|
Name |
Accession |
Description |
Interval |
E-value |
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
41-380 |
0e+00 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 683.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 41 GLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFknLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASG 120
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEF--PRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 121 AVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGP 200
Cdd:cd01156 79 SVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 201 DADVLIVYAKTDLAavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGL 280
Cdd:cd01156 159 DADTLVVYAKTDPS--AGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 281 DLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGV 360
Cdd:cd01156 237 DYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGV 316
|
330 340
....*....|....*....|
gi 1444691839 361 ILYSAECATQVALDGIQCFG 380
Cdd:cd01156 317 ILYAAEKATQVALDAIQILG 336
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
7-391 |
0e+00 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 558.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 7 LLGWRVAswRLRPPLAGFVSQRAHSLLpvddaingLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNLREFWKQLGN 86
Cdd:PLN02519 1 MLLSAAK--ARRRGLARRFSSSSSSLL--------FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVNLWKLMGD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 87 LGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSE 166
Cdd:PLN02519 71 FNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 167 PNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvpASRGITAFIVEKGMPGFSTSKKLDKLGMR 246
Cdd:PLN02519 151 PNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAA--GSKGITAFIIEKGMPGFSTAQKLDKLGMR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 247 GSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKM 326
Cdd:PLN02519 229 GSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKL 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1444691839 327 ADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCF-GQTFSAQHPPGR 391
Cdd:PLN02519 309 ADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLgGNGYINEYPTGR 374
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
42-380 |
1.15e-145 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 421.94 E-value: 1.15e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 42 LSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGA 121
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFP--RELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 122 VGLSYGAHsNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPD 201
Cdd:COG1960 83 LALPVGVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 202 ADVLIVYAKTDLAavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLD 281
Cdd:COG1960 162 ADVILVLARTDPA--AGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 282 LERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVI 361
Cdd:COG1960 240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAK 319
|
330
....*....|....*....
gi 1444691839 362 LYSAECATQVALDGIQCFG 380
Cdd:COG1960 320 LFATEAALEVADEALQIHG 338
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
44-380 |
4.46e-131 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 384.31 E-value: 4.46e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 44 EEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVG 123
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFP--REVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 124 LSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDAD 203
Cdd:cd01158 79 VIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 204 VLIVYAKTDLAAvpASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLE 283
Cdd:cd01158 159 FYIVFAVTDPSK--GYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 284 RLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILY 363
Cdd:cd01158 237 RIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLF 316
|
330
....*....|....*..
gi 1444691839 364 SAECATQVALDGIQCFG 380
Cdd:cd01158 317 ASEVAMRVTTDAVQIFG 333
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
44-380 |
5.63e-110 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 328.86 E-value: 5.63e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 44 EEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFknLREFWKQLGNLGVlgitapvqyggsglgylehvlvmeeisrasgavg 123
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEE--PWELLAELGLLLG---------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 124 lsygahsnlcINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDAD 203
Cdd:cd00567 45 ----------AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDAD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 204 VLIVYAKTDLAAvPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLE 283
Cdd:cd00567 115 LFIVLARTDEEG-PGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 284 RLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHC-TAKDCAGVIL 362
Cdd:cd00567 194 RLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKL 273
|
330
....*....|....*...
gi 1444691839 363 YSAECATQVALDGIQCFG 380
Cdd:cd00567 274 FATEAAREVADLAMQIHG 291
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
44-380 |
1.49e-96 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 295.95 E-value: 1.49e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 44 EEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRAsGAVG 123
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVP--REVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARA-GGSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 124 LSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDAD 203
Cdd:cd01160 78 PGLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 204 VLIVYAKTDLAAVPASrGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLE 283
Cdd:cd01160 158 VVIVVARTGGEARGAG-GISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 284 RLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGH------CTAKDC 357
Cdd:cd01160 237 RLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRldvaeaSMAKYW 316
|
330 340
....*....|....*....|...
