|
Name |
Accession |
Description |
Interval |
E-value |
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
48-434 |
0e+00 |
|
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: 733.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 48 FDWKDPLILEEQLTADEKLIRDTFRNYWQERLMSQILLANRNEVFHRDIVYEMGELGVLGPTIKGYGCAGVSSVAYGLLT 127
Cdd:cd01151 1 FNWEDPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGYGCAGLSSVAYGLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 128 RELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARhnPSNQSYTLS 207
Cdd:cd01151 81 REVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRAR--KDGGGYKLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 208 GTKTWITNSPVADLFIVWARC-EDNCIPGFILEKGMRGSSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVSSLAGP 286
Cdd:cd01151 159 GSKTWITNSPIADVFVVWARNdETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 287 FGCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEM 366
Cdd:cd01151 239 FKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQ 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439521 367 VSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITGIQAF 434
Cdd:cd01151 319 ISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
59-430 |
4.54e-123 |
|
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: 362.62 E-value: 4.54e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 59 QLTADEKLIRDTFRNYWQERLMSQILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGY 137
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIpEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 138 RSMMSVQSSlVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARhnPSNQSYTLSGTKTWITNSP 217
Cdd:COG1960 84 ALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV--RDGDGYVLNGQKTFITNAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 218 VADLFIVWARCEDNC----IPGFILEKGMRGSSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVS-SLAGPFGCLNT 292
Cdd:COG1960 161 VADVILVLARTDPAAghrgISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGkGFKIAMSTLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 293 ARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSMLKR 372
Cdd:COG1960 241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1439521 373 NNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITG 430
Cdd:COG1960 321 FATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
65-426 |
1.64e-92 |
|
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: 282.64 E-value: 1.64e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 65 KLIRDTFRNYWQERLMSQILLANRNEVFHRDIVYEMGELGVlgptikgygcagvssvayglltrelervdsgyrsmmsvq 144
Cdd:cd00567 4 RELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLG--------------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 145 sslvMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARhnPSNQSYTLSGTKTWITNSPVADLFIV 224
Cdd:cd00567 45 ----AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTAR--KDGDGYVLNGRKIFISNGGDADLFIV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 225 WARCEDN-----CIPGFILEKGMRGSSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNV-SSLAGPFGCLNTARYGIT 298
Cdd:cd00567 119 LARTDEEgpghrGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEgGGFELAMKGLNVGRLLLA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 299 WGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKA-TPEMVSMLKRNNCGK 377
Cdd:cd00567 199 AVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKLFATEA 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1439521 378 ALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGR 426
Cdd:cd00567 279 AREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
56-434 |
4.21e-89 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 276.73 E-value: 4.21e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 56 LEEQLTADEKLIRDTFRNYwQERLMSQILLANRNEV---FHrdIVYEMGELGVLGPTIKGYGCAGVSSVAYGLLTRELER 132
Cdd:PLN02526 25 FDDLLTPEEQALRKRVREC-MEKEVAPIMTEYWEKAefpFH--IIPKLGSLGIAGGTIKGYGCPGLSITASAIATAEVAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 133 VDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSnqSYTLSGTKTW 212
Cdd:PLN02526 102 VDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEG--GWILNGQKRW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 213 ITNSPVADLFIVWAR-CEDNCIPGFILEKGMRGSSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVSSLAGPFGCLN 291
