
Cdd:cd07149 435 -REGPRYAIEEMTEIKL 450
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
8-471 |
6.22e-119 |
|
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: 357.10 E-value: 6.22e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 8 IAGEWV---GGDGVANINPSNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRL 84
Cdd:cd07144 12 INNEFVkssDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGEERGELLDKLADLVEKNRDLLAAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 85 LSREEGKTL---AEG-IGETVragQIFEFFAGETLRLAGEVVPSVRPGIGVEItREPAGVVGIITPWNFPIAIPAWKIAP 160
Cdd:cd07144 92 EALDSGKPYhsnALGdLDEII---AVIRYYAGWADKIQGKTIPTSPNKLAYTL-HEPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 161 ALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHN 240
Cdd:cd07144 168 ALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 241 RKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIK-GLVVDDALKPGTHI 319
Cdd:cd07144 248 KAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 320 GPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVIS-RDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALA 398
Cdd:cd07144 328 GPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPeGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIK 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 803452457 399 VANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGvDFHVPFGGRKASSYGpREQGKYAAEFYTNVK 471
Cdd:cd07144 408 KANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDS-DVGVPFGGFKMSGIG-RELGEYGLETYTQTK 478
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
4-471 |
1.59e-117 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 353.06 E-value: 1.59e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 4 HQNLIAGEWVGGDGVAN--INPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDEL 81
Cdd:PRK13473 3 TKLLINGELVAGEGEKQpvYNPA-TGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 82 GRLLSREEGK----TLAEGIGETVragQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWK 157
Cdd:PRK13473 82 ARLESLNCGKplhlALNDEIPAIV---DVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 158 IAPALCYGNTVVLKPAELVPGCSWAIVDILHRAgLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASV 237
Cdd:PRK13473 159 LAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 238 EHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGT 317
Cdd:PRK13473 238 DSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 318 HIGPVVDQSQLNQDTDYIAIGKQEG-AKLAFGGEVISRdtPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEA 396
Cdd:PRK13473 318 ELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDG--KGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 803452457 397 LAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVN--LPTAGvdfHVPFGGRKASSYGpREQGKYAAEFYTNVK 471
Cdd:PRK13473 396 VRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNthFMLVS---EMPHGGQKQSGYG-KDMSLYGLEDYTVVR 468
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
4-472 |
3.41e-117 |
|
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: 352.42 E-value: 3.41e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 4 HQNLIAGEW---VGGDGVANINPSnTDDVVGEYA---RASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILAR 77
Cdd:cd07141 7 TKIFINNEWhdsVSGKTFPTINPA-TGEKICEVQegdKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLADLIERD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 78 KDELGRLLSREEGKTLAEG-IGETVRAGQIFEFFAGETLRLAGEVVPSvrPGIGVEITR-EPAGVVGIITPWNFPIAIPA 155
Cdd:cd07141 86 RAYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIPM--DGDFFTYTRhEPVGVCGQIIPWNFPLLMAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 156 WKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVA 235
Cdd:cd07141 164 WKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 236 SVEHN-RKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALK 314
Cdd:cd07141 244 AGKSNlKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 315 PGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEviSRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYD 394
Cdd:cd07141 324 PKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGK--RHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTID 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 803452457 395 EALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAgVDFHVPFGGRKASSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNV-VSPQAPFGGYKMSGNG-RELGEYGLQEYTEVKT 477
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
55-472 |
7.71e-117 |
|
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: 350.77 E-value: 7.71e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGiLERHAILKKTADEILARKDELGRLLSREEGKTLAegigeTVRAGQI------FEFFAGETLRLAGEVVPSVRPG 128
Cdd:cd07089 37 WSTDA-EERARCLRQLHEALEARKEELRALLVAEVGAPVM-----TARAMQVdgpighLRYFADLADSFPWEFDLPVPAL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 129 IGVE----ITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKG 204
Cdd:cd07089 111 RGGPgrrvVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 205 SVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASS 284
Cdd:cd07089 191 NAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 285 RIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTPGFYLQPA 364
Cdd:cd07089 271 RLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGRPAGLDKGFYVEPT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 365 LFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlPTAGVDFHV 444
Cdd:cd07089 351 LFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN-GGGGYGPDA 429
|
410 420
....*....|....*....|....*...
gi 803452457 445 PFGGRKASSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07089 430 PFGGYKQSGLG-RENGIEGLEEFLETKS 456
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
7-452 |
1.86e-116 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 351.54 E-value: 1.86e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 7 LIAGEWVGGDG-VANINPSNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLL 85
Cdd:PRK03137 40 IIGGERITTEDkIVSINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 86 SREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYG 165
Cdd:PRK03137 120 VKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 166 NTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVavasVEHNRKYQ- 244
Cdd:PRK03137 200 NTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRI----YERAAKVQp 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 245 ---------LEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKP 315
Cdd:PRK03137 276 gqiwlkrviAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 316 gTHIGPVVDQSQLNQDTDYIAIGKQEGaKLAFGGEviSRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDE 395
Cdd:PRK03137 356 -AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGE--GDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDH 431
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 803452457 396 ALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAG--VDFHvPFGGRKAS 452
Cdd:PRK03137 432 ALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGaiVGYH-PFGGFNMS 489
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
4-475 |
2.08e-116 |
|
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: 350.49 E-value: 2.08e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 4 HQNLIAGEWV---GGDGVANINPSNtDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDE 80
Cdd:cd07559 1 YDNFINGEWVapsKGEYFDNYNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 81 LGRLLSREEGKTLAEGIGETVR-AGQIFEFFAGETLRLAGEVVPSVRPGIGVEItREPAGVVGIITPWNFPIAIPAWKIA 159
Cdd:cd07559 80 LAVAETLDNGKPIRETLAADIPlAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHF-HEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 160 PALCYGNTVVLKPAELVPGCSWAIVDILHRAgLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEH 239
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 240 NRKYQLEMGGKNPFVVLDDA-----DLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALK 314
Cdd:cd07559 238 LIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 315 PGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGE--VISRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKD 392
Cdd:cd07559 318 PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGErlTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 393 YDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVN----LPTagvdfHVPFGGRKASSYGpREQGKYAAEFYT 468
Cdd:cd07559 398 EEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcyhqYPA-----HAPFGGYKKSGIG-RETHKMMLDHYQ 471
|
....*..
gi 803452457 469 NVKTAYT 475
Cdd:cd07559 472 QTKNILV 478
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
55-472 |
2.59e-116 |
|
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: 349.23 E-value: 2.59e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVrPGIGVEIT 134
Cdd:cd07109 36 WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAADKLHGETIPLG-PGYFVYTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 135 REPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDS 214
Cdd:cd07109 115 REPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 215 PDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHD 294
Cdd:cd07109 195 PGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 295 RFVAAMGERIKGLVVDDALKpGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTP-GFYLQPALFTEATNEM 373
Cdd:cd07109 275 EVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVARARARGARIVAGGRIAEGAPAgGYFVAPTLLDDVPPDS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 374 RISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRKASS 453
Cdd:cd07109 354 RLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGIELPFGGVKKSG 433
|
410
....*....|....*....
gi 803452457 454 YGpREQGKYAAEFYTNVKT 472
Cdd:cd07109 434 HG-REKGLEALYNYTQTKT 451
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
26-476 |
7.20e-116 |
|
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: 348.19 E-value: 7.20e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 26 TDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSgilERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQ 105
Cdd:cd07146 8 TGEVVGTVPAGTEEALREALALAASYRSTLTRY---QRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 106 IFEFFAGETLRLAGEVVPS-VRPGIGVEI---TREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSW 181
Cdd:cd07146 85 VLRFAAAEALRDDGESFSCdLTANGKARKiftLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 182 AIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVehNRKYQLEMGGKNPFVVLDDADL 261
Cdd:cd07146 165 YLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLIVMDDADL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 262 AVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQE 341
Cdd:cd07146 243 ERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 342 GAKLAFGGEvisRDtpGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATH 421
Cdd:cd07146 323 GARVLLGNQ---RQ--GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 803452457 422 FKRNAEAGMVMVNlptAGVDF---HVPFGGRKASSYGPREQGKYAAEFYTNVKTaYTL 476
Cdd:cd07146 398 LVERLDVGTVNVN---EVPGFrseLSPFGGVKDSGLGGKEGVREAMKEMTNVKT-YSL 451
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
21-472 |
1.66e-115 |
|
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: 347.41 E-value: 1.66e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 21 INPSNtDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGET 100
Cdd:cd07145 4 RNPAN-GEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 101 VRAGQIFEFFAGETLRLAGEVVPsVRPGIGVE-----ITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAEL 175
Cdd:cd07145 83 ERTIRLFKLAAEEAKVLRGETIP-VDAYEYNErriafTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 176 VPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVV 255
Cdd:cd07145 162 TPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 256 LDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYI 335
Cdd:cd07145 242 LKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 336 AIGKQEGAKLAFGGEVIsrdtPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTS 415
Cdd:cd07145 322 NDAVEKGGKILYGGKRD----EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTND 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 803452457 416 LKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRKASSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07145 398 INRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKSGIG-REGVRYTMLEMTEEKT 453
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
1-474 |
1.39e-114 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 346.10 E-value: 1.39e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 1 MTLHQNLIAGEWV---GGDGVANINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILAR 77
Cdd:PRK13252 4 QPLQSLYIDGAYVeatSGETFEVINPA-TGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 78 KDELGRLLSREEGKTLAEGIGETVRAG-QIFEFFAGETLRLAGEVVPsVRPGIGVEITREPAGVVGIITPWNFPIAIPAW 156
Cdd:PRK13252 83 NDELAALETLDTGKPIQETSVVDIVTGaDVLEYYAGLAPALEGEQIP-LRGGSFVYTRREPLGVCAGIGAWNYPIQIACW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 157 KIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVvGQAMLDSPDVQAITFTGSTATGKRVAVAS 236
Cdd:PRK13252 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 237 VEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPG 316
Cdd:PRK13252 241 AASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 317 THIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTP--GFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYD 394
Cdd:PRK13252 321 TNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFanGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDED 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 395 EALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlpTAGV-DFHVPFGGRKASSYGpREQGKYAAEFYTNVKTA 473
Cdd:PRK13252 401 EVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWIN--TWGEsPAEMPVGGYKQSGIG-RENGIATLEHYTQIKSV 477
|
.
gi 803452457 474 Y 474
Cdd:PRK13252 478 Q 478
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
55-475 |
5.44e-112 |
|
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: 339.08 E-value: 5.44e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEG-IGETVRAGQIFEFFAGETLRLAGEVVPSVRPgIGVEI 133
Cdd:cd07142 59 WPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGP-HHVYT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 134 TREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLD 213
Cdd:cd07142 138 LHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIAS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 214 SPDVQAITFTGSTATGKRVAVASVEHN-RKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGI 292
Cdd:cd07142 218 HMDVDKVAFTGSTEVGKIIMQLAAKSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 293 HDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISrdTPGFYLQPALFTEATNE 372
Cdd:cd07142 298 YDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIG--SKGYYIQPTIFSDVKDD 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 373 MRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLpTAGVDFHVPFGGRKAS 452
Cdd:cd07142 376 MKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNC-YDVFDASIPFGGYKMS 454
|
410 420
....*....|....*....|...