gi 1444691839 358 AGvilysaECATQVALDGIQCFG 380
Cdd:cd01160 317 AT------ELQNRVAYECVQLHG 333
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
6-389 |
1.89e-90 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 281.83 E-value: 1.89e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 6 RLLGWRVASWRLRPPLAGFVSQRAHSLL--PvddainglSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQ 83
Cdd:PTZ00461 7 SSLGRRSATCGWTAAATMTSASRAFMDLynP--------TPEHAALRETVAKFSREVVDKHAREDDINMHFN--RDLFKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 84 LGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALA 163
Cdd:PTZ00461 77 LGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 164 MSEPNAGSDVVSMKLKAEKKGN-HYILNGNKFWITNGPDADVLIVYAKTDlaavpasRGITAFIVEKGMPGFSTSKKLDK 242
Cdd:PTZ00461 157 MSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVADVFLIYAKVD-------GKITAFVVERGTKGFTQGPKIDK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 243 LGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLM 322
Cdd:PTZ00461 230 CGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQI 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444691839 323 QGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGQTFSAQHPP 389
Cdd:PTZ00461 310 QRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMP 376
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
31-380 |
1.39e-85 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 268.95 E-value: 1.39e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 31 SLLPVDDAIN-GLSEEQRQLRQTMAKFLQEHLAP-KAQEIDrsnefKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEH 108
Cdd:cd01161 15 QVFPYPSVLTeEQTEELNMLVGPVEKFFEEVNDPaKNDQLE-----KIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 109 VLVMEEISRASGaVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKK--GNH 186
Cdd:cd01161 90 ARLAEIVGMDLG-FSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 187 YILNGNKFWITNGPDADVLIVYAKTDLAAVPASR--GITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAAN 264
Cdd:cd01161 169 YVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVkdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVEN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 265 ILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVA 344
Cdd:cd01161 249 VLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTS 328
|
330 340 350
....*....|....*....|....*....|....*...
gi 1444691839 345 KACDEGHCT--AKDCAGVILYSAECATQVALDGIQCFG 380
Cdd:cd01161 329 GNMDRGLKAeyQIEAAISKVFASEAAWLVVDEAIQIHG 366
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
42-380 |
4.07e-84 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 264.31 E-value: 4.07e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 42 LSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGA 121
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFP--VDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 122 VGlSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPD 201
Cdd:cd01162 79 TA-AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 202 ADVLIVYAKTDlaaVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLD 281
Cdd:cd01162 158 SDVYVVMARTG---GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 282 LERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTA-KDCAGV 360
Cdd:cd01162 235 GGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAvKLCAMA 314
|
330 340
....*....|....*....|
gi 1444691839 361 ILYSAECATQVALDGIQCFG 380
Cdd:cd01162 315 KRFATDECFDVANQALQLHG 334
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
42-350 |
1.44e-76 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 244.96 E-value: 1.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 42 LSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITaPVQYGGSGLGYLEHVLVMEEISRASGA 121
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFD--RKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVDSG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 122 VGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPD 201
Cdd:cd01151 90 YRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 202 ADVLIVYAKTDLAAvpasrGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENkGVYVLMSGLD 281
Cdd:cd01151 170 ADVFVVWARNDETG-----KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAE-GLRGPFKCLN 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1444691839 282 LERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEG 350
Cdd:cd01151 244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQG 312
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
42-388 |
3.87e-70 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 227.85 E-value: 3.87e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 42 LSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEIsrASGA 121
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYP--WPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEEL--AYGC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 122 VGLSYGAHSN-LCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGP 200
Cdd:cd01157 77 TGVQTAIEANsLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 201 DADVLIVYAKTDL-AAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSG 279
Cdd:cd01157 157 KANWYFLLARSDPdPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 280 LDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAG 359
Cdd:cd01157 237 FDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASI 316
|
330 340 350
....*....|....*....|....*....|
gi 1444691839 360 VILYSAECATQVALDGIQCF-GQTFSAQHP 388
Cdd:cd01157 317 AKAFAADIANQLATDAVQIFgGNGFNSEYP 346
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
42-380 |
5.81e-53 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 183.01 E-value: 5.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 42 LSEEQR----QLRQTMAK-FLQEHLApkaqEIDRSNEFKnlREFWKQLGN--LGVLGItaPVQYGGSGLGYLEHVLVMEE 114
Cdd:PRK12341 5 LTEEQElllaSIRELITRnFPEEYFR----TCDENGTYP--REFMRALADngISMLGV--PEEFGGTPADYVTQMLVLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 115 ISRASGAVglsYGAHSNLCINQLVRNGNEAQKEK-YLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNK 193
Cdd:PRK12341 77 VSKCGAPA---FLITNGQCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 194 FWITNGPDADVLIVYAKTDLAAVPASRgITAFIVEKGMPGFSTsKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGV 273
Cdd:PRK12341 154 TFITGAKEYPYMLVLARDPQPKDPKKA-FTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 274 YVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCT 353
Cdd:PRK12341 232 LNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSL 311
|
330 340
....*....|....*....|....*..