Cdd:PLN02526 180 IGNSTFADVLVIFARnTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSFQDTNKVLA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 292 TARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSMLK 371
Cdd:PLN02526 260 VSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGK 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439521 372 RNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITGIQAF 434
Cdd:PLN02526 340 AWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIASF 402
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
63-428 |
2.80e-86 |
|
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: 267.98 E-value: 2.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 63 DEKLIRDTFRNYWQERLMSQILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYRSMM 141
Cdd:cd01158 2 EHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIpEEYGGAGLDFLAYAIAIEELAKVDASVAVIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 142 SVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSNqsYTLSGTKTWITNSPVADL 221
Cdd:cd01158 82 SVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDD--YVLNGSKMWITNGGEADF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 222 FIVWARCED----NCIPGFILEKGMRGSSAPRIEGKFSLRASATGMIIMDSVEVPEENVLpnvsslaGPFG--------C 289
Cdd:cd01158 160 YIVFAVTDPskgyRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENIL-------GEEGegfkiamqT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 290 LNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSM 369
Cdd:cd01158 233 LDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAM 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1439521 370 LKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 428
Cdd:cd01158 313 AKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
60-428 |
1.51e-66 |
|
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: 217.28 E-value: 1.51e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 60 LTADEKLIRDTFRNYWQERLMSQILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYR 138
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITApEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 139 SMMSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARHNpsNQSYTLSGTKTWITNSPV 218
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKK--GDRYVLNGSKMWITNGPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 219 ADLFIVWARCEDNC----IPGFILEKGMRG-SSAPRIEgKFSLRASATGMIIMDSVEVPEENVLPNVSS-----LAGpfg 288
Cdd:cd01156 160 ADTLVVYAKTDPSAgahgITAFIVEKGMPGfSRAQKLD-KLGMRGSNTCELVFEDCEVPEENILGGENKgvyvlMSG--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 289 cLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEitlgLHACLQL----GRLKDQDKATP 364
Cdd:cd01156 236 -LDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTR----LNASRSYlytvAKACDRGNMDP 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1439521 365 EMVSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHamnLEAVNTYE---GTHDIHALILGRAI 428
Cdd:cd01156 311 KDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRL---LRDAKLYEigaGTSEIRRMVIGREL 374
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
38-432 |
1.53e-63 |
|
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: 210.40 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 38 IRPAKSSRPVFdwKDPLILEEQLTADEKLIRDTFrnywqERLMSQILLANRN---EVFHRDIVYEMGELGVLGPTI-KGY 113
Cdd:cd01161 7 FLGDIVTKQVF--PYPSVLTEEQTEELNMLVGPV-----EKFFEEVNDPAKNdqlEKIPRKTLTQLKELGLFGLQVpEEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 114 GCAGVSSVAYGLLTrELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMET 193
Cdd:cd01161 80 GGLGLNNTQYARLA-EIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 194 RARHNPSNQSYTLSGTKTWITNSPVADLFIVWARCEDNCIPG--------FILEKGMRGSSAPRIEGKFSLRASATGMII 265
Cdd:cd01161 159 TAVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGsvkdkitaFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 266 MDSVEVPEENVLPNVSS---LAgpFGCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTE 342
Cdd:cd01161 239 FEDVKIPVENVLGEVGDgfkVA--MNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAIL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 343 ITLGLHACLQLGRLKDQD-KATPEMVSMLKRNNCGKALD-IARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIH 420
Cdd:cd01161 317 QYATESMAYMTSGNMDRGlKAEYQIEAAISKVFASEAAWlVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEIL 396
|
410
....*....|..