gi 803452457 453 SYGpREQGKYAAEFYTNVKTAYT 475
Cdd:cd07142 455 GIG-REKGIYALNNYLQVKAVVM 476
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
7-474 |
2.11e-110 |
|
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: 334.81 E-value: 2.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 7 LIAGEWV---GGDGVANINPSNtDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGR 83
Cdd:cd07117 4 FINGEWVkgsSGETIDSYNPAN-GETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 84 LLSREEGKTLAEGIGETV-RAGQIFEFFAGETLRLAGEVVPSVRPGIGVeITREPAGVVGIITPWNFPIAIPAWKIAPAL 162
Cdd:cd07117 83 VETLDNGKPIRETRAVDIpLAADHFRYFAGVIRAEEGSANMIDEDTLSI-VLREPIGVVGQIIPWNFPFLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 163 CYGNTVVLKPAELVPGCSWAIVDILHRAgLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRK 242
Cdd:cd07117 162 AAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 243 YQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPV 322
Cdd:cd07117 241 ATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 323 VDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRD--TPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVA 400
Cdd:cd07117 321 VNKDQLDKILSYVDIAKEEGAKILTGGHRLTENglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 803452457 401 NDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVN----LPTagvdfHVPFGGRKASSYGpREQGKYAAEFYTNVKTAY 474
Cdd:cd07117 401 NDSEYGLGGGVFTKDINRALRVARAVETGRVWVNtynqIPA-----GAPFGGYKKSGIG-RETHKSMLDAYTQMKNIY 472
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
21-471 |
2.23e-110 |
|
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: 333.91 E-value: 2.23e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 21 INPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGET 100
Cdd:cd07092 2 VDPA-TGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 101 V-RAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGC 179
Cdd:cd07092 81 LpGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 180 SWAIVDILHRaGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDA 259
Cdd:cd07092 161 TLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 260 DLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAiGK 339
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE-RA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 340 QEGAKLAFGGEviSRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHA 419
Cdd:cd07092 319 PAHARVLTGGR--RAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 803452457 420 THFKRNAEAGMVMVN--LPTAGvdfHVPFGGRKASSYGpREQGKYAAEFYTNVK 471
Cdd:cd07092 397 MRLSARLDFGTVWVNthIPLAA---EMPHGGFKQSGYG-KDLSIYALEDYTRIK 446
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
55-471 |
4.11e-110 |
|
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: 333.24 E-value: 4.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEIT 134
Cdd:TIGR01780 35 WRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEILYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 135 REPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMG-KGSVVGQAMLD 213
Cdd:TIGR01780 115 KQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSALALARLAEQAGIPKGVLNVITGsRAKEVGNVLTT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 214 SPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIH 293
Cdd:TIGR01780 195 SPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIY 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 294 DRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDtpGFYLQPALFTEATNEM 373
Cdd:TIGR01780 275 DEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAVEKGAKVVTGGKRHELG--GNFFEPTVLSNVTADM 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 374 RISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlpTAGVDFHV-PFGGRKAS 452
Cdd:TIGR01780 353 LVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWRVAEALEYGMVGIN--TGLISNVVaPFGGVKQS 430
|
410
....*....|....*....
gi 803452457 453 SYGpREQGKYAAEFYTNVK 471
Cdd:TIGR01780 431 GLG-REGSKYGIEEYLETK 448
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
7-466 |
2.74e-108 |
|
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: 330.67 E-value: 2.74e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 7 LIAGEWVGGDG-VANINPSNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLL 85
Cdd:TIGR01237 36 VINGERVETENkIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 86 SREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYG 165
Cdd:TIGR01237 116 VKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 166 NTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRV-AVASV-----EH 239
Cdd:TIGR01237 196 NCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIfERAAKvqpgqKH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 240 NRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHI 319
Cdd:TIGR01237 276 LKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 320 GPVVDQSQLNQDTDYIAIGKQEGaKLAFGGEviSRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAV 399
Cdd:TIGR01237 356 GPVIDQKSFNKIMEYIEIGKAEG-RLVSGGC--GDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEI 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 400 ANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAG--VDFHvPFGGRKASSYGPREQG-KYAAEF 466
Cdd:TIGR01237 433 ANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGaiVGYQ-PFGGFKMSGTDSKAGGpDYLALF 501
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
8-472 |
9.03e-107 |
|
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: 325.64 E-value: 9.03e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 8 IAGEWVggDGVAN-----INPSNtDDVVGEYARASAEDAKAAIAAAKAA-FPAWSRS-GILERHAILKKTADEILARKDE 80
Cdd:cd07143 11 INGEFV--DSVHGgtvkvYNPST-GKLITKIAEATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 81 LGRLLSREEGKT-LAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIgvEITR-EPAGVVGIITPWNFPIAIPAWKI 158
Cdd:cd07143 88 LASIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKL--TYTRhEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 159 APALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVE 238
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 239 HN-RKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGT 317
Cdd:cd07143 246 SNlKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 318 HIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEviSRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEAL 397
Cdd:cd07143 326 FQGPQVSQIQYERIMSYIESGKAEGATVETGGK--RHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 803452457 398 AVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAgVDFHVPFGGRKASSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07143 404 KRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNL-LHHQVPFGGYKQSGIG-RELGEYALENYTQIKA 476
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
21-455 |
5.67e-106 |
|
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: 322.63 E-value: 5.67e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 21 INPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGET 100
Cdd:cd07099 1 RNPA-TGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 101 VRAGQIFEFFAGETLR-LAGEVVP--SVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVP 177
Cdd:cd07099 80 LLALEAIDWAARNAPRvLAPRKVPtgLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 178 GCSWAIVDILHRAGLPKGVLNLVMGKGSVvGQAMLDSPdVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLD 257
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 258 DADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAI 337
Cdd:cd07099 238 DADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 338 GKQEGAKLAFGGEVIsrDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLK 417
Cdd:cd07099 318 AVAKGAKALTGGARS--NGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLA 395
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 803452457 418 HATHFKRNAEAGMVMVN--LPTAGVdFHVPFGGRKASSYG 455
Cdd:cd07099 396 RAEAIARRLEAGAVSINdvLLTAGI-PALPFGGVKDSGGG 434
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
55-472 |
9.16e-106 |
|
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: 322.07 E-value: 9.16e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPS-VRPGIGVE- 132
Cdd:cd07094 37 RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRLAAEEAERIRGEEIPLdATQGSDNRl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 133 --ITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQA 210
Cdd:cd07094 117 awTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 211 MLDSPDVQAITFTGSTATGKRVAVASveHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTE 290
Cdd:cd07094 197 FAADERVAMLSFTGSAAVGEALRANA--GGKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 291 GIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEvisRDtpGFYLQPALFTEAT 370
Cdd:cd07094 275 ELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEAGARLLCGGE---RD--GALFKPTVLEDVP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 371 NEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRK 450
Cdd:cd07094 350 RDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVK 429
|
410 420
....*....|....*....|..
gi 803452457 451 ASSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07094 430 ESGVG-REGVPYAMEEMTEEKT 450
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
5-475 |
3.24e-105 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 322.45 E-value: 3.24e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 5 QNLIAGEWVG---GDGVANINPSnTDDVVGEYARAS-----AEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILA 76
Cdd:PLN02467 9 QLFIGGEWREpvlGKRIPVVNPA-TEETIGDIPAATaedvdAAVEAARKAFKRNKGKDWARTTGAVRAKYLRAIAAKITE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 77 RKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGI---GVEITREPAGVVGIITPWNFPIAI 153
Cdd:PLN02467 88 RKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMetfKGYVLKEPLGVVGLITPWNYPLLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 154 PAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVA 233
Cdd:PLN02467 168 ATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 234 VASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDAL 313
Cdd:PLN02467 248 TAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 314 KPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDY 393
Cdd:PLN02467 328 EEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 394 DEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNL--PTagvdF-HVPFGGRKASSYGpREQGKYAAEFYTNV 470
Cdd:PLN02467 408 DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCsqPC----FcQAPWGGIKRSGFG-RELGEWGLENYLSV 482
|
....*..
gi 803452457 471 K--TAYT 475
Cdd:PLN02467 483 KqvTKYI 489
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
55-475 |
1.22e-104 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 321.00 E-value: 1.22e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEG-IGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEI 133
Cdd:PLN02766 76 WPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGkAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 134 tREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLD 213
Cdd:PLN02766 156 -KEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIAS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 214 SPDVQAITFTGSTATGKRVAVASVEHN-RKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGI 292
Cdd:PLN02766 235 HMDVDKVSFTGSTEVGRKIMQAAATSNlKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 293 HDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDtpGFYLQPALFTEATNE 372
Cdd:PLN02766 315 YDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDK--GYYIEPTIFTDVTED 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 373 MRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLpTAGVDFHVPFGGRKAS 452
Cdd:PLN02766 393 MKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNC-YFAFDPDCPFGGYKMS 471
|
410 420
....*....|....*....|...
gi 803452457 453 SYGpREQGKYAAEFYTNVKTAYT 475
Cdd:PLN02766 472 GFG-RDQGMDALDKYLQVKSVVT 493
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
8-472 |
5.25e-104 |
|
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: 318.62 E-value: 5.25e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 8 IAGEWVGGDG---VANINPSnTDDVVGEYARASAEDAKAAIAAAKAA-FPAWSRSGILERHAILKKTADEILARKDELGR 83
Cdd:cd07113 4 IDGRPVAGQSekrLDITNPA-TEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 84 LLSREEGKTLAEGIGETVRAGQIF-EFFAGETLRLAGEVVPSVRPGIGVE-----ITREPAGVVGIITPWNFPIAIPAWK 157
Cdd:cd07113 83 LETLCSGKSIHLSRAFEVGQSANFlRYFAGWATKINGETLAPSIPSMQGErytafTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 158 IAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVvGQAMLDSPDVQAITFTGSTATGKRVAVASV 237
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 238 EHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGT 317
Cdd:cd07113 242 SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 318 HIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRdtPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEAL 397
Cdd:cd07113 322 MFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAG--EGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 803452457 398 AVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAgVDFHVPFGGRKASSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07113 400 QLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTF-LDPAVPFGGMKQSGIG-REFGSAFIDDYTELKS 472
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
55-472 |
7.48e-104 |
|
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: 316.44 E-value: 7.48e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTlAEGIGETVR-AGQIFEFFAGETLRLAGEVVPSVRPGIGVEI 133
Cdd:cd07105 16 WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT-AAWAGFNVDlAAGMLREAASLITQIIGGSIPSDKPGTLAMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 134 TREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGK---GSVVGQA 210
Cdd:cd07105 95 VKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSpedAPEVVEA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 211 MLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTE 290
Cdd:cd07105 175 LIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 291 GIHDRFVAAMGERIKGLVVDDalkpgTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGeVISRDTPGFYLQPALFTEAT 370
Cdd:cd07105 255 SIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGG-LADESPSGTSMPPTILDNVT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 371 NEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRK 450
Cdd:cd07105 329 PDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDEPTLPHGGVK 408
|
410 420
....*....|....*....|..
