|
Name |
Accession |
Description |
Interval |
E-value |
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
44-411 |
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: 662.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 44 GLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlrvswevravggsqgvglsctaawksshsfLEFWKQLGNLGVLG 123
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFP-------------------------------RDLWRKMGKLGLLG 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 124 ITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGS 203
Cdd:cd01156 50 ITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 204 DVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTC 283
Cdd:cd01156 130 DVVSMKLRAEKKGDRYVLNGSKMWITNGPDADTLVVYAKTDPS--AGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTC 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 284 ELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYT 363
Cdd:cd01156 208 ELVFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYT 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1034590511 364 RLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCF 411
Cdd:cd01156 288 RLNASRSYLYTVAKACDRGNMDPKDAAGVILYAAEKATQVALDAIQIL 335
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
10-415 |
0e+00 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 533.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 10 LLGWRVAswRLRPPLAGFVSQRAHSLLpvddaingLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlrvswevrav 89
Cdd:PLN02519 1 MLLSAAK--ARRRGLARRFSSSSSSLL--------FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFP----------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 90 ggsqgvglsctaawksshSFLEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQL 169
Cdd:PLN02519 60 ------------------KDVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 170 VRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvp 249
Cdd:PLN02519 122 VRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAA-- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 250 ASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQA 329
Cdd:PLN02519 200 GSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 330 VLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQ 409
Cdd:PLN02519 280 CLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQ 359
|
....*.
gi 1034590511 410 CFVSRG 415
Cdd:PLN02519 360 CLGGNG 365
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
45-417 |
3.27e-137 |
|
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: 397.67 E-value: 3.27e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 45 LSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlrvswevravggsqgvglsctaawksshsfLEFWKQLGNLGVLGI 124
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFP-------------------------------RELWRKLAELGLLGL 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 125 TAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHsNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSD 204
Cdd:COG1960 54 TIPEEYGGLGLSLVELALVLEELARADASLALPVGVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 205 VVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCE 284
Cdd:COG1960 133 AAALRTTAVRDGDGYVLNGQKTFITNAPVADVILVLARTDPA--AGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 285 LIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTR 364
Cdd:COG1960 211 LFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAE 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1034590511 365 LMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFVSRGIS 417
Cdd:COG1960 291 LEAARALVYRAAWLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYT 343
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
47-411 |
6.23e-123 |
|
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: 361.20 E-value: 6.23e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 47 EEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNlrvswevravggsqgvglsctaawksshsflEFWKQLGNLGVLGITA 126
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPR-------------------------------EVIKEMAELGLMGIPI 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 127 PVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVV 206
Cdd:cd01158 50 PEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 207 SMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvpASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELI 286
Cdd:cd01158 130 ALKTTAKKDGDDYVLNGSKMWITNGGEADFYIVFAVTDPSK--GYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 287 FEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLM 366
Cdd:cd01158 208 FEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIE 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1034590511 367 ACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCF 411
Cdd:cd01158 288 AARLLTYKAARLKDNGEPFIKEAAMAKLFASEVAMRVTTDAVQIF 332
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
47-417 |
7.30e-103 |
|
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: 308.06 E-value: 7.30e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 47 EEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFknlrvswevravggsqgvglsctaawksshsFLEFWKQLGNLGVlgita 126
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEE-------------------------------PWELLAELGLLLG----- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 127 pvqyggsglgylehvlvmeeisrasgavglsygahsnlcINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVV 206
Cdd:cd00567 45 ---------------------------------------AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLA 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 207 SMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELI 286
Cdd:cd00567 86 GIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEEG-PGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 287 FEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLM 366
Cdd:cd00567 165 FDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELE 244
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1034590511 367 ACRQYVYNVAKACDEGHC-TAKDCAGVILYSAECATQVALDGIQCFVSRGIS 417
Cdd:cd00567 245 AARLLLYRAAWLLDQGPDeARLEAAMAKLFATEAAREVADLAMQIHGGRGYS 296