gi 1439521 421 ALILgrAITGIQ 432
Cdd:cd01161 397 RLFI--ALTGLQ 406
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
62-428 |
2.65e-52 |
|
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: 179.62 E-value: 2.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 62 ADEKLIRDTFRNYWQERLMSQILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVdSGYRSM 140
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFpEEYGGIGGDLLSAAVLWEELARA-GGSGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 141 MSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSNqsYTLSGTKTWITNSPVAD 220
Cdd:cd01160 80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDH--YVLNGSKTFITNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 221 LFIVWARCEDNCIPG-----FILEKGMRGSSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVS-SLAGPFGCLNTAR 294
Cdd:cd01160 158 VVIVVARTGGEARGAggislFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENkGFYYLMQNLPQER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 295 YGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLG---LHACLQLGRLKDQDKATpemVSMLK 371
Cdd:cd01160 238 LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTrafLDNCAWRHEQGRLDVAE---ASMAK 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1439521 372 rNNCGKALD-IARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 428
Cdd:cd01160 315 -YWATELQNrVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
60-430 |
2.43e-50 |
|
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: 174.55 E-value: 2.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 60 LTADEKLIRDTFRNYWQERLMSQILLANRNEVFHRDIVYEMGELGVLGPTIKG-YGCAGVSSVAYGLLTRELERVDSGYR 138
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDdVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 139 SMMSVQSsLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARHnpSNQSYTLSGTKTWITNSPV 218
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVR--EGDHYVLNGSKAFISGAGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 219 ADLFIVWARCEDN---CIPGFILEKGMRGSSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPN-----VSSLAGpfgcL 290
Cdd:cd01162 158 SDVYVVMARTGGEgpkGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGegqgfGIAMAG----L 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 291 NTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEIT----LGLHACLQLGRlKDQDKAtpEM 366
Cdd:cd01162 234 NGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVasrlMVRRAASALDR-GDPDAV--KL 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439521 367 VSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITG 430
Cdd:cd01162 311 CAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
60-430 |
2.43e-47 |
|
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: 166.99 E-value: 2.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 60 LTADEKLIRDTFRNYWQERLMSQILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYR 138
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIpEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 139 SMMSVqSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARHNpsNQSYTLSGTKTWITNSPV 218
Cdd:cd01157 81 TAIEA-NSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKK--GDEYIINGQKMWITNGGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 219 ADLFIVWARCEDN-------CIPGFILEKGMRGSSAPRIEGKFSLRASATGMIIMDSVEVPEENVLpnVSSLAG---PFG 288
Cdd:cd01157 158 ANWYFLLARSDPDpkcpaskAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVL--IGEGAGfkiAMG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 289 CLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVS 368
Cdd:cd01157 236 AFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYAS 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439521 369 MLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITG 430
Cdd:cd01157 316 IAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
3-342 |
1.26e-45 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 163.18 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 3 LRGVSAQLLSRRSGlrfprfPRTWSSAAAHTektqirpaKSSRPVFDWKDPlileeqlTADEKLIRDTFRNYWQERLMSQ 82
Cdd:PTZ00461 1 MRRVLQSSLGRRSA------TCGWTAAATMT--------SASRAFMDLYNP-------TPEHAALRETVAKFSREVVDKH 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 83 ILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQR 161
Cdd:PTZ00461 60 AREDDINMHFNRDLFKQLGDLGVMGVTVpEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 162 QKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARHNpSNQSYTLSGTKTWITNSPVADLFIVWARCeDNCIPGFILEKG 241
Cdd:PTZ00461 140 ARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD-SNGNYVLNGSKIWITNGTVADVFLIYAKV-DGKITAFVVERG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 242 MRG-SSAPRIEgKFSLRASATGMIIMDSVEVPEENVL-PNVSSLAGPFGCLNTARYGITWGVLGAAEFCLHTARQYALDR 319
Cdd:PTZ00461 218 TKGfTQGPKID-KCGMRASHMCQLFFEDVVVPAENLLgEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASER 296
|
330 340
....*....|....*....|...
gi 1439521 320 IQFGVPLARNQLVQKKLADMLTE 342
Cdd:PTZ00461 297 KAFGKPISNFGQIQRYIAEGYAD 319