gi 803452457 451 ASSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07105 409 SSGYG-RFNGKWGIDEFTETKW 429
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
4-472 |
1.11e-102 |
|
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: 314.89 E-value: 1.11e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 4 HQNLIAGEWVGGDG--VANINPSNtDDVVGEYARASAEDAKAAIAAAKAAFPAWSR-SGILERHAILKKTADEILARKDE 80
Cdd:cd07082 2 FKYLINGEWKESSGktIEVYSPID-GEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 81 LGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPS-----VRPGIGVeITREPAGVVGIITPWNFPIAIPA 155
Cdd:cd07082 81 VANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGdwfpgTKGKIAQ-VRREPLGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 156 WKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVA 235
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 236 sveHNRK-YQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALK 314
Cdd:cd07082 240 ---HPMKrLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 315 PGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEvisRDTPGfYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYD 394
Cdd:cd07082 317 NGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGG---REGGN-LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 803452457 395 EALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTA-GVDfHVPFGGRKASSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07082 393 EAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrGPD-HFPFLGRKDSGIG-TQGIGDALRSMTRRKG 469
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
55-468 |
4.54e-102 |
|
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: 312.31 E-value: 4.54e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVrPGIGVEIT 134
Cdd:cd07152 29 WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQPQGEILPSA-PGRLSLAR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 135 REPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCS-WAIVDILHRAGLPKGVLNLVMGkGSVVGQAMLD 213
Cdd:cd07152 108 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVLPG-GADAGEALVE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 214 SPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIH 293
Cdd:cd07152 187 DPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 294 DRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEvisRDtpGFYLQPALFTEATNEM 373
Cdd:cd07152 267 DAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGT---YD--GLFYRPTVLSGVKPGM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 374 RISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRKASS 453
Cdd:cd07152 342 PAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDEPHNPFGGMGASG 421
|
410
....*....|....*
gi 803452457 454 YGPREQGKYAAEFYT 468
Cdd:cd07152 422 NGSRFGGPANWEEFT 436
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
55-475 |
3.23e-101 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 313.28 E-value: 3.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIG-ETVRAGQIFEFFAGETLRLAGEVVPSVRPGiGVEI 133
Cdd:PLN02466 113 WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPADGPH-HVQT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 134 TREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLD 213
Cdd:PLN02466 192 LHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALAS 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 214 SPDVQAITFTGSTATGKRVAVASVEHNRK-YQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGI 292
Cdd:PLN02466 272 HMDVDKLAFTGSTDTGKIVLELAAKSNLKpVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERV 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 293 HDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISrdTPGFYLQPALFTEATNE 372
Cdd:PLN02466 352 YDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFG--SKGYYIQPTVFSNVQDD 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 373 MRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAgVDFHVPFGGRKAS 452
Cdd:PLN02466 430 MLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDV-FDAAIPFGGYKMS 508
|
410 420
....*....|....*....|...
gi 803452457 453 SYGpREQGKYAAEFYTNVKTAYT 475
Cdd:PLN02466 509 GIG-REKGIYSLNNYLQVKAVVT 530
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
4-472 |
1.12e-99 |
|
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: 307.88 E-value: 1.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 4 HQNLIAGEWV---GGDGVANINPSNtDDVVGE--YARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARK 78
Cdd:cd07140 6 HQLFINGEFVdaeGGKTYNTINPTD-GSVICKvsLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 79 DELGRLLSREEGK--TLA--EGIGETVragQIFEFFAGETLRLAGEVVP--SVRPGIGVEIT-REPAGVVGIITPWNFPI 151
Cdd:cd07140 85 EELATIESLDSGAvyTLAlkTHVGMSI---QTFRYFAGWCDKIQGKTIPinQARPNRNLTLTkREPIGVCGIVIPWNYPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 152 AIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKR 231
Cdd:cd07140 162 MMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 232 VAVASVEHN-RKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVD 310
Cdd:cd07140 242 IMKSCAVSNlKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 311 DALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRdtPGFYLQPALFTEATNEMRISREEIFGPVAAVIRV 390
Cdd:cd07140 322 DPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDR--PGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 391 K--DYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAgVDFHVPFGGRKASSYGpREQGKYAAEFYT 468
Cdd:cd07140 400 DdgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNK-TDVAAPFGGFKQSGFG-KDLGEEALNEYL 477
|
....
gi 803452457 469 NVKT 472
Cdd:cd07140 478 KTKT 481
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
21-472 |
3.62e-99 |
|
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: 305.45 E-value: 3.62e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 21 INPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGET 100
Cdd:cd07107 2 INPA-TGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 101 VRAGQIFEFFAGETLRLAGEVVPSvrPGIGVEIT-REPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGC 179
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPV--GGRNLHYTlREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 180 SWAIVDILhRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDA 259
Cdd:cd07107 159 ALRLAELA-REVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 260 DLAVAVEAAVNSAFFS-TGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIG 338
Cdd:cd07107 238 DPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 339 KQEGAKLAFGGEVISRDTP--GFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSL 416
Cdd:cd07107 318 KREGARLVTGGGRPEGPALegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 803452457 417 KHATHFKRNAEAGMVMVNlptaGVDFH---VPFGGRKASSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07107 398 SQAHRTARRVEAGYVWIN----GSSRHflgAPFGGVKNSGIG-REECLEELLSYTQEKN 451
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
4-471 |
8.53e-99 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 305.29 E-value: 8.53e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 4 HQNLIAGEWV---GGDGVANINPSNtDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDE 80
Cdd:PRK11241 11 QQALINGEWLdanNGEVIDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 81 LGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAP 160
Cdd:PRK11241 90 LARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 161 ALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHN 240
Cdd:PRK11241 170 ALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 241 RKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIG 320
Cdd:PRK11241 250 KKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 321 PVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDtpGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVA 400
Cdd:PRK11241 330 PLIDEKAVAKVEEHIADALEKGARVVCGGKAHELG--GNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQA 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 803452457 401 NDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlpTAGVDFHV-PFGGRKASSYGpREQGKYAAEFYTNVK 471
Cdd:PRK11241 408 NDTEFGLAAYFYARDLSRVFRVGEALEYGIVGIN--TGIISNEVaPFGGIKASGLG-REGSKYGIEDYLEIK 476
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
9-460 |
6.01e-98 |
|
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: 302.97 E-value: 6.01e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 9 AGEWVGGDG-VANINPSNtDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSR 87
Cdd:cd07130 4 DGEWGGGGGvVTSISPAN-GEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 88 EEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNT 167
Cdd:cd07130 83 EMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 168 VVLKPAELVPGCSWA----IVDILHRAGLPKGVLNLVMGkGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKY 243
Cdd:cd07130 163 VVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 244 QLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVV 323
Cdd:cd07130 242 LLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 324 DQSQLNQDTDYIAIGKQEGAKLAFGGEVISRdtPGFYLQPALfTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDT 403
Cdd:cd07130 322 TKAAVDNYLAAIEEAKSQGGTVLFGGKVIDG--PGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEV 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 803452457 404 PFGLSSGIATTSLKHATHF--KRNAEAGMVMVNLPTAGVDFHVPFGGRKASSYGpREQG 460
Cdd:cd07130 399 PQGLSSSIFTTDLRNAFRWlgPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGG-RESG 456
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
21-474 |
4.91e-97 |
|
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: 300.03 E-value: 4.91e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 21 INPSnTDDVVGEYARASAEDAKAAIAAAKA--AFPAWSRSGILeRHAILKKTADEILARKDELGRLLSREEGKTLAEGIG 98
Cdd:cd07120 2 IDPA-TGEVIGTYADGGVAEAEAAIAAARRafDETDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 99 ETVRAGQIFEFFAGETLRLAGEVVpSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPG 178
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMI-EPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 179 CSWAIVDILHRA-GLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLD 257
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 258 DADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAI 337
Cdd:cd07120 239 DADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVER 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 338 GKQEGAK-LAFGGEVISRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSL 416
Cdd:cd07120 319 AIAAGAEvVLRGGPVTEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 803452457 417 KHATHFKRNAEAGMVMVNlpTAGVDF-HVPFGGRKASSYGpREQGKYAAEFYTNVKTAY 474
Cdd:cd07120 399 ARAMRVARAIRAGTVWIN--DWNKLFaEAEEGGYRQSGLG-RLHGVAALEDFIEYKHIY 454
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
21-455 |
3.36e-94 |
|
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: 292.23 E-value: 3.36e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 21 INPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGET 100
Cdd:cd07102 1 ISPI-DGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 101 VRAGQIFEFFagetLRLAGEVVPSVR----PGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELV 176
Cdd:cd07102 80 RGMLERARYM----ISIAEEALADIRvpekDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 177 PGCSWAIVDILHRAGLPKGVLNLVMGKGSVvGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVL 256
Cdd:cd07102 156 PLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 257 DDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIA 336
Cdd:cd07102 235 PDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 337 IGKQEGAKLAFGGEVISRDTPG-FYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTS 415
Cdd:cd07102 315 DAIAKGARALIDGALFPEDKAGgAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKD 394
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 803452457 416 LKHATHFKRNAEAGMVMVNlPTAGVDFHVPFGGRKASSYG 455
Cdd:cd07102 395 IARAEALGEQLETGTVFMN-RCDYLDPALAWTGVKDSGRG 433
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
67-474 |
3.00e-93 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 288.56 E-value: 3.00e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 67 LKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITP 146
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 147 WNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGST 226
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 227 ATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKG 306
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 307 LVVDDALKPGT-HIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDtpGFYLQPALFTEATNEMRISREEIFGPVA 385
Cdd:PRK10090 241 VQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGK--GYYYPPTLLLDVRQEMSIMHEETFGPVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 386 AVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPT--AGVDFHVpfGGRKASSYGPreQGKYA 463
Cdd:PRK10090 319 PVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENfeAMQGFHA--GWRKSGIGGA--DGKHG 394
|
410
....*....|.
gi 803452457 464 AEFYTNVKTAY 474
Cdd:PRK10090 395 LHEYLQTQVVY 405
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
55-466 |
1.00e-92 |
|
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: 288.02 E-value: 1.00e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGE-TVRAGQIfeffaGETLRLAGEVVPSVR-PGIGVE 132
Cdd:cd07095 16 WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEvAAMAGKI-----DISIKAYHERTGERAtPMAQGR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 133 --ITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGkGSVVGQA 210
Cdd:cd07095 91 avLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG-GRETGEA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 211 MLDSPDVQAITFTGSTATGKRVAVASVEHNRK-YQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVT 289
Cdd:cd07095 170 LAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 290 EG-IHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQsqlNQDTDYIaigKQEGAKLAFGGEVISR----DTPGFYLQPA 364
Cdd:cd07095 250 DGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIA---AAAARYL---LAQQDLLALGGEPLLAmerlVAGTAFLSPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 365 LFtEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHV 444
Cdd:cd07095 324 II-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGASSTA 402
|
410 420
....*....|....*....|..