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
47-402 |
4.25e-89 |
|
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: 274.76 E-value: 4.25e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 47 EEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNlrvswevravggsqgvglsctaawksshsflEFWKQLGNLGVLGITA 126
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPR-------------------------------EVWRKAGEQGLLGVGF 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 127 PVQYGGSGLGYLEHVLVMEEISRAsGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVV 206
Cdd:cd01160 50 PEEYGGIGGDLLSAAVLWEELARA-GGSGPGLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 207 SMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASrGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELI 286
Cdd:cd01160 129 GIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGGEARGAG-GISLFLVERGTPGFSRGRKLKKMGWKAQDTAELF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 287 FEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLM 366
Cdd:cd01160 208 FDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVA 287
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1034590511 367 ACRQYVYNVAKACDEGH------CTAKDCAGVILysAECATQ 402
Cdd:cd01160 288 VTRAFLDNCAWRHEQGRldvaeaSMAKYWATELQ--NRVAYE 327
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
9-417 |
1.71e-83 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 261.41 E-value: 1.71e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 9 RLLGWRVASWRLRPPLAGFVSQRAHSLL--PvddainglSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNlrvswev 86
Cdd:PTZ00461 7 SSLGRRSATCGWTAAATMTSASRAFMDLynP--------TPEHAALRETVAKFSREVVDKHAREDDINMHFNR------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 87 ravggsqgvglsctaawksshsflEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCI 166
Cdd:PTZ00461 72 ------------------------DLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSMLFV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 167 NQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGN-HYILNGNKFWITNGPDADVLIVYAKTDl 245
Cdd:PTZ00461 128 NNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVADVFLIYAKVD- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 246 aavpasRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLG 325
Cdd:PTZ00461 207 ------GKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 326 LMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVAL 405
Cdd:PTZ00461 281 IAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAKKVAD 360
|
410
....*....|..
gi 1034590511 406 DGIQCFVSRGIS 417
Cdd:PTZ00461 361 SAIQVMGGMGYS 372
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
114-409 |
7.69e-83 |
|
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: 259.71 E-value: 7.69e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 114 KQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGaVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGA 193
Cdd:cd01161 63 TQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLG-FSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 194 LAMSEPNAGSDVVSMKLKAEKK--GNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASR--GITAFIVEKGMPGFSTS 269
Cdd:cd01161 142 FALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVkdKITAFIVERSFGGVTNG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 270 KKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIG 349
Cdd:cd01161 222 PPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIH 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034590511 350 HFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCT--AKDCAGVILYSAECATQVALDGIQ 409
Cdd:cd01161 302 EFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAeyQIEAAISKVFASEAAWLVVDEAIQ 363
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
45-411 |
2.04e-78 |
|
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: 247.36 E-value: 2.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 45 LSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKnlrvswevravggsqgvglsctaawksshsfLEFWKQLGNLGVLGI 124
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFP-------------------------------VDVLRKAAELGFGGI 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 125 TAPVQYGGSGLGYLEHVLVMEEISRASGAVGlSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSD 204
Cdd:cd01162 50 YIRDDVGGSGLSRLDASIIFEALSTGCVSTA-AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 205 VVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDlaaVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCE 284
Cdd:cd01162 129 AAALRTRAVREGDHYVLNGSKAFISGAGDSDVYVVMARTG---GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 285 LIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTR 364
Cdd:cd01162 206 VIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATE 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1034590511 365 LMACRQYVYNVAKACDEGHCTA-KDCAGVILYSAECATQVALDGIQCF 411
Cdd:cd01162 286 LVASRLMVRRAASALDRGDPDAvKLCAMAKRFATDECFDVANQALQLH 333
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
45-382 |
2.73e-74 |
|
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: 236.87 E-value: 2.73e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 45 LSEEQRQLRQTMAKFLQEHLAPkaqeidrsnefknlRVswevravggsqgvglscTAAWKSSHSFLEFWKQLGNLGVLGI 124
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAP--------------RV-----------------LEAYREEKFDRKIIEEMGELGLLGA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 125 TaPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSD 204
Cdd:cd01151 62 T-IKGYGCAGLSSVAYGLIAREVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 205 VVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvpasrGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCE 284
Cdd:cd01151 141 PGGMETRARKDGGGYKLNGSKTWITNSPIADVFVVWARNDETG-----KIRGFILERGMKGLSAPKIQGKFSLRASITGE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 285 LIFEDCKIPAANILGHENkGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTR 364
Cdd:cd01151 216 IVMDNVFVPEENLLPGAE-GLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTE 294
|
330
....*....|....*...