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
68-426 |
7.75e-45 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 160.81 E-value: 7.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 68 RDTFRNYWQERLMSQILLANRNEVFHRDIVY--EMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYRSMMSVQ 144
Cdd:PLN02519 34 KESVQQFAQENIAPHAAAIDATNSFPKDVNLwkLMGDFNLHGITApEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 145 SSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRArhNPSNQSYTLSGTKTWITNSPVADLFIV 224
Cdd:PLN02519 114 SNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKA--ERVDGGYVLNGNKMWCTNGPVAQTLVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 225 WARCEDNC----IPGFILEKGMRGSSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVS-SLAGPFGCLNTARYGITW 299
Cdd:PLN02519 192 YAKTDVAAgskgITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGkGVYVMMSGLDLERLVLAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 300 GVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSMLKRNNCGKAL 379
Cdd:PLN02519 272 GPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERAT 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1439521 380 DIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGR 426
Cdd:PLN02519 352 QVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGR 398
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
61-172 |
4.05e-38 |
|
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: 134.13 E-value: 4.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 61 TADEKLIRDTFRNYWQERLMSQILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYRS 139
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIpEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 1439521 140 MMSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGE 172
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
152-429 |
7.03e-28 |
|
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: 114.41 E-value: 7.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 152 IYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARHNpSNQSYTLSGTKTWITN--SPVAD--LFIVWAR 227
Cdd:cd01153 96 LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQ-ADGSWRINGVKRFISAgeHDMSEniVHLVLAR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 228 CEDnCIPG------FILEK----GMR-GSSAPRIEGKFSLRASATGMIIMDSVEVP---EENvlpnvSSLAGPFGCLNTA 293
Cdd:cd01153 175 SEG-APPGvkglslFLVPKflddGERnGVTVARIEEKMGLHGSPTCELVFDNAKGEligEEG-----MGLAQMFAMMNGA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 294 RYGITWGVLGAAEFCLHTARQYALDRIQFGVPLA-------------RNQLVQKKL-------ADM--LTEITLGLHACL 351
Cdd:cd01153 249 RLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKaapavtiihhpdvRRSLMTQKAyaegsraLDLytATVQDLAERKAT 328
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439521 352 QLGRLKDQDKATPEMVSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHAL-ILGRAIT 429
Cdd:cd01153 329 EGEDRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALdLIGRKIV 407
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
288-428 |
1.44e-27 |
|
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: 106.95 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 288 GCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMV 367
Cdd:pfam00441 9 ETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGAEA 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439521 368 SMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 428
Cdd:pfam00441 89 SMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
146-428 |
7.39e-25 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 105.20 E-value: 7.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 146 SLVMHPIYTYGSEEQ-RQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARHNpsNQSYTLSGTKTWITNSPVADLFIV 224
Cdd:PRK12341 90 GQCIHSMRRFGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRK--NGKVYLNGQKTFITGAKEYPYMLV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 225 WARCEDNCIPGFILEKGMRGSSAPRIE----GKFSLRASATGMIIMDSVEVPEE-----------NVLPNvsslagpfgc 289
Cdd:PRK12341 168 LARDPQPKDPKKAFTLWWVDSSKPGIKinplHKIGWHMLSTCEVYLDNVEVEESdlvgeegmgflNVMYN---------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 290 LNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEI----TLGLHACLQlgrlKDQDKATPE 365
Cdd:PRK12341 238 FEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIenmrNMVYKVAWQ----ADNGQSLRT 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439521 366 MVSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 428
Cdd:PRK12341 314 SAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQI 376
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
176-267 |
5.62e-23 |
|
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: 92.73 E-value: 5.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 176 CFGLTEPNHGSDPGGMETRARhNPSNQSYTLSGTKTWITNSPVADLFIVWARCEDNCIPG----FILEKGMRGSSAPRIE 251
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAA-DGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGgislFLVPKDAPGVSVRRIE 79
|
90
....*....|....*.