gi 803452457 445 PFGGRKASSYGpREQGKYAAEF 466
Cdd:cd07095 403 PFGGVGLSGNH-RPSAYYAADY 423
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
7-456 |
1.72e-91 |
|
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: 287.55 E-value: 1.72e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 7 LIAGEWVGGDGVANINPSNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLS 86
Cdd:cd07125 37 INGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 87 REEGKTLAEGIGEtVRAGQIF-EFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYG 165
Cdd:cd07125 117 AEAGKTLADADAE-VREAIDFcRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 166 NTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRvaVASVEHNRKYQL 245
Cdd:cd07125 196 NTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKL--INRALAERDGPI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 246 -----EMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIG 320
Cdd:cd07125 274 lpliaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 321 PVVDQSQLNQDTDYIAIGKQEGAKLAfggEVISRDTPGFYLQPALFtEATNemrIS--REEIFGPVAAVIRVK--DYDEA 396
Cdd:cd07125 354 PLIDKPAGKLLRAHTELMRGEAWLIA---PAPLDDGNGYFVAPGII-EIVG---IFdlTTEVFGPILHVIRFKaeDLDEA 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 803452457 397 LAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHV-PFGGRKASSYGP 456
Cdd:cd07125 427 IEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRqPFGGWGLSGTGP 487
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
8-461 |
1.09e-90 |
|
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: 284.29 E-value: 1.09e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 8 IAGEWVGGDG---VANINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRL 84
Cdd:cd07111 26 INGKWVKPENrksFPTINPA-TGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 85 LSREEGKTLAEgigetVR------AGQIFEFFAGETLRLAGEVvpsvrPGigveitREPAGVVGIITPWNFPIAIPAWKI 158
Cdd:cd07111 105 ESLDNGKPIRE-----SRdcdiplVARHFYHHAGWAQLLDTEL-----AG------WKPVGVVGQIVPWNFPLLMLAWKI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 159 APALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVvGQAMLDSPDVQAITFTGSTATGKRVAVASVE 238
Cdd:cd07111 169 CPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 239 HNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTH 318
Cdd:cd07111 248 TGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAID 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 319 IGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDtpGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALA 398
Cdd:cd07111 328 MGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSK--GPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVA 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 803452457 399 VANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlpTAGV-DFHVPFGGRKASSYGpREQGK 461
Cdd:cd07111 406 LANNTPYGLAASVWSENLSLALEVALSLKAGVVWIN--GHNLfDAAAGFGGYRESGFG-REGGK 466
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
55-457 |
1.98e-90 |
|
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: 282.66 E-value: 1.98e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLR-LAGEVVPSVRPGIG-VE 132
Cdd:cd07101 34 WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAERlLKPRRRRGAIPVLTrTT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 133 ITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAML 212
Cdd:cd07101 114 VNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 213 DSPDVqaITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGI 292
Cdd:cd07101 194 DNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 293 HDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTPGFYlQPALFTEATNE 372
Cdd:cd07101 272 YDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARPDLGPYFY-EPTVLTGVTED 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 373 MRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVN--LPTAGVDFHVPFGGRK 450
Cdd:cd07101 351 MELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNegYAAAWASIDAPMGGMK 430
|
....*..
gi 803452457 451 ASSYGPR 457
Cdd:cd07101 431 DSGLGRR 437
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
4-471 |
2.26e-89 |
|
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: 280.88 E-value: 2.26e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 4 HQNLIAGEW---VGGDGVANINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDE 80
Cdd:cd07116 1 YDNFIGGEWvapVKGEYFDNITPV-TGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 81 LGRLLSREEGKTLAEGIGETVR-AGQIFEFFAGETLRLAGEVVPSVRPGIGVEItREPAGVVGIITPWNFPIAIPAWKIA 159
Cdd:cd07116 80 LAVAETWDNGKPVRETLAADIPlAIDHFRYFAGCIRAQEGSISEIDENTVAYHF-HEPLGVVGQIIPWNFPLLMATWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 160 PALCYGNTVVLKPAELVPGCSWAIVDILHRAgLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEH 239
Cdd:cd07116 159 PALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 240 NRKYQLEMGGKNPFVVL------DDADLAVAVEAAVNSAfFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDAL 313
Cdd:cd07116 238 IIPVTLELGGKSPNIFFadvmdaDDAFFDKALEGFVMFA-LNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 314 KPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGE--VISRDTPGFYLQPALFtEATNEMRISREEIFGPVAAVIRVK 391
Cdd:cd07116 317 DTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGErnELGGLLGGGYYVPTTF-KGGNKMRIFQEEIFGPVLAVTTFK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 392 DYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVN----LPTagvdfHVPFGGRKASSYGpREQGKYAAEFY 467
Cdd:cd07116 396 DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNcyhlYPA-----HAAFGGYKQSGIG-RENHKMMLDHY 469
|
....
gi 803452457 468 TNVK 471
Cdd:cd07116 470 QQTK 473
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
18-474 |
2.72e-89 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 280.09 E-value: 2.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 18 VANINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGI 97
Cdd:PRK09406 3 IATINPA-TGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 98 GETVRAGQIFEFFA--GETLrLAGEvvPSVRPGIGVE---ITREPAGVVGIITPWNFPIaipaWKI----APALCYGNTV 168
Cdd:PRK09406 82 AEALKCAKGFRYYAehAEAL-LADE--PADAAAVGASrayVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGNVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 169 VLKPAELVPGCSWAIVDILHRAGLPKGVL-NLVMGKGSVvgQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEM 247
Cdd:PRK09406 155 LLKHASNVPQTALYLADLFRRAGFPDGCFqTLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 248 GGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQ 327
Cdd:PRK09406 233 GGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 328 LNQDTDYIAIGKQEGAKLAFGGEVISRdtPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGL 407
Cdd:PRK09406 313 RDEVEKQVDDAVAAGATILCGGKRPDG--PGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 803452457 408 SSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDfHVPFGGRKASSYGpREQGKYAAEFYTNVKTAY 474
Cdd:PRK09406 391 GSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYP-ELPFGGVKRSGYG-RELSAHGIREFCNIKTVW 455
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
7-475 |
2.86e-89 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 280.61 E-value: 2.86e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 7 LIAGEWVGGDGVANINPSN--TDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRL 84
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNpaTNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 85 LSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCY 164
Cdd:TIGR01722 84 ITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIAC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 165 GNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQaMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQ 244
Cdd:TIGR01722 164 GNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDR-LLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 245 LEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTeGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVD 324
Cdd:TIGR01722 243 ALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLV-GAADEWVPEIRERAEKIRIGPGDDPGAEMGPLIT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 325 QSQLNQDTDYIAIGKQEGAKLAFGGEVISRD--TPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVAND 402
Cdd:TIGR01722 322 PQAKDRVASLIAGGAAEGAEVLLDGRGYKVDgyEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 803452457 403 TPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPT-AGVDFHvPFGGRKASSYGPRE-QGKYAAEFYTNVKTAYT 475
Cdd:TIGR01722 402 SPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIpVPLPYF-SFTGWKDSFFGDHHiYGKQGTHFYTRGKTVTT 475
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
8-472 |
2.21e-86 |
|
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: 273.69 E-value: 2.21e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 8 IAGEWVG-GDGVANINPSNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLS 86
Cdd:cd07083 23 IGGEWVDtKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 87 REEGKTLAEGIGETVRAGQIFEFFAGETLRLAG--EVVPSVrPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCY 164
Cdd:cd07083 103 YEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPY-PGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 165 GNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRV--AVASVEHNR- 241
Cdd:cd07083 182 GNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIyeAAARLAPGQt 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 242 ---KYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTH 318
Cdd:cd07083 262 wfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 319 IGPVVDQSQLNQDTDYIAIGKQEGaKLAFGGEVIsrDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVK--DYDEA 396
Cdd:cd07083 342 LGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRL--EGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKddDFAEA 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 803452457 397 LAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHV-PFGGRKASSYGPREQGKYAAEFYTNVKT 472
Cdd:cd07083 419 LEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVqPFGGFKLSGTNAKTGGPHYLRRFLEMKA 495
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
62-471 |
3.38e-86 |
|
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: 271.81 E-value: 3.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 62 ERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVP--SVRPGIGVE--ITREP 137
Cdd:cd07147 44 RRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEATRIYGEVLPldISARGEGRQglVRRFP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 138 AGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNlVMGKGSVVGQAMLDSPDV 217
Cdd:cd07147 124 IGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFS-VLPCSRDDADLLVTDERI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 218 QAITFTGSTATG---KRVAVAsvehnRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHD 294
Cdd:cd07147 203 KLLSFTGSPAVGwdlKARAGK-----KKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 295 RFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEvisRDtpGFYLQPALFTEATNEMR 374
Cdd:cd07147 278 EFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGGK---RD--GALLEPTILEDVPPDME 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 375 ISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVN-LPTAGVDfHVPFGGRKASS 453
Cdd:cd07147 353 VNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINdVPTFRVD-HMPYGGVKDSG 431
|
410
....*....|....*...
gi 803452457 454 YGpREQGKYAAEFYTNVK 471
Cdd:cd07147 432 IG-REGVRYAIEEMTEPR 448
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
55-474 |
5.38e-86 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 272.54 E-value: 5.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVR-AGQIFEFFAGETLRLAGEVVPSVRPGIGVeI 133
Cdd:PRK09847 75 WSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDDIPgAARAIRWYAEAIDKVYGEVATTSSHELAM-I 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 134 TREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLD 213
Cdd:PRK09847 154 VREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 214 SPDVQAITFTGSTATGKRVAVASVEHNRK-YQLEMGGKNPFVVLDDA-DLAVAVEAAVNSAFFSTGQRCTASSRIIVTEG 291
Cdd:PRK09847 234 HNDIDAIAFTGSTRTGKQLLKDAGDSNMKrVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEES 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 292 IHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEvisRDTPGfYLQPALFTEATN 371
Cdd:PRK09847 314 IADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRN---AGLAA-AIGPTIFVDVDP 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 372 EMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGvDFHVPFGGRKA 451
Cdd:PRK09847 390 NASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDG-DMTVPFGGYKQ 468
|
410 420
....*....|....*....|...
gi 803452457 452 SSYGpREQGKYAAEFYTNVKTAY 474
Cdd:PRK09847 469 SGNG-RDKSLHALEKFTELKTIW 490
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
15-472 |
1.70e-85 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 272.14 E-value: 1.70e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 15 GDGVANINPSNTDDVVGEYARAsaedakaaiaaaKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLA 94
Cdd:PRK09407 42 GEPLATVPVSTAADVEAAFARA------------RAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 95 EGIGETVRAGQIFEFFA--GETLrLAGEVVPSVRPGIG-VEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLK 171
Cdd:PRK09407 110 HAFEEVLDVALTARYYArrAPKL-LAPRRRAGALPVLTkTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 172 PAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVqaITFTGSTATGKRVAVASVEHNRKYQLEMGGKN 251
Cdd:PRK09407 189 PDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNADY--LMFTGSTATGRVLAEQAGRRLIGFSLELGGKN 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 252 PFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQD 331
Cdd:PRK09407 267 PMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 332 TDYIAIGKQEGAKLAFGGEVISRDTPGFYlQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGI 411
Cdd:PRK09407 347 SAHVDDAVAKGATVLAGGKARPDLGPLFY-EPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASV 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 803452457 412 ATTSLKHATHFKRNAEAGMVMVN---LPTAG-VDfhVPFGGRKASSYGpREQGKYAAEFYTNVKT 472
Cdd:PRK09407 426 WTGDTARGRAIAARIRAGTVNVNegyAAAWGsVD--APMGGMKDSGLG-RRHGAEGLLKYTESQT 487
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
1-466 |
5.88e-82 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 261.82 E-value: 5.88e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 1 MTLhqnLIAGEWVGGDG--VANINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARK 78
Cdd:PRK09457 1 MTL---WINGDWIAGQGeaFESRNPV-SGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 79 DELGRLLSREEGKTLAEGIGE-TVRAGQI------FEFFAGETLRLAGEVVPSVRpgigveitREPAGVVGIITPWNFPI 151
Cdd:PRK09457 77 EELAEVIARETGKPLWEAATEvTAMINKIaisiqaYHERTGEKRSEMADGAAVLR--------HRPHGVVAVFGPYNFPG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 152 AIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGkGSVVGQAMLDSPDVQAITFTGSTATGKR 231
Cdd:PRK09457 149 HLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 232 VavasvehNRKY--------QLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIH-DRFVAAMGE 302
Cdd:PRK09457 228 L-------HRQFagqpekilALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 303 RIKGLVVD--DAlKPGTHIGPVVDQSQLNQDTDYIAigkqegAKLAFGGEVI---SRDTPGF-YLQPALFtEATNEMRIS 376
Cdd:PRK09457 301 VAKRLTVGrwDA-EPQPFMGAVISEQAAQGLVAAQA------QLLALGGKSLlemTQLQAGTgLLTPGII-DVTGVAELP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 377 REEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRKASSyGP 456
Cdd:PRK09457 373 DEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASSAAPFGGVGASG-NH 451
|
490
....*....|
gi 803452457 457 REQGKYAAEF 466
Cdd:PRK09457 452 RPSAYYAADY 461
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
132-477 |
1.37e-74 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 242.36 E-value: 1.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 132 EITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDIL-HRAGLPKGVLNLVMGKGSVVGQA 210
Cdd:TIGR04284 136 TLRREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELIaEHTDFPPGVVNIVTSSDHRLGAL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 211 MLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTE 290
Cdd:TIGR04284 216 LAKDPRVDMVSFTGSTATGRAVMADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 291 GIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTPGFYLQPALFTEAT 370
Cdd:TIGR04284 296 ARYDEAVAAAAATMGSIKPGDPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGRPADRDRGFFVEPTVIAGLD 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 371 NEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlptAGVDF--HVPFGG 448
Cdd:TIGR04284 376 NNARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVN---GGVWYsaDAPFGG 452
|
330 340
....*....|....*....|....*....