gi 1444691839 354 AKDCAGVILYSAECATQVALDGIQCFG 380
Cdd:PRK12341 312 RTSAALAKLYCARTAMEVIDDAIQIMG 338
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
43-157 |
1.69e-50 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 167.64 E-value: 1.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 43 SEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAV 122
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFP--RELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASV 78
|
90 100 110
....*....|....*....|....*....|....*
gi 1444691839 123 GLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGE 157
Cdd:pfam02771 79 ALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
42-380 |
1.13e-43 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 158.07 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 42 LSEEQR----QLRQTMAKflqEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISR 117
Cdd:PRK03354 5 LNDEQElfvaGIRELMAS---ENWEAYFAECDRDSVYP--ERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 118 ASGAVGLSYGAHSNlcINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWIT 197
Cdd:PRK03354 80 LGAPTYVLYQLPGG--FNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 198 NGPDADVLIVYAKTdlAAVPASRGITAFIVEKGMPGFSTSkKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLM 277
Cdd:PRK03354 158 SSAYTPYIVVMARD--GASPDKPVYTEWFVDMSKPGIKVT-KLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 278 SGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDC 357
Cdd:PRK03354 235 EEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDA 314
|
330 340
....*....|....*....|...
gi 1444691839 358 AGVILYSAECATQVALDGIQCFG 380
Cdd:PRK03354 315 AMCKYFCANAAFEVVDSAMQVLG 337
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
44-291 |
2.85e-41 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 151.73 E-value: 2.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 44 EEQRQLRQTMAKFLQEHLAP---KAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRAsG 120
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPelrEESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAA-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 121 AVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGP 200
Cdd:cd01152 80 APVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 201 DADVLIVYAKTDLaAVPASRGITAFIVEKGMPGFsTSKKLDKLgMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGL 280
Cdd:cd01152 160 YADWAWLLVRTDP-EAPKHRGISILLVDMDSPGV-TVRPIRSI-NGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTL 236
|
250
....*....|.
gi 1444691839 281 DLERLVLAGGP 291
Cdd:cd01152 237 NFERVSIGGSA 247
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
42-329 |
1.34e-40 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 150.39 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 42 LSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPvQYGGSGLGYLEHVLVMEEISRASGA 121
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFP--FHIIPKLGSLGIAGGTIK-GYGCPGLSITASAIATAEVARVDAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 122 VGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPD 201
Cdd:PLN02526 106 CSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 202 ADVLIVYAKTdlaavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDC------KIPAANILGHENKgvyv 275
Cdd:PLN02526 186 ADVLVIFARN-----TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVfvpdedRLPGVNSFQDTNK---- 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1444691839 276 lmsGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADM 329
Cdd:PLN02526 257 ---VLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRM 307
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
52-380 |
6.78e-36 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 137.52 E-value: 6.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 52 TMAKFLQEHLAPKAQEIDRSN-EFKNLR--------EFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAV 122
Cdd:cd01153 4 EVARLAENVLAPLNADGDREGpVFDDGRvvvpppfkEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 123 GLSYGAHSnlCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGN-HYILNGNKFWITNG-- 199
Cdd:cd01153 84 MYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGeh 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 200 --PDADVLIVYAKTDlAAVPASRGITAFIVEK----GMPGFSTSKKLD-KLGMRGSNTCELIFEDCKipaANILGHENKG 272
Cdd:cd01153 162 dmSENIVHLVLARSE-GAPPGVKGLSLFLVPKflddGERNGVTVARIEeKMGLHGSPTCELVFDNAK---GELIGEEGMG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 273 VYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQ--------KIGHFQLMQGKMADMYTRLMACRQYVYNVA 344
Cdd:cd01153 238 LAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDlikaapavTIIHHPDVRRSLMTQKAYAEGSRALDLYTA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1444691839 345 KACDEGH---------CTAKDCAGVIL-----YSAECATQVALDGIQCFG 380
Cdd:cd01153 318 TVQDLAErkategedrKALSALADLLTpvvkgFGSEAALEAVSDAIQVHG 367
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
161-256 |
2.73e-32 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 118.54 E-value: 2.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 161 ALAMSEPNAGSDVVSMKLKA-EKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvpASRGITAFIVEKGMPGFSTSKK 239
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDD--RHGGISLFLVPKDAPGVSVRRI 78
|
90
....*....|....*..