gi 1034590511 365 LMACRQYVYNVAKACDEG 382
Cdd:cd01151 295 IALGLLACLRVGRLKDQG 312
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
45-418 |
1.87e-65 |
|
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: 213.99 E-value: 1.87e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 45 LSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFknlrvSWEVravggsqgvglsCTAAWKsshsflefwkqlgnLGVLGI 124
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEY-----PWPL------------IKRAWE--------------LGLMNT 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 125 TAPVQYGGSGLGYLEHVLVMEEIsrASGAVGLSYGAHSN-LCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGS 203
Cdd:cd01157 50 HIPEDCGGLGLGTFDTCLITEEL--AYGCTGVQTAIEANsLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 204 DVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDL-AAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNT 282
Cdd:cd01157 128 DVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPdPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 283 CELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMY 362
Cdd:cd01157 208 RGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMA 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034590511 363 TRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFVSRGISS 418
Cdd:cd01157 288 MKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNGFNS 343
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
103-411 |
2.60e-50 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 174.15 E-value: 2.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 103 WKSSHSF-LEFWKQLGN--LGVLGItaPVQYGGSGLGYLEHVLVMEEISRASGAVglsYGAHSNLCINQLVRNGNEAQKE 179
Cdd:PRK12341 32 CDENGTYpREFMRALADngISMLGV--PEEFGGTPADYVTQMLVLEEVSKCGAPA---FLITNGQCIHSMRRFGSAEQLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 180 K-YLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASRgITAFI 258
Cdd:PRK12341 107 KtAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLARDPQPKDPKKA-FTLWW 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 259 VEKGMPGFSTsKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYL 338
Cdd:PRK12341 186 VDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYA 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034590511 339 HVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCF 411
Cdd:PRK12341 265 NQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVIDDAIQIM 337
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
46-189 |
1.04e-45 |
|
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: 153.39 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 46 SEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFknlrvswevravggsqgvglsctaawksshsFLEFWKQLGNLGVLGIT 125
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEF-------------------------------PRELWKKLGELGLLGIT 49
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034590511 126 APVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGE 189
Cdd:pfam02771 50 IPEEYGGAGLDYLAYALVAEELARADASVALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
112-418 |
1.46e-42 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 153.45 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 112 FWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNlcINQLVRNGNEAQKEKYLPKLISGEYI 191
Cdd:PRK03354 42 FVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVLYQLPGG--FNTFLREGTQEQIDKIMAFRGTGKQM 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 192 GALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTdlAAVPASRGITAFIVEKGMPGFSTSkK 271
Cdd:PRK03354 120 WNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARD--GASPDKPVYTEWFVDMSKPGIKVT-K 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 272 LDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHF 351
Cdd:PRK03354 197 LEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRF 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034590511 352 QLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFVSRGISS 418
Cdd:PRK03354 277 QLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAG 343
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
110-323 |
9.14e-39 |
|
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: 143.26 E-value: 9.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 110 LEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRAsGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGE 189
Cdd:cd01152 38 RRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAA-GAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 190 YIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLaAVPASRGITAFIVEKGMPGFsTS 269
Cdd:cd01152 117 EIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDP-EAPKHRGISILLVDMDSPGV-TV 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034590511 270 KKLDKLgMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGP 323
Cdd:cd01152 195 RPIRSI-NGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSA 247
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
45-361 |
3.89e-38 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 142.30 E-value: 3.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 45 LSEEQRQLRQTMAKFLQEHLAPKAQEIdrsnefknlrvsWEvravggsqgvglsctaawKSSHSFlEFWKQLGNLGVLGI 124
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEY------------WE------------------KAEFPF-HIIPKLGSLGIAGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 125 TAPvQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSD 204
Cdd:PLN02526 78 TIK-GYGCPGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 205 VVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTdlaavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCE 284
Cdd:PLN02526 157 ASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFARN-----TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 285 LIFEDC------KIPAANILGHENKgvyvlmsGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKM 358
Cdd:PLN02526 232 IVLKDVfvpdedRLPGVNSFQDTNK-------VLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKL 304
|
...