gi 803452457 449 RKASSYGpREQGKYAAEFYTNVKTAYTLA 477
Cdd:TIGR04284 453 YKQSGIG-REMGVAGFEEYLETKLIATAA 480
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
55-455 |
3.16e-74 |
|
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: 241.05 E-value: 3.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEG-IGE----------TVRAGQifeffagETLRlagevvP 123
Cdd:cd07098 34 WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEilvtcekirwTLKHGE-------KALR------P 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 124 SVRPG------IGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRA----GLP 193
Cdd:cd07098 101 ESRPGgllmfyKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 194 KGVLNLVMGKGSVvGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAF 273
Cdd:cd07098 181 PDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 274 FSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGE--V 351
Cdd:cd07098 260 QSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKryP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 352 ISRDTPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMV 431
Cdd:cd07098 340 HPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMV 419
|
410 420 430
....*....|....*....|....*....|.
gi 803452457 432 MVNlptagvDFHV-------PFGGRKASSYG 455
Cdd:cd07098 420 AIN------DFGVnyyvqqlPFGGVKGSGFG 444
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
8-460 |
3.82e-72 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 237.04 E-value: 3.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 8 IAGEW-VGGDGVANINPSNtDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLS 86
Cdd:PLN02315 25 VGGEWrANGPLVSSVNPAN-NQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 87 REEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGN 166
Cdd:PLN02315 104 LEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 167 TVVLKPAELVPGCSWA----IVDILHRAGLPKGVLNLVMGkGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRK 242
Cdd:PLN02315 184 CVVWKGAPTTPLITIAmtklVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 243 YQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPV 322
Cdd:PLN02315 263 CLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 323 VDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDtpGFYLQPALfTEATNEMRISREEIFGPVAAVIRVKDYDEALAVAND 402
Cdd:PLN02315 343 HTPESKKNFEKGIEIIKSQGGKILTGGSAIESE--GNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNS 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 803452457 403 TPFGLSSGIATTslKHATHFK----RNAEAGMVMVNLPTAGVDFHVPFGGRKASSyGPREQG 460
Cdd:PLN02315 420 VPQGLSSSIFTR--NPETIFKwigpLGSDCGIVNVNIPTNGAEIGGAFGGEKATG-GGREAG 478
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
20-474 |
2.54e-71 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 233.60 E-value: 2.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 20 NINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGE 99
Cdd:PRK13968 11 SVNPA-TGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 100 TVRAGQIFEFFA--GETLrLAGEvvPSVRPGIGVEITREPAGVVGIITPWNFPIaipaWKI----APALCYGNTVVLKPA 173
Cdd:PRK13968 90 VAKSANLCDWYAehGPAM-LKAE--PTLVENQQAVIEYRPLGTILAIMPWNFPL----WQVmrgaVPILLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 174 ELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQaMLDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPF 253
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQ-MINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 254 VVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHD----RFVAAmgerIKGLVVDDALKPGTHIGPVVD---QS 326
Cdd:PRK13968 242 IVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASafteRFVAA----AAALKMGDPRDEENALGPMARfdlRD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 327 QLNQDtdyIAIGKQEGAKLAFGGEVISRDtpGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFG 406
Cdd:PRK13968 318 ELHHQ---VEATLAEGARLLLGGEKIAGA--GNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFG 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 803452457 407 LSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGvDFHVPFGGRKASSYGpREQGKYAAEFYTNVKTAY 474
Cdd:PRK13968 393 LSATIFTTDETQARQMAARLECGGVFINGYCAS-DARVAFGGVKKSGFG-RELSHFGLHEFCNIQTVW 458
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
6-472 |
3.32e-71 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 236.95 E-value: 3.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 6 NLIAGEWVGGDG---VANINPSnTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELG 82
Cdd:PLN02419 116 NLIGGSFVESQSssfIDVINPA-TQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 83 RLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPAL 162
Cdd:PLN02419 195 MNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 163 CYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVgQAMLDSPDVQAITFTGSTATGKRVAVASVEHNRK 242
Cdd:PLN02419 275 TCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 243 YQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIV---TEGIHDRFVaamgERIKGLVVDDALKPGTHI 319
Cdd:PLN02419 354 IQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLV----ERAKALKVTCGSEPDADL 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 320 GPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISrdTPGF----YLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDE 395
Cdd:PLN02419 430 GPVISKQAKERICRLIQSGVDDGAKLLLDGRDIV--VPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDE 507
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 803452457 396 ALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHVPFGGRKASSYGPRE-QGKYAAEFYTNVKT 472
Cdd:PLN02419 508 AISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNfYGKAGVDFFTQIKL 585
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
62-455 |
1.36e-66 |
|
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: 220.75 E-value: 1.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 62 ERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGEVVP----SVRPGIGVEITREP 137
Cdd:cd07148 45 ERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREIPmgltPASAGRIAFTTREP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 138 AGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKgSVVGQAMLDSPDV 217
Cdd:cd07148 125 IGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCE-NAVAEKLVTDPRV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 218 QAITFTGSTATGKRVAvASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFV 297
Cdd:cd07148 204 AFFSFIGSARVGWMLR-SKLAPGTRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 298 AAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTpgfyLQPALFTEATNEMRISR 377
Cdd:cd07148 283 QRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTT----YAPTVLLDPPRDAKVST 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 803452457 378 EEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTA-GVDFhVPFGGRKASSYG 455
Cdd:cd07148 359 QEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAfRVDW-MPFAGRRQSGYG 436
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
8-473 |
3.11e-65 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 227.39 E-value: 3.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 8 IAGEWVGGDGVANI--NPSNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLL 85
Cdd:PRK11904 552 QAGPIINGEGEARPvvSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALC 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 86 SREEGKTLAEGIGEtVRAGQIF-EFFAGETLRLAGEVVPSVRP-GIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALC 163
Cdd:PRK11904 632 VREAGKTLQDAIAE-VREAVDFcRYYAAQARRLFGAPEKLPGPtGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALA 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 164 YGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVavasvehNRky 243
Cdd:PRK11904 711 AGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARII-------NR-- 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 244 QL------------EMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVA----AMGErikgL 307
Cdd:PRK11904 782 TLaardgpivpliaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEmlkgAMAE----L 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 308 VVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEgAKLAFGGEVISRDTPGFYLQPALFteatnEM-RIS--REEIFGPV 384
Cdd:PRK11904 858 KVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPLPAGTENGHFVAPTAF-----EIdSISqlEREVFGPI 931
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 385 AAVIRVK--DYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHV-PFGGRKASSYGPREQG- 460
Cdd:PRK11904 932 LHVIRYKasDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVqPFGGQGLSGTGPKAGGp 1011
|
490
....*....|....*..
gi 803452457 461 ----KYAAEFYTNVKTA 473
Cdd:PRK11904 1012 hyllRFATEKTVTVNTT 1028
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
7-456 |
4.65e-65 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 227.44 E-value: 4.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 7 LIAGEWVGGDGVANINPSNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLS 86
Cdd:PRK11905 558 LLAGGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAV 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 87 REEGKTLAEGIGEtVRAGQIF-EFFAGETLRLAGEVvpsvrpgigveiTREPAGVVGIITPWNFPIAIPAWKIAPALCYG 165
Cdd:PRK11905 638 REAGKTLANAIAE-VREAVDFlRYYAAQARRLLNGP------------GHKPLGPVVCISPWNFPLAIFTGQIAAALVAG 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 166 NTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVAVASVEH-NRKYQ 244
Cdd:PRK11905 705 NTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRsGPPVP 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 245 L--EMGGKNPFVVlDDADLA-VAVEAAVNSAFFSTGQRCTAsSRII-VTEGIHDRFVA----AMGErikgLVVDDALKPG 316
Cdd:PRK11905 785 LiaETGGQNAMIV-DSSALPeQVVADVIASAFDSAGQRCSA-LRVLcLQEDVADRVLTmlkgAMDE----LRIGDPWRLS 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 317 THIGPVVDQSQLNQDTDYIAIGKQEG---AKLAFGGEVisrdTPGFYLQPALF-TEATNEMrisREEIFGPVAAVIRVK- 391
Cdd:PRK11905 859 TDVGPVIDAEAQANIEAHIEAMRAAGrlvHQLPLPAET----EKGTFVAPTLIeIDSISDL---EREVFGPVLHVVRFKa 931
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 803452457 392 -DYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHV-PFGGRKASSYGP 456
Cdd:PRK11905 932 dELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVqPFGGEGLSGTGP 998
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
7-455 |
2.93e-64 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 215.78 E-value: 2.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 7 LIAGEW---VGGDGVANINPS-----------NTDDVVGEYARASAEDAKaaiaaakaafpaWSRSGILERHAILKKTAD 72
Cdd:PLN00412 19 YADGEWrtsSSGKSVAITNPStrktqykvqacTQEEVNKAMESAKAAQKA------------WAKTPLWKRAELLHKAAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 73 EILARKDELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLRLAGE---VVPSVRPGIGVE----ITREPAGVVGIIT 145
Cdd:PLN00412 87 ILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEgkfLVSDSFPGNERNkyclTSKIPLGVVLAIP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 146 PWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGS 225
Cdd:PLN00412 167 PFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 226 TaTGkrVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIK 305
Cdd:PLN00412 247 D-TG--IAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 306 GLVV----DDAlkpgtHIGPVVDQSQLNQDTDYIAIGKQEGAKLAfggEVISRDtpGFYLQPALFTEATNEMRISREEIF 381
Cdd:PLN00412 324 KLTVgppeDDC-----DITPVVSESSANFIEGLVMDAKEKGATFC---QEWKRE--GNLIWPLLLDNVRPDMRIAWEEPF 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 803452457 382 GPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTA-GVDfHVPFGGRKASSYG 455
Cdd:PLN00412 394 GPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPArGPD-HFPFQGLKDSGIG 467
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
7-456 |
5.01e-62 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 218.65 E-value: 5.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 7 LIAGEWVGGDGVANINPSNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLS 86
Cdd:COG4230 561 LIAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLV 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 87 REEGKTLAEGIGEtVR---------AGQIFEFFAGETlrlagevvpsvrpgigveiTREPAGVVGIITPWNFPIAIPAWK 157
Cdd:COG4230 641 REAGKTLPDAIAE-VReavdfcryyAAQARRLFAAPT-------------------VLRGRGVFVCISPWNFPLAIFTGQ 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 158 IAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRVavasv 237
Cdd:COG4230 701 VAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLI----- 775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 238 ehNRkyQL------------EMGGKNPFVVlDDADLAVAVEA-AVNSAFFSTGQRCTAsSRII-VTEGIHDRFVA----A 299
Cdd:COG4230 776 --NR--TLaardgpivpliaETGGQNAMIV-DSSALPEQVVDdVLASAFDSAGQRCSA-LRVLcVQEDIADRVLEmlkgA 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 300 MGErikgLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGaKLAFGGEVISRDTPGFYLQPALFteatnemRISR-- 377
Cdd:COG4230 850 MAE----LRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEG-RLVHQLPLPEECANGTFVAPTLI-------EIDSis 917
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 378 ---EEIFGPVAAVIRVK--DYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNL----PTAGVDfhvPFGG 448
Cdd:COG4230 918 dleREVFGPVLHVVRYKadELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRniigAVVGVQ---PFGG 994
|
....*...