gi 1444691839 240 LDKLGMRGSNTCELIFE 256
Cdd:pfam02770 79 ETKLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
75-273 |
1.87e-26 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 112.65 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 75 KNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAV----GLSYGAhsnlcINQLVRNGNEAQKEKYL 150
Cdd:PTZ00456 99 KGFKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFsmypGLSIGA-----ANTLMAWGSEEQKEQYL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 151 PKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGN-HYILNGNKFWITNGpDAD-----VLIVYAKTDlAAVPASRGITA 224
Cdd:PTZ00456 174 TKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAG-DHDlteniVHIVLARLP-NSLPTTKGLSL 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1444691839 225 FIVEKGMP----GFSTSKKLD------KLGMRGSNTCELIFEDCKipaANILGHENKGV 273
Cdd:PTZ00456 252 FLVPRHVVkpdgSLETAKNVKciglekKMGIKGSSTCQLSFENSV---GYLIGEPNAGM 307
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
48-386 |
2.79e-25 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 107.09 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 48 QLRQTMAKFLQEHLAPKAQEIDRSNE------------FKNLREFWKQLG--NLGVlgitaPVQYGGSGLGYLEHVLVME 113
Cdd:cd01155 5 ELRARVKAFMEEHVYPAEQEFLEYYAeggdrwwtpppiIEKLKAKAKAEGlwNLFL-----PEVSGLSGLTNLEYAYLAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 114 EISR---ASGAVGLSYGAHSNLCInqLVRNGNEAQKEKYLPKLISGEYIGALAMSEPN-AGSDVVSMKLKAEKKGNHYIL 189
Cdd:cd01155 80 ETGRsffAPEVFNCQAPDTGNMEV--LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 190 NGNKFWITNG--PDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKLDKLG---MRGSNtCELIFEDCKIPAAN 264
Cdd:cd01155 158 NGRKWWSSGAgdPRCKIAIVMGRTDPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGyddAPHGH-AEITFDNVRVPASN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 265 ILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVA 344
Cdd:cd01155 237 LILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAA 316
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1444691839 345 KACDEGhcTAKDCAGVILYSAECATQVALDGIQCFGQTFSAQ 386
Cdd:cd01155 317 HMIDTV--GNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAA 356
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
270-380 |
7.93e-25 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 100.02 E-value: 7.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 270 NKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDE 349
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110
....*....|....*....|....*....|.
gi 1444691839 350 GHCTAKDCAGVILYSAECATQVALDGIQCFG 380
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHG 111
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
137-380 |
5.68e-24 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 103.60 E-value: 5.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 137 LVRNGNEAQKEkYLPKLISGEY----IGALAMSEPNAGSDVVSMKLKAEK-KGNHYILNGNKfWITNGPDADVLIVYAKT 211
Cdd:cd01154 123 LRKYGPEELKQ-YLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLARP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 212 DlAAVPASRGITAFIVEKGMP-----GFSTSKKLDKLGMRGSNTCELIFEDCKipaANILGHENKGVYVLMSGLDLERLV 286
Cdd:cd01154 201 E-GAPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDAE---AYLIGDEGKGIYYILEMLNISRLD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 287 LAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDE-GHCTAKDCAGVIL--- 362
Cdd:cd01154 277 NAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRaAADKPVEAHMARLatp 356
|
250 260
....*....|....*....|..
