|
Name |
Accession |
Description |
Interval |
E-value |
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
57-443 |
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: 747.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 57 FDWKDPLILEEQLTADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTIKGYGCAGVSSVAYGLLT 136
Cdd:cd01151 1 FNWEDPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGYGCAGLSSVAYGLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 137 RELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARhnPSNQSYTLS 216
Cdd:cd01151 81 REVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRAR--KDGGGYKLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 217 GTKTWITNSPVADLFIVWARC-EDNCIRGFILEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVSSLAGP 295
Cdd:cd01151 159 GSKTWITNSPIADVFVVWARNdETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 296 FGCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEM 375
Cdd:cd01151 239 FKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQ 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 390190197 376 VSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITGIQAF 443
Cdd:cd01151 319 ISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
68-439 |
7.29e-127 |
|
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: 372.64 E-value: 7.29e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 68 QLTADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGY 146
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIpEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 147 RSMMSVQSSlVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARhnPSNQSYTLSGTKTWITNSP 226
Cdd:COG1960 84 ALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV--RDGDGYVLNGQKTFITNAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 227 VADLFIVWARCEDNC----IRGFILEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVS-SLAGPFGCLNT 301
Cdd:COG1960 161 VADVILVLARTDPAAghrgISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGkGFKIAMSTLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 302 ARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSMLKR 381
Cdd:COG1960 241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 390190197 382 NNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITG 439
Cdd:COG1960 321 FATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
74-435 |
2.04e-93 |
|
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: 284.95 E-value: 2.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 74 KLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVlgptikgygcagvssvayglltrelervdsgyrsmmsvq 153
Cdd:cd00567 4 RELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLG--------------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 154 sslvMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARhnPSNQSYTLSGTKTWITNSPVADLFIV 233
Cdd:cd00567 45 ----AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTAR--KDGDGYVLNGRKIFISNGGDADLFIV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 234 WARCEDN-----CIRGFILEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNV-SSLAGPFGCLNTARYGIT 307
Cdd:cd00567 119 LARTDEEgpghrGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEgGGFELAMKGLNVGRLLLA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 308 WGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKA-TPEMVSMLKRNNCGK 386
Cdd:cd00567 199 AVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKLFATEA 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 390190197 387 ALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGR 435
Cdd:cd00567 279 AREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
65-443 |
5.91e-92 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 284.44 E-value: 5.91e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 65 LEEQLTADEKLIRDTFRNyCQERLMSRILLANRNEV---FHrdIVYEMGELGVLGPTIKGYGCAGVSSVAYGLLTRELER 141
Cdd:PLN02526 25 FDDLLTPEEQALRKRVRE-CMEKEVAPIMTEYWEKAefpFH--IIPKLGSLGIAGGTIKGYGCPGLSITASAIATAEVAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 142 VDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSnqSYTLSGTKTW 221
Cdd:PLN02526 102 VDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEG--GWILNGQKRW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 222 ITNSPVADLFIVWAR-CEDNCIRGFILEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVSSLAGPFGCLN 300
Cdd:PLN02526 180 IGNSTFADVLVIFARnTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSFQDTNKVLA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 301 TARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSMLK 380
Cdd:PLN02526 260 VSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGK 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 390190197 381 RNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITGIQAF 443
Cdd:PLN02526 340 AWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIASF 402
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
72-437 |
2.57e-88 |
|
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: 273.76 E-value: 2.57e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 72 DEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYRSMM 150
Cdd:cd01158 2 EHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIpEEYGGAGLDFLAYAIAIEELAKVDASVAVIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 151 SVQSSLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSNqsYTLSGTKTWITNSPVADL 230
Cdd:cd01158 82 SVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDD--YVLNGSKMWITNGGEADF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 231 FIVWARCED----NCIRGFILEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLpnvsslaGPFG--------C 298
Cdd:cd01158 160 YIVFAVTDPskgyRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENIL-------GEEGegfkiamqT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 299 LNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSM 378
Cdd:cd01158 233 LDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAM 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 390190197 379 LKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 437
Cdd:cd01158 313 AKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
69-437 |
1.58e-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: 1.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 69 LTADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYR 147
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITApEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 148 SMMSVQSSLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNpsNQSYTLSGTKTWITNSPV 227
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKK--GDRYVLNGSKMWITNGPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 228 ADLFIVWARCEDNC----IRGFILEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVSS-----LAGpfgc 298