gi 803452457 449 RKASSYGP 456
Cdd:COG4230 995 EGLSGTGP 1002
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
21-471 |
2.18e-57 |
|
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: 197.83 E-value: 2.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 21 INPSNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGET 100
Cdd:TIGR01238 56 TNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 101 VRAGQIFEFFAGEtlrlAGEVVPsvrpgigvEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCS 180
Cdd:TIGR01238 136 REAVDFCRYYAKQ----VRDVLG--------EFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 181 WAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRV--AVASVEHNR-KYQLEMGGKNPFVVlD 257
Cdd:TIGR01238 204 YRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLInqTLAQREDAPvPLIAETGGQNAMIV-D 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 258 DADLAVAVEAAV-NSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIA 336
Cdd:TIGR01238 283 STALPEQVVRDVlRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 337 IGKQEGAKLAFGGEVISRDTP-GFYLQPALFteATNEMRISREEIFGPVAAVIRVK--DYDEALAVANDTPFGLSSGIAT 413
Cdd:TIGR01238 363 HMSQTQKKIAQLTLDDSRACQhGTFVAPTLF--ELDDIAELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVHS 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 803452457 414 TSLKHATHFKRNAEAGMVMVNLPTAGVDFHV-PFGGRKASSYGPREQGKYAAEFYTNVK 471
Cdd:TIGR01238 441 RIETTYRWIEKHARVGNCYVNRNQVGAVVGVqPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
120-472 |
1.19e-54 |
|
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: 188.50 E-value: 1.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 120 EVVPSVRPGIGvEITREPAGVVGIITPWNFPIA---IPAwkiAPALCYGNTVVLKPAELVPGCSWAIVDILHRAgLPKGV 196
Cdd:cd07087 84 SVPLLLQPAKA-YVIPEPLGVVLIIGPWNYPLQlalAPL---IGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 197 LNLVMGKGSVvGQAMLDSP-DVqaITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFS 275
Cdd:cd07087 159 VAVVEGGVEV-ATALLAEPfDH--IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 276 TGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKpGTHIGPVVDQSQLNQDTDYIaigkqEGAKLAFGGEVisrD 355
Cdd:cd07087 236 AGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKE-SPDYGRIINERHFDRLASLL-----DDGKVVIGGQV---D 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 356 TPGFYLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNl 435
Cdd:cd07087 307 KEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVN- 385
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 803452457 436 ptaGVDFHV-----PFGGRKASSYGpREQGKYAAEFYTNVKT 472
Cdd:cd07087 386 ---DVLLHAaipnlPFGGVGNSGMG-AYHGKAGFDTFSHLKS 423
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
7-452 |
1.11e-52 |
|
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: 185.48 E-value: 1.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 7 LIAGEWVGGDGVANI-NPSNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTAD--------EILAr 77
Cdd:cd07123 36 VIGGKEVRTGNTGKQvMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADllsgkyryELNA- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 78 KDELGrllsreEGKTL--AEG--IGETVragQIFEFFAGETLRLAGEVVPSVRPGIGVEITREP-AGVVGIITPWNF-PI 151
Cdd:cd07123 115 ATMLG------QGKNVwqAEIdaACELI---DFLRFNVKYAEELYAQQPLSSPAGVWNRLEYRPlEGFVYAVSPFNFtAI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 152 A--IPAwkiAPALcYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATG 229
Cdd:cd07123 186 GgnLAG---APAL-MGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 230 KRVAVASVEHNRKYQL------EMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGER 303
Cdd:cd07123 262 KSLWKQIGENLDRYRTyprivgETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 304 IKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQE-GAKLAFGGEviSRDTPGFYLQPALFtEATNEM-RISREEIF 381
Cdd:cd07123 342 LKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGK--CDDSVGYFVEPTVI-ETTDPKhKLMTEEIF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 382 GPVAAVIRVKD--YDEALAVANDT-PFGLSSGI----------ATTSLKHAthfkrnaeAGMVMVN-LPTAGVDFHVPFG 447
Cdd:cd07123 419 GPVLTVYVYPDsdFEETLELVDTTsPYALTGAIfaqdrkaireATDALRNA--------AGNFYINdKPTGAVVGQQPFG 490
|
....*
gi 803452457 448 GRKAS 452
Cdd:cd07123 491 GARAS 495
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
55-455 |
1.42e-52 |
|
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: 183.20 E-value: 1.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEgigetVRAGQIFEF-----FAGETLR--LAGEVVPS--V 125
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAE-----VDLTEILPVlseinHAIKHLKkwMKPKRVRTplL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 126 RPGIGVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVlNLVMGkGS 205
Cdd:cd07134 89 LFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-AVFEG-DA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 206 VVGQAMLDSPdVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSR 285
Cdd:cd07134 167 EVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 286 IIVTEGIHDRFVAAMGERI-KGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVisrDTPGFYLQPA 364
Cdd:cd07134 246 VFVHESVKDAFVEHLKAEIeKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQF---DAAQRYIAPT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 365 LFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlptaGVDFHV 444
Cdd:cd07134 323 VLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN----DVVLHF 398
|
410
....*....|....*.
gi 803452457 445 -----PFGGRKASSYG 455
Cdd:cd07134 399 lnpnlPFGGVNNSGIG 414
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
7-460 |
8.22e-49 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 180.17 E-value: 8.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 7 LIAGEWVGGDGVANINPSNTDDVVGEYARASAEDAKAAIAAAKAAFPAWSRSGILERHAILKKTADEILARKDELGRLLS 86
Cdd:PRK11809 650 MLEDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLV 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 87 REEGKTLAEGIGEtVR---------AGQIFEFFAGETLRlagevvpsvrpgigveitrePAGVVGIITPWNFPIAIPAWK 157
Cdd:PRK11809 730 REAGKTFSNAIAE-VReavdflryyAGQVRDDFDNDTHR--------------------PLGPVVCISPWNFPLAIFTGQ 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 158 IAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTatgkrvAVAS- 236
Cdd:PRK11809 789 VAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGST------EVARl 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 237 VEHNRKYQL-----------EMGGKNPFVVlDDADLAVAVEAAV-NSAFFSTGQRCTASSRIIVTEGIHDRFVA----AM 300
Cdd:PRK11809 863 LQRNLAGRLdpqgrpipliaETGGQNAMIV-DSSALTEQVVADVlASAFDSAGQRCSALRVLCLQDDVADRTLKmlrgAM 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 301 GErikgLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEGAK---LAFGGEVISRDtpGFYLQPALFT-EATNEMris 376
Cdd:PRK11809 942 AE----CRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPvfqAARENSEDWQS--GTFVPPTLIElDSFDEL--- 1012
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 377 REEIFGPVAAVIRVK--DYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFHV-PFGGRKASS 453
Cdd:PRK11809 1013 KREVFGPVLHVVRYNrnQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVqPFGGEGLSG 1092
|
....*..
gi 803452457 454 YGPREQG 460
Cdd:PRK11809 1093 TGPKAGG 1099
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
125-455 |
9.85e-49 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 174.45 E-value: 9.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 125 VRPGIGvEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAgLPKGVLNLVMGkG 204
Cdd:PTZ00381 98 FGPGKS-YIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-G 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 205 SVVGQAMLDSP-DVqaITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTAS 283
Cdd:PTZ00381 175 VEVTTELLKEPfDH--IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 284 SRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHiGPVVDQSQLNQDTDYIaigKQEGAKLAFGGEVisrDTPGFYLQP 363
Cdd:PTZ00381 253 DYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDY-SRIVNEFHTKRLAELI---KDHGGKVVYGGEV---DIENKYVAP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 364 ALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlptaGVDFH 443
Cdd:PTZ00381 326 TIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN----DCVFH 401
|
330
....*....|....*..
gi 803452457 444 V-----PFGGRKASSYG 455
Cdd:PTZ00381 402 LlnpnlPFGGVGNSGMG 418
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
131-455 |
5.83e-45 |
|
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: 162.65 E-value: 5.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 131 VEITREPAGVVGIITPWNFPIAIpawKIAP---ALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLnlVMGKGSVV 207
Cdd:cd07133 95 AEVEYQPLGVVGIIVPWNYPLYL---ALGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVA--VVTGGADV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 208 GQA--------MLdspdvqaitFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQR 279
Cdd:cd07133 170 AAAfsslpfdhLL---------FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 280 CTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPgtHIGPVVDQSQLNQDTDYIAIGKQEGAKLAFGGEVISRDTPGF 359
Cdd:cd07133 241 CVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNP--DYTSIINERHYARLQGLLEDARAKGARVIELNPAGEDFAATR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 360 YLQPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlptaG 439
Cdd:cd07133 319 KLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN----D 394
|
330 340
....*....|....*....|.
gi 803452457 440 VDFHV-----PFGGRKASSYG 455
Cdd:cd07133 395 TLLHVaqddlPFGGVGASGMG 415
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
133-468 |
1.09e-43 |
|
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: 159.59 E-value: 1.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 133 ITREPAGVVGIITPWNFPIAIpawKIAP---ALCYGNTVVLKPAELVPGCSWAIVDILHRAgLPKGVLNLVMGkGSVVGQ 209
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPFQL---ALAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 210 AMLDSPdVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVT 289
Cdd:cd07136 171 ELLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 290 EGIHDRFVAAMGERIKGLVVDDALKPG--THIgpvVDQSQLNQDTDYIaigkqEGAKLAFGGEvISRDTpgFYLQPALFT 367
Cdd:cd07136 250 ESVKEKFIKELKEEIKKFYGEDPLESPdyGRI---INEKHFDRLAGLL-----DNGKIVFGGN-TDRET--LYIEPTILD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 368 EATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVN-----LPTAgvdf 442
Cdd:cd07136 319 NVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtimhLANP---- 394
|
330 340
....*....|....*....|....*....