gi 1444691839 363 ----YSAECATQVALDGIQCFG 380
Cdd:cd01154 357 vaklIACKRAAPVTSEAMEVFG 378
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
43-325 |
1.17e-15 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 79.84 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 43 SEEQRQLRQTMAKFLQEHLAPKAQEIDR---SN-------EFKNLREFWKQLG--NL--------------------GVL 90
Cdd:PLN02876 403 SEKVLELRKKLIKFMEDHIYPMENEFYKlaqSSsrwtvhpEEERLKELAKKEGlwNLwipldsaararkllfednkhMVS 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 91 GITAPvQYGGSGLGYLEHVLVMEEISRASGAVG-LSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPN- 168
Cdd:PLN02876 483 GDSAD-QLLGAGLSNLEYGYLCEIMGRSVWAPQvFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQv 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 169 AGSDVVSMKLKAEKKGNHYILNGNKFWiTNG---PDADVLIVYAKTDLAAvPASRGITAFIVEKGMPGFSTSKKLDKLGM 245
Cdd:PLN02876 562 ASSDATNIECSIRRQGDSYVINGTKWW-TSGamdPRCRVLIVMGKTDFNA-PKHKQQSMILVDIQTPGVQIKRPLLVFGF 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 246 RGS--NTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERL----VLAGGPLGLMQAVLDHTIPylhvREAFGQKI--- 316
Cdd:PLN02876 640 DDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLhhcmRLIGAAERGMQLMVQRALS----RKAFGKLIaqh 715
|
....*....
gi 1444691839 317 GHFQLMQGK 325
Cdd:PLN02876 716 GSFLSDLAK 724
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
61-305 |
9.55e-15 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 75.82 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 61 LAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLcINQLVRN 140
Cdd:cd01163 10 IAEGAAERDRQRGLP--YEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGF-VEALLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 141 GNEAQKEKYLPKLISGEYIGAlAMSE---PNAGSDVVSMklkaEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvp 217
Cdd:cd01163 87 GPEQFRKRWFGRVLNGWIFGN-AVSErgsVRPGTFLTAT----VRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGK-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 218 asrgITAFIVEKGMPGFSTSKKLDKLGMR--GSNTceLIFEDCKIPAANILGHENKGVYVLMSGLdLERLVLAGGPLGLM 295
Cdd:cd01163 160 ----LVFAAVPTDRPGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLAAVLAGIA 232
|
250
....*....|
gi 1444691839 296 QAVLDHTIPY 305
Cdd:cd01163 233 RAALDDAVAY 242
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
67-329 |
1.92e-14 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 75.76 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 67 EIDRSNEFKNL-REFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRN-GNEA 144
Cdd:PRK13026 99 DWDIVQNRKDLpPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLGPGELLTHyGTQE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 145 QKEKYLPKLISGEYIGALAMSEPNAGSDVVSMK-----LKAEKKGNHYI---LNGNKFWITNGPDADVL----IVYAKTD 212
Cdd:PRK13026 179 QKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEVLglrLTWDKRYITLAPVATVLglafKLRDPDG 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 213 LAAVPASRGITAFIVEKGMPGFSTSKKLDKLGMR---GSNTCELIFedckIPAANILG---HENKGVYVLMSGLDLERlv 286
Cdd:PRK13026 259 LLGDKKELGITCALIPTDHPGVEIGRRHNPLGMAfmnGTTRGKDVF----IPLDWIIGgpdYAGRGWRMLVECLSAGR-- 332
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1444691839 287 laGGPLGLMQAVLDH-----TIPYLHVREAFGQKIGHFQLMQGKMADM 329
Cdd:PRK13026 333 --GISLPALGTASGHmatrtTGAYAYVRRQFGMPIGQFEGVQEALARI 378
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
79-351 |
5.85e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 71.39 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 79 EFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQ-LVRNGNEAQKEKYLPKLISGE 157
Cdd:PRK09463 113 EVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLGPGElLLHYGTDEQKDHYLPRLARGE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 158 YIGALAMSEPNAGSDVVSMK-----LKAEKKGNHYI---LNGNKFWITNGPDADVL-----------IVYAKTDLaavpa 218
Cdd:PRK09463 193 EIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLgmrLTWNKRYITLAPIATVLglafklydpdgLLGDKEDL----- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 219 srGITAFIVEKGMPGFSTSKKLDKLG---MRGSNTCELIFedckIPAANILG---HENKGVYVLMSGLDLERLV-LAGGP 291
Cdd:PRK09463 268 --GITCALIPTDTPGVEIGRRHFPLNvpfQNGPTRGKDVF----IPLDYIIGgpkMAGQGWRMLMECLSVGRGIsLPSNS 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444691839 292 LGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADM--YTRLM-ACRQYvynVAKACDEGH 351
Cdd:PRK09463 342 TGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIagNAYLMdAARTL---TTAAVDLGE 401
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
75-299 |
5.33e-11 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 64.52 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 75 KNLREFWKQLGNLGvlGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLI 154