gi 1034590511 359 ADM 361
Cdd:PLN02526 305 VRM 307
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
109-388 |
3.37e-35 |
|
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: 134.44 E-value: 3.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 109 FLEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSnlCINQLVRNGNEAQKEKYLPKLISG 188
Cdd:cd01153 38 FKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQG--AAATLLAHGTEAQREKWIPRLAEG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 189 EYIGALAMSEPNAGSDVVSMKLKAEKKGN-HYILNGNKFWITNG----PDADVLIVYAKTDlAAVPASRGITAFIVEK-- 261
Cdd:cd01153 116 EWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGehdmSENIVHLVLARSE-GAPPGVKGLSLFLVPKfl 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 262 --GMPGFSTSKKLD-KLGMRGSNTCELIFEDCKipaANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYL 338
Cdd:cd01153 195 ddGERNGVTVARIEeKMGLHGSPTCELVFDNAK---GELIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYA 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034590511 339 HVREAFGQ--------KIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKD 388
Cdd:cd01153 272 KERKQGGDlikaapavTIIHHPDVRRSLMTQKAYAEGSRALDLYTATVQDLAERKATE 329
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
193-288 |
1.15e-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: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 193 ALAMSEPNAGSDVVSMKLKA-EKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvpASRGITAFIVEKGMPGFSTSKK 271
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDD--RHGGISLFLVPKDAPGVSVRRI 78
|
90
....*....|....*..
gi 1034590511 272 LDKLGMRGSNTCELIFE 288
Cdd:pfam02770 79 ETKLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
109-305 |
3.14e-26 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 111.11 E-value: 3.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 109 FLEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAV----GLSYGAhsnlcINQLVRNGNEAQKEKYLPK 184
Cdd:PTZ00456 101 FKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFsmypGLSIGA-----ANTLMAWGSEEQKEQYLTK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 185 LISGEYIGALAMSEPNAGSDVVSMKLKAEKKGN-HYILNGNKFWITNGpDAD-----VLIVYAKTDlAAVPASRGITAFI 258
Cdd:PTZ00456 176 LVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAG-DHDlteniVHIVLARLP-NSLPTTKGLSLFL 253
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034590511 259 VEKGMP----GFSTSKKLD------KLGMRGSNTCELIFEDCKipaANILGHENKGV 305
Cdd:PTZ00456 254 VPRHVVkpdgSLETAKNVKciglekKMGIKGSSTCQLSFENSV---GYLIGEPNAGM 307
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
51-418 |
5.84e-26 |
|
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: 108.25 E-value: 5.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 51 QLRQTMAKFLQEHLAPKAQEIDrsnefknlrvswEVRAVGGSqgvglsctaAWKSSHSFLEFWKQLGN-LGVLGITAPVQ 129
Cdd:cd01155 5 ELRARVKAFMEEHVYPAEQEFL------------EYYAEGGD---------RWWTPPPIIEKLKAKAKaEGLWNLFLPEV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 130 YGGSGLGYLEHVLVMEEISR---ASGAVGLSYGAHSNLCInqLVRNGNEAQKEKYLPKLISGEYIGALAMSEPN-AGSDV 205
Cdd:cd01155 64 SGLSGLTNLEYAYLAEETGRsffAPEVFNCQAPDTGNMEV--LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 206 VSMKLKAEKKGNHYILNGNKFWITNG--PDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKLDKLG---MRGS 280
Cdd:cd01155 142 TNIECSIERDGDDYVINGRKWWSSGAgdPRCKIAIVMGRTDPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGyddAPHG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 281 NtCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMAD 360
Cdd:cd01155 222 H-AEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAK 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034590511 361 MYTRLMACRQYVYNVAKACDEGhcTAKDCAGVILYSAECATQVALD----GIQCFVSRGISS 418
Cdd:cd01155 301 SRIEIEQARLLVLKAAHMIDTV--GNKAARKEIAMIKVAAPRMALKiidrAIQVHGAAGVSQ 360
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
302-417 |
1.51e-23 |
|
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: 95.78 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 302 NKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDE 381
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1034590511 382 GHCTAKDCAGVILYSAECATQVALDGIQCFVSRGIS 417
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYL 116
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
169-361 |
4.60e-23 |
|
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: 100.14 E-value: 4.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 169 LVRNGNEAQKEkYLPKLISGEY----IGALAMSEPNAGSDVVSMKLKAEK-KGNHYILNGNKfWITNGPDADVLIVYAKT 243
Cdd:cd01154 123 LRKYGPEELKQ-YLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLARP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 244 DlAAVPASRGITAFIVEKGMP-----GFSTSKKLDKLGMRGSNTCELIFEDCKipaANILGHENKGVYVLMSGLDLERLV 318
Cdd:cd01154 201 E-GAPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDAE---AYLIGDEGKGIYYILEMLNISRLD 276
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034590511 319 LAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADM 361
Cdd:cd01154 277 NAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEM 319
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
46-357 |
5.41e-16 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 80.22 E-value: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 46 SEEQRQLRQTMAKFLQEHLAPKaqeidrSNEFKNLRVS---WEV-------RAVGGSQGVG---LSCTAAWKSSHSFLEF 112
Cdd:PLN02876 403 SEKVLELRKKLIKFMEDHIYPM------ENEFYKLAQSssrWTVhpeeerlKELAKKEGLWnlwIPLDSAARARKLLFED 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 113 WKQlgnlGVLGITAPvQYGGSGLGYLEHVLVMEEISRASGAVG-LSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYI 191
Cdd:PLN02876 477 NKH----MVSGDSAD-QLLGAGLSNLEYGYLCEIMGRSVWAPQvFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIR 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 192 GALAMSEPN-AGSDVVSMKLKAEKKGNHYILNGNKFWiTNG---PDADVLIVYAKTDLAAvPASRGITAFIVEKGMPGFS 267
Cdd:PLN02876 552 SGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWW-TSGamdPRCRVLIVMGKTDFNA-PKHKQQSMILVDIQTPGVQ 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 268 TSKKLDKLGMRGS--NTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERL----VLAGGPLGLMQAVLDHTIPylhvR 341
Cdd:PLN02876 630 IKRPLLVFGFDDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLhhcmRLIGAAERGMQLMVQRALS----R 705
|
330
....*....|....*....