Cdd:cd01156 160 ADTLVVYAKTDPSAgahgITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKgvyvlMSG---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 299 LNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEitlgLHACLQL----GRLKDQDKATPE 374
Cdd:cd01156 236 LDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTR----LNASRSYlytvAKACDRGNMDPK 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 390190197 375 MVSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHamnLEAVNTYE---GTHDIHALILGRAI 437
Cdd:cd01156 312 DAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRL---LRDAKLYEigaGTSEIRRMVIGREL 374
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
47-441 |
7.16e-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: 208.86 E-value: 7.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 47 IRPAKSSRPVFdwKDPLILEEQLTADEKLIRDTFRNYCQERLMSRILlaNRNEVFHRDIVYEMGELGVLGPTI-KGYGCA 125
Cdd:cd01161 7 FLGDIVTKQVF--PYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKN--DQLEKIPRKTLTQLKELGLFGLQVpEEYGGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 126 GVSSVAYGLLTrELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRAR 205
Cdd:cd01161 83 GLNNTQYARLA-EIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 206 HNPSNQSYTLSGTKTWITNSPVADLFIVWARCEDNCIRG--------FILEKGMRGLSAPRIEGKFSLRASATGMIIMDS 277
Cdd:cd01161 162 LSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGsvkdkitaFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 278 VEVPEENVLPNVSS---LAgpFGCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITL 354
Cdd:cd01161 242 VKIPVENVLGEVGDgfkVA--MNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 355 GLHACLQLGRLKDQD-KATPEMVSMLKRNNCGKALD-IARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALI 432
Cdd:cd01161 320 TESMAYMTSGNMDRGlKAEYQIEAAISKVFASEAAWlVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLF 399
|
....*....
gi 390190197 433 LgrAITGIQ 441
Cdd:cd01161 400 I--ALTGLQ 406
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
71-437 |
5.45e-53 |
|
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: 181.93 E-value: 5.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 71 ADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVdSGYRSM 149
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFpEEYGGIGGDLLSAAVLWEELARA-GGSGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 150 MSVQSSLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSNqsYTLSGTKTWITNSPVAD 229
Cdd:cd01160 80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDH--YVLNGSKTFITNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 230 LFIVWARCEDNC-----IRGFILEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVS-SLAGPFGCLNTAR 303
Cdd:cd01160 158 VVIVVARTGGEArgaggISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENkGFYYLMQNLPQER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 304 YGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLG---LHACLQLGRLKDQDKATpemVSMLK 380
Cdd:cd01160 238 LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTrafLDNCAWRHEQGRLDVAE---ASMAK 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 390190197 381 rNNCGKALD-IARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 437
Cdd:cd01160 315 -YWATELQNrVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
69-439 |
3.75e-52 |
|
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: 179.56 E-value: 3.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 69 LTADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTIKG-YGCAGVSSVAYGLLTRELERVDSGYR 147
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDdVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 148 SMMSVQSsLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHnpSNQSYTLSGTKTWITNSPV 227
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVR--EGDHYVLNGSKAFISGAGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 228 ADLFIVWARCEDNCIRG---FILEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPN-----VSSLAGpfgcL 299
Cdd:cd01162 158 SDVYVVMARTGGEGPKGiscFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGegqgfGIAMAG----L 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 300 NTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEIT----LGLHACLQLGRlKDQDKAtpEM 375
Cdd:cd01162 234 NGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVasrlMVRRAASALDR-GDPDAV--KL 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 390190197 376 VSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITG 439
Cdd:cd01162 311 CAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
69-439 |
4.55e-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: 166.22 E-value: 4.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 69 LTADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYR 147
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIpEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 148 SMMSVqSSLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNpsNQSYTLSGTKTWITNSPV 227
Cdd:cd01157 81 TAIEA-NSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKK--GDEYIINGQKMWITNGGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 228 ADLFIVWARCEDN-------CIRGFILEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLpnVSSLAG---PFG 297
Cdd:cd01157 158 ANWYFLLARSDPDpkcpaskAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVL--IGEGAGfkiAMG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 298 CLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVS 377
Cdd:cd01157 236 AFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYAS 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 390190197 378 MLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITG 439
Cdd:cd01157 316 IAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
12-351 |
3.78e-45 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 162.03 E-value: 3.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 12 LRGVSARLLSRRSGlrfprfPRTWSSAAAHTektqirpaKSSRPVFDWKDPlileeqlTADEKLIRDTFRNYCQERLMSR 91
Cdd:PTZ00461 1 MRRVLQSSLGRRSA------TCGWTAAATMT--------SASRAFMDLYNP-------TPEHAALRETVAKFSREVVDKH 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 92 ILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQR 170
Cdd:PTZ00461 60 AREDDINMHFNRDLFKQLGDLGVMGVTVpEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 171 QKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNpSNQSYTLSGTKTWITNSPVADLFIVWARCeDNCIRGFILEKG 250
Cdd:PTZ00461 140 ARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD-SNGNYVLNGSKIWITNGTVADVFLIYAKV-DGKITAFVVERG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 251 MRGLS-APRIEgKFSLRASATGMIIMDSVEVPEENVL-PNVSSLAGPFGCLNTARYGITWGVLGAAEFCLHTARQYALDR 328
Cdd:PTZ00461 218 TKGFTqGPKID-KCGMRASHMCQLFFEDVVVPAENLLgEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASER 296
|
330 340
....*....|....*....|...