Cdd:PTZ00457 53 EQIRSNDKILGNLY--GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 155 SGEYIGALAMSEPNaGSDVVSMKLKAEKKGN-HYILNGNKFWItNGPDADVLIVYAKT------DLAAVPASRgITAFIV 227
Cdd:PTZ00457 131 DGTIMMGWATEEGC-GSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKTltqtaaEEGATEVSR-NSFFIC 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444691839 228 EKGMPGFSTskkldklgmrgsNTCELIFEDckIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVL 299
Cdd:PTZ00457 208 AKDAKGVSV------------NGDSVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVV 265
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
156-348 |
5.23e-10 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 61.69 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 156 GEYIGaLAMSEPNAGSDVVSMKLKAEK-KGNHYILNGNKfWITNGPDADVLIVYAKTDlaavpasRGITAFIVEKGMP-G 233
Cdd:PRK11561 177 GLLIG-MGMTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAK-------GGLSCFFVPRFLPdG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 234 FSTSKKL----DKLGMRGSNTCELIFEDCkipAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVR 309
Cdd:PRK11561 248 QRNAIRLerlkDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQR 324
|
170 180 190
....*....|....*....|....*....|....*....
gi 1444691839 310 EAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACD 348
Cdd:PRK11561 325 QVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWD 363
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
112-279 |
1.16e-07 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 54.26 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 112 MEEISRASGAVGLSYGA----HSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA--EKKGN 185
Cdd:cd01150 84 MLALTNSLGGYDLSLGAklglHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 186 HYILN-----GNKFWITN-GPDADVLIVYAKTdlaAVPASR-GITAFIVE-------KGMPGFSTSKKLDKLGMRGSNTC 251
Cdd:cd01150 164 EFVINtpdftATKWWPGNlGKTATHAVVFAQL---ITPGKNhGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNG 240
|
170 180
....*....|....*....|....*...
gi 1444691839 252 ELIFEDCKIPAANILgheNKGVYVLMSG 279
Cdd:cd01150 241 FLQFRNVRIPRENLL---NRFGDVSPDG 265
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
111-329 |
1.13e-06 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 51.01 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 111 VMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA--EKKGNHYI 188
Cdd:PLN02636 126 ITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 189 LN-----GNKFWITNGP-DADVLIVYAKTDLAAvPASRGIT-----AFIV-------EKGMPGFSTSKKLDKLGMRGSNT 250
Cdd:PLN02636 206 INtpndgAIKWWIGNAAvHGKFATVFARLKLPT-HDSKGVSdmgvhAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDN 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 251 CELIFEDCKIPAANILGH----------------ENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQ 314
Cdd:PLN02636 285 GALRFRSVRIPRDNLLNRfgdvsrdgkytsslptINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGP 364
|
250 260
....*....|....*....|.
gi 1444691839 315 ------KIGHFQLMQGKMADM 329
Cdd:PLN02636 365 pkqpeiSILDYQSQQHKLMPM 385
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
141-266 |
1.99e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 47.15 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 141 GNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA--EKKGNHYILN-----GNKFWITN-GPDADVLIVYAKtd 212
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAK-- 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444691839 213 LAAVPASRGITAFIVE-------KGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANIL 266
Cdd:PTZ00460 188 LIVNGKNKGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLL 248
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
59-266 |
2.19e-04 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 43.49 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 59 EHLAPKAQEidRSNEFKNLREFWKQ----LGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVG---LSYGAHSn 131
Cdd:cd01159 4 EDLAPLIRE--RAPEAERARRLPDEvvraLREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAwvaSIVATHS- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691839 132 lciNQLVRNGNEAQKEKYlpklisGEYIGALAmsepnagSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAK- 210
Cdd:cd01159 81 ---RMLAAFPPEAQEEVW------GDGPDTLL-------AGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIv 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1444691839 211 TDLAAVPASRgitAFIVEKGmpGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANIL 266
Cdd:cd01159 145 EDDDGGPLPR---AFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTL 195
|
|
| |