gi 1439521 252 GKFSLRASATGMIIMD 267
Cdd:pfam02770 80 TKLGVRGLPTGELVFD 95
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
56-428 |
2.05e-22 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 98.37 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 56 LEEQLTADEKLIRDTFRNYW-QERLMSQILLANRNEVFHRDIVYEMGELG---VLGPTIKGYGCAGVSSVA--------Y 123
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELMaSENWEAYFAECDRDSVYPERFVKALADMGidsLLIPEEHGGLDAGFVTLAavwmelgrL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 124 GLLTRELERVDSGYRSMMSvqsslvmhpiytYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRarHNPSNQS 203
Cdd:PRK03354 81 GAPTYVLYQLPGGFNTFLR------------EGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTT--YTRRNGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 204 YTLSGTKTWITNSPVADLFIVWAR-CEDNCIPGF---ILEKGMRGSSAPRIEgKFSLRASATGMIIMDSVEVPEENVlpn 279
Cdd:PRK03354 147 VYLNGSKCFITSSAYTPYIVVMARdGASPDKPVYtewFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDM--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 280 vsslagpFGC-----------LNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLH 348
Cdd:PRK03354 223 -------FGRegngfnrvkeeFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 349 ACLQLGRLKDQDKATPEMVSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 428
Cdd:PRK03354 296 MLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAV 375
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
152-428 |
3.10e-21 |
|
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: 95.13 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 152 IYTYGSEEQRQkYLPRLA----KGELLGCFGLTEPNHGSDPGGMETRARHNPSNqSYTLSGTKtWITNSPVADLFIVWAR 227
Cdd:cd01154 123 LRKYGPEELKQ-YLPGLLsdryKTGLLGGTWMTEKQGGSDLGANETTAERSGGG-VYRLNGHK-WFASAPLADAALVLAR 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 228 CEDNC----------IPGFiLEKGMR-GSSAPRIEGKFSLRASATGMIIMDSVEV----PEENVLPNVSSLagpfgcLNT 292
Cdd:cd01154 200 PEGAPagarglslflVPRL-LEDGTRnGYRIRRLKDKLGTRSVATGEVEFDDAEAyligDEGKGIYYILEM------LNI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 293 ARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLkdQDKATPE------- 365
Cdd:cd01154 273 SRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARA--FDRAAADkpveahm 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439521 366 ---MVSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 428
Cdd:cd01154 351 arlATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVL 416
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
126-415 |
1.08e-16 |
|
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: 82.38 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 126 LTRELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSNQSY- 204
Cdd:cd01150 87 LTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFv 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 205 ----TLSGTKTWITNSPV-ADLFIVWAR--CEDNC--IPGFILE-------KGMRGSSAPRIEGKFSLRASATGMIIMDS 268
Cdd:cd01150 167 intpDFTATKWWPGNLGKtATHAVVFAQliTPGKNhgLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNGFLQFRN 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 269 VEVPEEN-------VLPN---VSSLAGP-------FGCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFG-------V 324
Cdd:cd01150 247 VRIPRENllnrfgdVSPDgtyVSPFKDPnkrygamLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGpkpsdpeV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 325 PLARNQLVQKKLADML----------TEITLGLHAClQLGRLKDQDKATPEM---VSMLKRNN---CGKALDIARQArdi 388
Cdd:cd01150 327 QILDYQLQQYRLFPQLaaayafhfaaKSLVEMYHEI-IKELLQGNSELLAELhalSAGLKAVAtwtAAQGIQECREA--- 402
|
330 340
....*....|....*....|....*....
gi 1439521 389 LGGNGISDE--YHVIRhAMNlEAVNTYEG 415
Cdd:cd01150 403 CGGHGYLAMnrLPTLR-DDN-DPFCTYEG 429
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
124-319 |
3.66e-15 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 77.60 E-value: 3.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 124 GLLTRELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARHNpSNQS 203
Cdd:PTZ00456 132 GFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPS-ADGS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 204 YTLSGTKTWIT----NSPVADLFIVWARCEdNCIPGfilEKGMRGSSAPR-------------------IEGKFSLRASA 260
Cdd:PTZ00456 211 YKITGTKIFISagdhDLTENIVHIVLARLP-NSLPT---TKGLSLFLVPRhvvkpdgsletaknvkcigLEKKMGIKGSS 286