gi 1034590511 342 EAFGQKI---GHFQLMQGK 357
Cdd:PLN02876 706 KAFGKLIaqhGSFLSDLAK 724
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
111-361 |
1.87e-14 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 75.38 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 111 EFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRN-GNEAQKEKYLPKLISGE 189
Cdd:PRK13026 112 EVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLGPGELLTHyGTQEQKDYWLPRLADGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 190 YIGALAMSEPNAGSDVVSMK-----LKAEKKGNHYI---LNGNKFWITNGPDADVL----IVYAKTDLAAVPASRGITAF 257
Cdd:PRK13026 192 EIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEVLglrLTWDKRYITLAPVATVLglafKLRDPDGLLGDKKELGITCA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 258 IVEKGMPGFSTSKKLDKLGMR---GSNTCELIFedckIPAANILG---HENKGVYVLMSGLDLERlvlaGGPLGLMQAVL 331
Cdd:PRK13026 272 LIPTDHPGVEIGRRHNPLGMAfmnGTTRGKDVF----IPLDWIIGgpdYAGRGWRMLVECLSAGR----GISLPALGTAS 343
|
250 260 270
....*....|....*....|....*....|....*
gi 1034590511 332 DH-----TIPYLHVREAFGQKIGHFQLMQGKMADM 361
Cdd:PRK13026 344 GHmatrtTGAYAYVRRQFGMPIGQFEGVQEALARI 378
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
107-337 |
1.02e-13 |
|
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: 71.97 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 107 HSFLEFWKQLGnlgVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLcINQLVRNGNEAQKEKYLPKLI 186
Cdd:cd01163 25 YEEVALLRQSG---LGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGF-VEALLLAGPEQFRKRWFGRVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 187 SGEYIGAlAMSE---PNAGSDVVSMklkaEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvpasrgITAFIVEKGM 263
Cdd:cd01163 101 NGWIFGN-AVSErgsVRPGTFLTAT----VRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGK------LVFAAVPTDR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034590511 264 PGFSTSKKLDKLGMR--GSNTceLIFEDCKIPAANILGHENKGVYVLMSGLdLERLVLAGGPLGLMQAVLDHTIPY 337
Cdd:cd01163 170 PGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLAAVLAGIARAALDDAVAY 242
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
103-383 |
3.14e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 71.39 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 103 WKSSHSF----LEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQ-LVRNGNEAQ 177
Cdd:PRK09463 101 WQITHELadlpPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLGPGElLLHYGTDEQ 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 178 KEKYLPKLISGEYIGALAMSEPNAGSDVVSMK-----LKAEKKGNHYI---LNGNKFWITNGPDADVL-----------I 238
Cdd:PRK09463 181 KDHYLPRLARGEEIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLgmrLTWNKRYITLAPIATVLglafklydpdgL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 239 VYAKTDLaavpasrGITAFIVEKGMPGFSTSKKLDKLG---MRGSNTCELIFedckIPAANILG---HENKGVYVLMSGL 312
Cdd:PRK09463 261 LGDKEDL-------GITCALIPTDTPGVEIGRRHFPLNvpfQNGPTRGKDVF----IPLDYIIGgpkMAGQGWRMLMECL 329
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034590511 313 DLERLV-LAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADM--YTRLM-ACRQYvynVAKACDEGH 383
Cdd:PRK09463 330 SVGRGIsLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIagNAYLMdAARTL---TTAAVDLGE 401
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
114-331 |
1.12e-10 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 63.36 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 114 KQLGNLGvlGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGA 193
Cdd:PTZ00457 60 KILGNLY--GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 194 LAMSEPNaGSDVVSMKLKAEKKGN-HYILNGNKFWItNGPDADVLIVYAKT------DLAAVPASRgITAFIVEKGMPGF 266
Cdd:PTZ00457 138 WATEEGC-GSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKTltqtaaEEGATEVSR-NSFFICAKDAKGV 214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034590511 267 STskkldklgmrgsNTCELIFEDckIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVL 331