gi 803452457 443 HVPFGGRKAS---SYgpreQGKYAaeFYT 468
Cdd:cd07136 395 YLPFGGVGNSgmgSY----HGKYS--FDT 417
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
133-462 |
5.80e-39 |
|
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: 146.60 E-value: 5.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 133 ITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAgLPKGVLNLVMGkGSVVGQAML 212
Cdd:cd07135 104 IRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQG-GVPETTALL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 213 DSP-DvqAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEG 291
Cdd:cd07135 182 EQKfD--KIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 292 IHDRFVAAMGERIKGLVVDDAlKPGTHIGPVVDQSQLNQDTDYIaigKQEGAKLAFGGEvisRDTPGFYLQPALFTEATN 371
Cdd:cd07135 260 VYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLL---DTTKGKVVIGGE---MDEATRFIPPTIVSDVSW 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 372 EMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlptaGVDFHV-----PF 446
Cdd:cd07135 333 DDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVIN----DTLIHVgvdnaPF 408
|
330
....*....|....*.
gi 803452457 447 GGRKASSYGpREQGKY 462
Cdd:cd07135 409 GGVGDSGYG-AYHGKY 423
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
55-400 |
2.51e-34 |
|
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: 133.90 E-value: 2.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDEL--GRLLSREEGKTLAEGIGETVRAGQIFEFfAGETLRLAGEVVPSVRPGIGVE 132
Cdd:cd07084 15 ARRLALPKRADFLARIIQRLAAKSYDIaaGAVLVTGKGWMFAENICGDQVQLRARAF-VIYSYRIPHEPGNHLGQGLKQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 133 ITRE--PAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAG-LPKGVLNLVMGKGSvVGQ 209
Cdd:cd07084 94 SHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGK-TMQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 210 AMLDSPDVQAITFTGSTATGKrvAVASVEHNRKYQLEMGGKNPFVVLDDAD-LAVAVEAAVNSAFFSTGQRCTASSRIIV 288
Cdd:cd07084 173 ALLLHPNPKMVLFTGSSRVAE--KLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 289 TEGIHDR-FVAAMGERIKGLVVDDALkpgthIGPVVDQSQLNQdtdYIAIGKQEGAKLAFGG-EVISRDTPGFY---LQP 363
Cdd:cd07084 251 PENWSKTpLVEKLKALLARRKLEDLL-----LGPVQTFTTLAM---IAHMENLLGSVLLFSGkELKNHSIPSIYgacVAS 322
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 803452457 364 ALF---TEATNEMRISREEIFGPVAAVIRVKDYDEALAVA 400
Cdd:cd07084 323 ALFvpiDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLE 362
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
130-462 |
6.94e-34 |
|
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: 132.35 E-value: 6.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 130 GVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAgLPKGVLNLVMGKGSVVGQ 209
Cdd:cd07132 93 DVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKY-LDKECYPVVLGGVEETTE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 210 AMLDSPDVqaITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFSTGQRCTASSRIIVT 289
Cdd:cd07132 172 LLKQRFDY--IFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCT 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 290 EGIHDRFVAAMGERIKGLVVDDAlKPGTHIGPVVDQSQLNQDTDYIaigkqEGAKLAFGGEVISRDTpgfYLQPALFTEA 369
Cdd:cd07132 250 PEVQEKFVEALKKTLKEFYGEDP-KESPDYGRIINDRHFQRLKKLL-----SGGKVAIGGQTDEKER---YIAPTVLTDV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 370 TNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVN--LPTAGVDfHVPFG 447
Cdd:cd07132 321 KPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNdtIMHYTLD-SLPFG 399
|
330
....*....|....*
gi 803452457 448 GRKASSYGpREQGKY 462
Cdd:cd07132 400 GVGNSGMG-AYHGKY 413
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
63-471 |
2.59e-33 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 130.61 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 63 RHAILKKTADEILARKDELGRLLSREEGKTLAEG----IGETVRA-----GQIFEFFAGETLRLAGEVVPSvrpgiGVEI 133
Cdd:cd07137 23 RKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfrdeVSVLVSScklaiKELKKWMAPEKVKTPLTTFPA-----KAEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 134 TREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSwAIVDILHRAGLPKGVLNLVMGkGSVVGQAMLD 213
Cdd:cd07137 98 VSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATS-ALLAKLIPEYLDTKAIKVIEG-GVPETTALLE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 214 SpDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAFFS-TGQRCTASSRIIVTEGI 292
Cdd:cd07137 176 Q-KWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVEESF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 293 HDRFVAAMGERIKGLVVDDALKPGtHIGPVVDQSQLNQDTDYIAiGKQEGAKLAFGGEvisRDTPGFYLQPALFTEATNE 372
Cdd:cd07137 255 APTLIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQRLSRLLD-DPSVADKIVHGGE---RDEKNLYIEPTILLDPPLD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 373 MRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNlpTAGVDF---HVPFGGR 449
Cdd:cd07137 330 SSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFN--DTVVQYaidTLPFGGV 407
|
410 420
....*....|....*....|..
gi 803452457 450 KASSYGpREQGKYAAEFYTNVK 471
Cdd:cd07137 408 GESGFG-AYHGKFSFDAFSHKK 428
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
55-401 |
6.19e-30 |
|
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: 121.49 E-value: 6.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 55 WSRSGILERHAILKKTADEILARKDELGRLLSREEGKTLAEGIGETVR-AGQifeffagetLRLAGEVV----------- 122
Cdd:cd07129 15 YRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRtTGQ---------LRLFADLVregswldarid 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 123 ---PSVRPGIGVEITRE--PAGVVGIITPWNFPIA--IPAWKIAPALCYGNTVVLKP-------AELVPGcswAIVDILH 188
Cdd:cd07129 86 padPDRQPLPRPDLRRMlvPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAhpahpgtSELVAR---AIRAALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 189 RAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTATGKRV--AVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVE 266
Cdd:cd07129 163 ATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALfdAAAARPEPIPFYAELGSVNPVFILPGALAERGEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 267 AA---VNSAFFSTGQRCTASSRIIVTEGIH-DRFVAAMGERIKglvvddALKPGTHIGPVVDQSqLNQDTDyiAIGKQEG 342
Cdd:cd07129 243 IAqgfVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALA------AAPAQTMLTPGIAEA-YRQGVE--ALAAAPG 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 803452457 343 AKLAFGGEVisrDTPGFYLQPALF-TEATNEMRIS--REEIFGPVAAVIRVKDYDEALAVAN 401
Cdd:cd07129 314 VRVLAGGAA---AEGGNQAAPTLFkVDAAAFLADPalQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
132-471 |
2.50e-28 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 117.45 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 132 EITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAgLPKGVLNLVmgKGSVVGQAM 211
Cdd:PLN02174 107 EIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVV--EGAVTETTA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 212 LDSPDVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVVLDDADLAVAVEAAVNSAF-FSTGQRCTASSRIIVTE 290
Cdd:PLN02174 184 LLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 291 GIHDRFVAAMGERIKGLVVDDALKpGTHIGPVVDQSQLNQDTDYIAiGKQEGAKLAFGGEvisRDTPGFYLQPALFTEAT 370
Cdd:PLN02174 264 EYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLD-EKEVSDKIVYGGE---KDRENLKIAPTILLDVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 371 NEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPTAGVDFH-VPFGGR 449
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHtLPFGGV 418
|
330 340
....*....|....*....|..
gi 803452457 450 KASSYGPReQGKYAAEFYTNVK 471
Cdd:PLN02174 419 GESGMGAY-HGKFSFDAFSHKK 439
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
132-471 |
4.93e-28 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 116.36 E-value: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 132 EITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVlnLVMGKGSVVGQAM 211
Cdd:PLN02203 103 EVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAV--KVIEGGPAVGEQL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 212 LDSPdVQAITFTGSTATGKRVAVASVEHNRKYQLEMGGKNPFVV--LDDA-DLAVAVEAAVNSAFFS-TGQRCTASSRII 287
Cdd:PLN02203 181 LQHK-WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIAIDYVL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 288 VTEGIHDRFVAAMGERIKGLVVDDALKPGtHIGPVVDQSQLNQDTDYIAiGKQEGAKLAFGGEVisrDTPGFYLQPALFT 367
Cdd:PLN02203 260 VEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLK-DPRVAASIVHGGSI---DEKKLFIEPTILL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 368 EATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGLSSGIATTSLKHATHFKRNAEAGMVMVN--LPTAGVDfHVP 445
Cdd:PLN02203 335 NPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNdaIIQYACD-SLP 413
|
330 340
....*....|....*....|....*.
gi 803452457 446 FGGRKASSYGpREQGKYAAEFYTNVK 471
Cdd:PLN02203 414 FGGVGESGFG-RYHGKYSFDTFSHEK 438
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
62-401 |
6.78e-23 |
|
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: 101.58 E-value: 6.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 62 ERHAILKKTADEILARKDELGRLlSREEGKTLAE-------GIGE-TVRAGQIFEFFAGETLRLAGEVVPSVRPG--IGV 131
Cdd:cd07128 60 ERAAMLKALAKYLMERKEDLYAL-SAATGATRRDswididgGIGTlFAYASLGRRELPNAHFLVEGDVEPLSKDGtfVGQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 132 EITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAG-LPKGVLNLVMGKgsvVGQA 210
Cdd:cd07128 139 HILTPRRGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGS---VGDL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 211 M--LDSPDVqaITFTGSTATGK--RVAVASVEHNRKYQLEMGGKNPFVVLDDA-------DL---AVAVEAAVNsaffsT 276
Cdd:cd07128 216 LdhLGEQDV--VAFTGSAATAAklRAHPNIVARSIRFNAEADSLNAAILGPDAtpgtpefDLfvkEVAREMTVK-----A 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 277 GQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEgAKLAFGG----EVI 352
Cdd:cd07128 289 GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGpdrfEVV 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 803452457 353 SRDT-PGFYLQPALFTEAT--NEMRISREEIFGPVAAVIRVKDYDEALAVAN 401
Cdd:cd07128 368 GADAeKGAFFPPTLLLCDDpdAATAVHDVEAFGPVATLMPYDSLAEAIELAA 419
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
79-397 |
1.29e-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: 100.26 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 79 DELGRLLSREEGKTLAEGIGETVRAGQIFEFFAGETLR-LA-GEVVPSVRPGIGVEITREPAGVVGIITPWNFPIAIPAW 156
Cdd:cd07126 82 DFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRfLArSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIPAL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 157 KIAPALCYGNTVVLKPAELVPGCSWAIVDILHRAGLPKGVLNLVMGKGSVVGQAMLDSpDVQAITFTGSTATGKRVAvas 236
Cdd:cd07126 162 QLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEA-NPRMTLFTGSSKVAERLA--- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 237 VEHNRKYQLEMGGKNpFVVL--DDADLAVAVEAAVNSAFFSTGQRCTASSRIIVtegiHDRFV-AAMGERIKGLVVDDAL 313
Cdd:cd07126 238 LELHGKVKLEDAGFD-WKILgpDVSDVDYVAWQCDQDAYACSGQKCSAQSILFA----HENWVqAGILDKLKALAEQRKL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 314 KPGThIGPVV---DQSQLNQDTDYIAIgkqEGAKLAFGGEVISRDT-PGFY--LQP-ALF----TEATNE-MRISREEIF 381
Cdd:cd07126 313 EDLT-IGPVLtwtTERILDHVDKLLAI---PGAKVLFGGKPLTNHSiPSIYgaYEPtAVFvpleEIAIEEnFELVTTEVF 388
|
330
....*....|....*.