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439521 261 TG-MIIMDSVE--VPEENvlpnvSSLAGPFGCLNTARYGITWGVLGAAEFCLHTARQYALDR 319
Cdd:PTZ00456 287 TCqLSFENSVGylIGEPN-----AGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARER 343
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
147-396 |
5.25e-14 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 74.22 E-value: 5.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 147 LVMHpiytYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGME-----TRARHN-PSNQSYTLSGTKTWITNSPVAD 220
Cdd:PRK13026 170 LLTH----YGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEgEEVLGLRLTWDKRYITLAPVAT 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 221 LFIVWARCEDnciP-GFILEKGMRG-------SSAPRIE-GKfslRASATGMIIMD------SVEVPEENVlpnvssLAG 285
Cdd:PRK13026 246 VLGLAFKLRD---PdGLLGDKKELGitcalipTDHPGVEiGR---RHNPLGMAFMNgttrgkDVFIPLDWI------IGG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 286 P----------FGCLNTARyGITWGVLGAA--EFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTeITLGLHACLQL 353
Cdd:PRK13026 314 PdyagrgwrmlVECLSAGR-GISLPALGTAsgHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAG-NTYLLEAARRL 391
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1439521 354 GRLKDQDKATPEMVS-MLKRNNCGKALDIARQARDILGGNGISD 396
Cdd:PRK13026 392 TTTGLDLGVKPSVVTaIAKYHMTELARDVVNDAMDIHAGKGIQL 435
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
149-398 |
2.56e-13 |
|
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: 71.27 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 149 MHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPN-HGSDPGGMETRARHNpsNQSYTLSGTKTWITNS--PVADLFIVW 225
Cdd:cd01155 101 MEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERD--GDDYVINGRKWWSSGAgdPRCKIAIVM 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 226 ARCEDNCIP-----GFILEKgmrgSSAPRIEGKFSLRA-------SATGMIIMDSVEVPEEN-VLPNVSSLAGPFGCLNT 292
Cdd:cd01155 179 GRTDPDGAPrhrqqSMILVP----MDTPGVTIIRPLSVfgyddapHGHAEITFDNVRVPASNlILGEGRGFEIAQGRLGP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 293 ARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQ--DKATPEMVSML 370
Cdd:cd01155 255 GRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTvgNKAARKEIAMI 334
|
250 260
....*....|....*....|....*...
gi 1439521 371 KRNNCGKALDIARQARDILGGNGISDEY 398
Cdd:cd01155 335 KVAAPRMALKIIDRAIQVHGAAGVSQDT 362
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
92-227 |
4.45e-13 |
|
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: 70.45 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 92 FHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYRSMMSVQSSLVmHPIYTYGSEEQRQKYLPRLAK 170
Cdd:cd01152 36 DRRRWQRALAAAGWAAPGWpKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAG-PTILAYGTDEQKRRFLPPILS 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1439521 171 GELLGCFGLTEPNHGSDPGGMETRARHNpsNQSYTLSGTKTWITNSPVADLFIVWAR 227
Cdd:cd01152 115 GEEIWCQGFSEPGAGSDLAGLRTRAVRD--GDDWVVNGQKIWTSGAHYADWAWLLVR 169
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
147-191 |
1.08e-12 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 70.23 E-value: 1.08e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1439521 147 LVMHpiytYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGM 191
Cdd:PRK09463 171 LLLH----YGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSI 211
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
141-348 |
9.19e-11 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 63.72 E-value: 9.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 141 MSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSNQSYTLS-----GTKTWITN 215
Cdd:PLN02636 141 LGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINtpndgAIKWWIGN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 216 SPVADLFI-VWARC----------EDNCIPGFILE-KGMRGSSA-PRIE-----GKFSLRASATGMIIMDSVEVPEENV- 276
Cdd:PLN02636 221 AAVHGKFAtVFARLklpthdskgvSDMGVHAFIVPiRDMKTHQVlPGVEirdcgHKVGLNGVDNGALRFRSVRIPRDNLl 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 277 ---------------LPNVSS-LAGPFGCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVP------LARNQLVQK 334
Cdd:PLN02636 301 nrfgdvsrdgkytssLPTINKrFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQH 380
|
250
....*....|....