Cdd:PTZ00457 215 SV------------NGDSVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVV 265
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
188-380 |
2.24e-10 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 62.46 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 188 GEYIGaLAMSEPNAGSDVVSMKLKAEK-KGNHYILNGNKfWITNGPDADVLIVYAKTDlaavpasRGITAFIVEKGMP-G 265
Cdd:PRK11561 177 GLLIG-MGMTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAK-------GGLSCFFVPRFLPdG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 266 FSTSKKL----DKLGMRGSNTCELIFEDCkipAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVR 341
Cdd:PRK11561 248 QRNAIRLerlkDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQR 324
|
170 180 190
....*....|....*....|....*....|....*....
gi 1034590511 342 EAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACD 380
Cdd:PRK11561 325 QVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWD 363
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
144-311 |
8.07e-08 |
|
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: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 144 MEEISRASGAVGLSYGA----HSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA--EKKGN 217
Cdd:cd01150 84 MLALTNSLGGYDLSLGAklglHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 218 HYILN-----GNKFWITN-GPDADVLIVYAKTdlaAVPASR-GITAFIVE-------KGMPGFSTSKKLDKLGMRGSNTC 283
Cdd:cd01150 164 EFVINtpdftATKWWPGNlGKTATHAVVFAQL---ITPGKNhGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNG 240
|
170 180
....*....|....*....|....*...
gi 1034590511 284 ELIFEDCKIPAANILgheNKGVYVLMSG 311
Cdd:cd01150 241 FLQFRNVRIPRENLL---NRFGDVSPDG 265
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
143-361 |
7.06e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 51.40 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 143 VMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA--EKKGNHYI 220
Cdd:PLN02636 126 ITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 221 LN-----GNKFWITNGP-DADVLIVYAKTDLAAvPASRGIT-----AFIV-------EKGMPGFSTSKKLDKLGMRGSNT 282
Cdd:PLN02636 206 INtpndgAIKWWIGNAAvHGKFATVFARLKLPT-HDSKGVSdmgvhAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDN 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 283 CELIFEDCKIPAANILGH----------------ENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQ 346
Cdd:PLN02636 285 GALRFRSVRIPRDNLLNRfgdvsrdgkytsslptINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGP 364
|
250 260
....*....|....*....|.
gi 1034590511 347 ------KIGHFQLMQGKMADM 361
Cdd:PLN02636 365 pkqpeiSILDYQSQQHKLMPM 385
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
173-298 |
1.56e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 47.15 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 173 GNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA--EKKGNHYILN-----GNKFWITN-GPDADVLIVYAKtd 244
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAK-- 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034590511 245 LAAVPASRGITAFIVE-------KGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANIL 298
Cdd:PTZ00460 188 LIVNGKNKGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLL 248
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
127-298 |
8.20e-03 |
|
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: 38.10 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 127 PVQYGGSGLGYLEHVLVMEEISRASGAVG---LSYGAHSnlciNQLVRNGNEAQKEKYlpklisGEYIGALAmsepnagS 203
Cdd:cd01159 42 PKRYGGLEGDFAEFAEAIATLAEACGSAAwvaSIVATHS----RMLAAFPPEAQEEVW------GDGPDTLL-------A 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034590511 204 DVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAK-TDLAAVPASRgitAFIVEKGmpGFSTSKKLDKLGMRGSNT 282
Cdd:cd01159 105 GSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIvEDDDGGPLPR---AFVVPRA--EYEIVDTWHVVGLRGTGS 179
|
170
....*....|....*.
gi 1034590511 283 CELIFEDCKIPAANIL 298
Cdd:cd01159 180 NTVVVDDVFVPEHRTL 195
|
|
|