gi 803452457 382 GPVAAVIRVKDYDEAL 397
Cdd:cd07126 389 GPFQVVTEYKDEQLPL 404
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
126-400 |
7.80e-21 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 95.16 E-value: 7.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 126 RPGIGVEITREPA-----------GVVGIITPWNFPiaipAW----KIAPALCYGNTVVLKPAELVPGCSWAIVDILHRA 190
Cdd:PRK11903 126 RDGEAVQLGKDPAfqgqhvlvptrGVALFINAFNFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 191 G-LPKGVLNLVMGKGSVVgQAMLDSPDVqaITFTGSTATGK--RVAVASVEHNRKYQLEMGGKNPFVVLDDAD-----LA 262
Cdd:PRK11903 202 GiLPAGALSVVCGSSAGL-LDHLQPFDV--VSFTGSAETAAvlRSHPAVVQRSVRVNVEADSLNSALLGPDAApgseaFD 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 263 VAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMGERIKGLVVDDALKPGTHIGPVVDQSQLNQDTDYIAIGKQEG 342
Cdd:PRK11903 279 LFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQA 358
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 803452457 343 AKLAFGGEVISRDTP---GFYLQPALF--TEATNEMRISREEIFGPVAAVIRVKDYDEALAVA 400
Cdd:PRK11903 359 EVLFDGGGFALVDADpavAACVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALA 421
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
154-444 |
4.28e-14 |
|
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: 74.44 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 154 PAWKIAPA----LCYGNTVVLKP--AELVPgcsWAIV-----DILHRAGL-PKGVLNLVMGKGSVVGQAMLDSPDVQAIT 221
Cdd:cd07127 206 PTWNGYPGlfasLATGNPVIVKPhpAAILP---LAITvqvarEVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIID 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 222 FTGSTATGKRVAvasvEHNRKYQL--EMGGKNPFVVLDDADL-AVAVEAAVNSAFFStGQRCTASSRIIV-TEGI----- 292
Cdd:cd07127 283 FTGSNAFGDWLE----ANARQAQVytEKAGVNTVVVDSTDDLkAMLRNLAFSLSLYS-GQMCTTPQNIYVpRDGIqtddg 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 293 ---HDRFVAAMGERIKGLVVDDALKPGThIGPVVDQSQLnqdtDYIAIGKQEGAKLAFGGEVISRDTPGFYLQPALFTEA 369
Cdd:cd07127 358 rksFDEVAADLAAAIDGLLADPARAAAL-LGAIQSPDTL----ARIAEARQLGEVLLASEAVAHPEFPDARVRTPLLLKL 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 370 TNEMR-ISREEIFGPVAAVIRVKDYDEALAVANDTPF---GLSSGIATTS---LKHATHFKRNAEA-------GMVMVNL 435
Cdd:cd07127 433 DASDEaAYAEERFGPIAFVVATDSTDHSIELARESVRehgAMTVGVYSTDpevVERVQEAALDAGValsinltGGVFVNQ 512
|
....*....
gi 803452457 436 PTAGVDFHV 444
Cdd:cd07127 513 SAAFSDFHG 521
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
131-438 |
2.03e-12 |
|
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: 68.67 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 131 VEITrEPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILH----RAGLPKGVLNLVMGKGSV 206
Cdd:cd07122 90 VEIA-EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMReaavAAGAPEGLIQWIEEPSIE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 207 VGQAMLDSPDVQAITFTGSTATgkrVAVAsvehnrkYQ-----LEMG-GKNPFVVLDDADLAVAVEAAVNSAFFSTGQRC 280
Cdd:cd07122 169 LTQELMKHPDVDLILATGGPGM---VKAA-------YSsgkpaIGVGpGNVPAYIDETADIKRAVKDIILSKTFDNGTIC 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 281 TASSRIIVTEGIHDRFVAAMgERIKGLVVDDALKPGTHIGPVVDQSQLNQDtdyiAIGK--QEGAKLAfgGEVISRDTPg 358
Cdd:cd07122 239 ASEQSVIVDDEIYDEVRAEL-KRRGAYFLNEEEKEKLEKALFDDGGTLNPD----IVGKsaQKIAELA--GIEVPEDTK- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 359 fyLQPALFTEATNEMRISREEIFgPVAAVIRVKDYDEALAVANDT----PFGLSSGIATTSLKHATHFKRNAEAGMVMVN 434
Cdd:cd07122 311 --VLVAEETGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKARELleygGAGHTAVIHSNDEEVIEEFALRMPVSRILVN 387
|
....
gi 803452457 435 LPTA 438
Cdd:cd07122 388 TPSS 391
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
130-438 |
2.70e-11 |
|
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: 65.36 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 130 GVEITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAELVPGCSWAIVDILHRA----GLPKGVLNLVMGKGS 205
Cdd:cd07081 88 GTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLIGWIDNPSI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 206 VVGQAMLDSPDVQAITFTGSTATgkrvaVASVEHNRKYQLEMGGKNPFVVLD-DADLAVAVEAAVNSAFFSTGQRCTASS 284
Cdd:cd07081 168 ELAQRLMKFPGIGLLLATGGPAV-----VKAAYSSGKPAIGVGAGNTPVVIDeTADIKRAVQSIVKSKTFDNGVICASEQ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 285 RIIVTEGIHDRFVAAMGERIKGLVVDDALKpgtHIGPVVDQsqlNQDTDYIAIGKQEGAKLAFGGEVISRDTpgfylqPA 364
Cdd:cd07081 243 SVIVVDSVYDEVMRLFEGQGAYKLTAEELQ---QVQPVILK---NGDVNRDIVGQDAYKIAAAAGLKVPQET------RI 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 365 LFTEAT--NEMRISREEIFGPVAAVIRVKDYDEALAVA----NDTPFGLSSGIATTSLKHATHFKRNAEA---GMVMVNL 435
Cdd:cd07081 311 LIGEVTslAEHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKAIENMNQFANAmktSRFVKNG 390
|
...
gi 803452457 436 PTA 438
Cdd:cd07081 391 PCS 393
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
49-400 |
9.50e-10 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 60.69 E-value: 9.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 49 KAAFPAWSRSGILERHAILKKTADEILARKDELGRLlsreegkTLAE-GIGetvRAGQIFeffagETLRLAGEVVPsvrp 127
Cdd:PRK15398 46 KVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAEL-------AVEEtGMG---RVEDKI-----AKNVAAAEKTP---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 128 giGVE---------------ITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKPAelvPG----CSWAIV---D 185
Cdd:PRK15398 107 --GVEdlttealtgdngltlIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPH---PGakkvSLRAIEllnE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 186 ILHRAGlpkGVLNLVmgkGSV------VGQAMLDSPDVQAITFTGSTA-------TGKRVAVAsvehnrkyqlemGGKNP 252
Cdd:PRK15398 182 AIVAAG---GPENLV---VTVaeptieTAQRLMKHPGIALLVVTGGPAvvkaamkSGKKAIGA------------GAGNP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 253 FVVLDD-ADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMgERIKGLVVDDA---------LKPGTHIgpv 322
Cdd:PRK15398 244 PVVVDEtADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLM-EKNGAVLLTAEqaeklqkvvLKNGGTV--- 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 803452457 323 vdqsqlnqDTDYiaIGKQEGAKLAFGGEVISRDTpgfylqPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVA 400
Cdd:PRK15398 320 --------NKKW--VGKDAAKILEAAGINVPKDT------RLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALA 381
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
48-442 |
1.68e-09 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 59.56 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 48 AKAAFPAWSRSGILERHAILKKTADEILARKDELGRlLSREEgktlaEGIGETvrAGQIfeffagETLRLAGEVVPsvrp 127
Cdd:cd07121 13 AKAAQKQYRKCTLADREKIIEAIREALLSNAEELAE-MAVEE-----TGMGRV--EDKI------AKNHLAAEKTP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 128 giGVE---------------ITREPAGVVGIITPWNFPIAIPAWKIAPALCYGNTVVLKP---AELVpgCSWAIVDI--- 186
Cdd:cd07121 75 --GTEdltttawsgdngltlVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKV--SAYAVELInka 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 187 LHRAGLPKGVLNLVMGKGSVVGQAMLDSPDVQAITFTGSTA-------TGKRVAVAsvehnrkyqlemGGKNPFVVLDD- 258
Cdd:cd07121 151 IAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAvvkaalsSGKKAIGA------------GAGNPPVVVDEt 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 259 ADLAVAVEAAVNSAFFSTGQRCTASSRIIVTEGIHDRFVAAMgERIKGLVVDD--ALKPGTHIgpVVDQSQLNQDTDYia 336
Cdd:cd07121 219 ADIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAM-QRNGAYVLNDeqAEQLLEVV--LLTNKGATPNKKW-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 337 IGKQEGAKLAFGGEVISRDTpgfylqPALFTEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDTPFGL--SSGIATT 414
Cdd:cd07121 294 VGKDASKILKAAGIEVPADI------RLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSK 367
|
410 420
....*....|....*....|....*....
gi 803452457 415 SLKHATHFKRNAEAGMVMVNLPT-AGVDF 442
Cdd:cd07121 368 NVENLTKMARAMQTTIFVKNGPSyAGLGV 396
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
130-448 |
6.03e-08 |
|
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: 54.54 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 130 GVEITREPAGVVGIITPWNFPIAIPAwKIAPALCYGNTVVLKPAELVPGCSWAIvDILHRA----GLPKGVLNLVMGKGS 205
Cdd:cd07077 93 ETYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRAL-ALLFQAadaaHGPKILVLYVPHPSD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 206 VVGQAMLDSPDVQAITFTGstatGKRVAVASVEH-NRKYQLEMGGKNPFVVLDD-ADLAVAVEAAVNSAFFStGQRCTAS 283
Cdd:cd07077 171 ELAEELLSHPKIDLIVATG----GRDAVDAAVKHsPHIPVIGFGAGNSPVVVDEtADEERASGSVHDSKFFD-QNACASE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 284 SRIIVtegiHDRFVAAMGERIKGLVVddalkpgthigpvvdqsqlnqdtdYIAIGKQEGAKLAFGgevisrdtpgfylqp 363
Cdd:cd07077 246 QNLYV----VDDVLDPLYEEFKLKLV------------------------VEGLKVPQETKPLSK--------------- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 364 alftEATNEMRISREEIFGPVAAVIRVKDYDEALAVANDT----PFGLSSGIATTSLKHATHFKRNAEAGMVMVNLPT-A 438
Cdd:cd07077 283 ----ETTPSFDDEALESMTPLECQFRVLDVISAVENAWMIiesgGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSkK 358
|
330
....*....|
gi 803452457 439 GVDFHVPFGG 448
Cdd:cd07077 359 GRGAFAGKGV 368
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
62-200 |
1.44e-03 |
|
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).
Pssm-ID: 143398 Cd Length: 406 Bit Score: 40.88 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 62 ERHAILKKTADEILARKDE---------------------LGRLLSREEG-KTLAEGIgETVRA-----GQIfeffaget 114
Cdd:cd07079 21 QKNAALLAIADALEANRDEileanakdlaaareaglsealLDRLLLTPERiEAMAEGL-RQVAAlpdpvGEV-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803452457 115 lrLAGEVVPSvrpGIGVEITREPAGVVGII-------TPwnfpiaipawkIAPALCY--GNTVVLKpaelvpGCSWA--- 182
Cdd:cd07079 92 --LRGWTLPN---GLQIEKVRVPLGVIGIIyesrpnvTV-----------DAAALCLksGNAVILR------GGSEAlhs 149
|
170 180
....*....|....*....|....*
gi 803452457 183 ---IVDILHRA----GLPKGVLNLV 200
Cdd:cd07079 150 nraLVEIIQEAleeaGLPEDAVQLI 174
|
|
| |