gi 1439521 335 KLADMLTEiTLGLH 348
Cdd:PLN02636 381 KLMPMLAS-TYAFH 393
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
156-281 |
2.56e-10 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 62.55 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 156 GSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSN-----QSYTLSGTKTWITN-SPVADLFIVWARC- 228
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTdefviHSPTLTSSKWWPGGlGKVSTHAVVYARLi 193
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439521 229 ---EDNCIPGFILE-------KGMRGSSAPRIEGKFSLRASAT---GMIIMDSVEVPEENVLPNVS 281
Cdd:PLN02443 194 tngKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTmdnGFLRFDHVRIPRDQMLMRLS 259
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
152-324 |
2.87e-06 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 49.77 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 152 IYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSNQSYTL-----SGTKTWITNSPV-ADLFIVW 225
Cdd:PLN02312 164 IKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVIntpceSAQKYWIGGAANhATHTIVF 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 226 ARCEDNC----IPGFILE-KGMRGSSAPRIE-----GKFSLRASATGMIIMDSVEVPEEN-------VLPN---VSSLAG 285
Cdd:PLN02312 244 SQLHINGknegVHAFIAQiRDQDGNICPNIRiadcgHKIGLNGVDNGRIWFDNLRIPRENllnsvadVSPDgkyVSAIKD 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1439521 286 P---FGC----LNTARYGITWGVLGAAEFCLHTARQYALDRIQFGV 324
Cdd:PLN02312 324 PdqrFGAflapLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAFSV 369
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
188-430 |
4.73e-05 |
|
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: 45.42 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 188 PGGMETRArhnpsNQSYTLSGTKTWITNSPVADLFIVWARCEDNCIPG----FILEKgmrgsSAPRIEGKFS---LRASA 260
Cdd:cd01159 109 PGGRAERV-----DGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPlpraFVVPR-----AEYEIVDTWHvvgLRGTG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 261 TGMIIMDSVEVPEENVLPNVSSLAGPFGCLNTARYGITWG----------VLGAAEFCLHTARQYALDRIQ---FGVPLA 327
Cdd:cd01159 179 SNTVVVDDVFVPEHRTLTAGDMMAGDGPGGSTPVYRMPLRqvfplsfaavSLGAAEGALAEFLELAGKRVRqygAAVKMA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 328 RNQLVQKKLADMLTEITlglHACLQLGRLKDQ-------DKATPEMVSMLKRNNCGKALDIARQARDIL----GGNGISD 396
Cdd:cd01159 259 EAPITQLRLAEAAAELD---AARAFLERATRDlwahalaGGPIDVEERARIRRDAAYAAKLSAEAVDRLfhaaGGSALYT 335
|
250 260 270
....*....|....*....|....*....|....*....
gi 1439521 397 EYHVIR-----HAMNLEAVNTYEGThdihALILGRAITG 430
Cdd:cd01159 336 ASPLQRiwrdiHAAAQHAALNPETA----AEAYGRALLG 370
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
94-403 |
5.13e-04 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 42.47 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 94 RDIVYEMGELGVLGPTIKGYGCAGVSSVAYGLLTRELERvdsgyrSMMSVQ-------SSLVMHPIYTYGSEEQRQKYLP 166
Cdd:PLN02876 470 RKLLFEDNKHMVSGDSADQLLGAGLSNLEYGYLCEIMGR------SVWAPQvfncgapDTGNMEVLLRYGNKEQQLEWLI 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 167 RLAKGELLGCFGLTEPN-HGSDPGGMETRARHnpSNQSYTLSGTKTWITNS--PVADLFIVWARCEDNC----------- 232
Cdd:PLN02876 544 PLLEGKIRSGFAMTEPQvASSDATNIECSIRR--QGDSYVINGTKWWTSGAmdPRCRVLIVMGKTDFNApkhkqqsmilv 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 233 ---IPGFILEKgmrgssaPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVS---SLAGpfGCLNTARYGITWGVLGAAE 306
Cdd:PLN02876 622 diqTPGVQIKR-------PLLVFGFDDAPHGHAEISFENVRVPAKNILLGEGrgfEIAQ--GRLGPGRLHHCMRLIGAAE 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439521 307 FCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEIT----LGLHACLQLGRLKDQD-KATPEMVSMLKRNNCGKALDI 381
Cdd:PLN02876 693 RGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEqtrlLVLEAADQLDRLGNKKaRGIIAMAKVAAPNMALKVLDM 772
|
330 340
....*....|....*....|..
gi 1439521 382 ARQardILGGNGISDEYhVIRH 403
Cdd:PLN02876 773 AMQ---VHGAAGVSSDT-VLAH 790
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
142-212 |
1.02e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 41.37 E-value: 1.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439521 142 SVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSNQSYTL-----SGTKTW 212
Cdd:PTZ00460 96 TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIhtpsvEAVKFW 171
|
|
| |