gi 390190197 329 IQFGVPLARNQLVQKKLADMLTE 351
Cdd:PTZ00461 297 KAFGKPISNFGQIQRYIAEGYAD 319
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
77-435 |
1.36e-44 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 160.43 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 77 RDTFRNYCQERLMSRILLANRNEVFHRDIVY--EMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYRSMMSVQ 153
Cdd:PLN02519 34 KESVQQFAQENIAPHAAAIDATNSFPKDVNLwkLMGDFNLHGITApEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 154 SSLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRArhNPSNQSYTLSGTKTWITNSPVADLFIV 233
Cdd:PLN02519 114 SNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKA--ERVDGGYVLNGNKMWCTNGPVAQTLVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 234 WARCEDNC----IRGFILEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVS-SLAGPFGCLNTARYGITW 308
Cdd:PLN02519 192 YAKTDVAAgskgITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGkGVYVMMSGLDLERLVLAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 309 GVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSMLKRNNCGKAL 388
Cdd:PLN02519 272 GPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERAT 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 390190197 389 DIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGR 435
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 ... |
70-181 |
1.24e-39 |
|
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: 137.98 E-value: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 70 TADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYRS 148
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIpEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 390190197 149 MMSVQSSLVMHPIYTYGSEEQRQKYLPGLAKGE 181
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
297-437 |
3.07e-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: 106.18 E-value: 3.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 297 GCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMV 376
Cdd:pfam00441 9 ETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGAEA 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 390190197 377 SMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 437
Cdd:pfam00441 89 SMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
161-438 |
1.43e-26 |
|
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: 110.56 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 161 IYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNpSNQSYTLSGTKTWITN--SPVAD--LFIVWAR 236
Cdd:cd01153 96 LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQ-ADGSWRINGVKRFISAgeHDMSEniVHLVLAR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 237 CEDNC--IRG---FILEK----GMR-GLSAPRIEGKFSLRASATGMIIMDSVEVP---EENvlpnvSSLAGPFGCLNTAR 303
Cdd:cd01153 175 SEGAPpgVKGlslFLVPKflddGERnGVTVARIEEKMGLHGSPTCELVFDNAKGEligEEG-----MGLAQMFAMMNGAR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 304 YGITWGVLGAAEFCLHTARQYALDRIQFGVPLA-------------RNQLVQKKL-------ADM--LTEITLGLHACLQ 361
Cdd:cd01153 250 LGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKaapavtiihhpdvRRSLMTQKAyaegsraLDLytATVQDLAERKATE 329
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 390190197 362 LGRLKDQDKATPEMVSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHAL-ILGRAIT 438
Cdd:cd01153 330 GEDRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALdLIGRKIV 407
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
155-437 |
4.19e-25 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 105.97 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 155 SLVMHPIYTYGSEEQ-RQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNpsNQSYTLSGTKTWITNSPVADLFIV 233
Cdd:PRK12341 90 GQCIHSMRRFGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRK--NGKVYLNGQKTFITGAKEYPYMLV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 234 WAR-CED----NCIRGFILEKGMRGLSAPRIEgKFSLRASATGMIIMDSVEVPEE-----------NVLPNvsslagpfg 297
Cdd:PRK12341 168 LARdPQPkdpkKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESdlvgeegmgflNVMYN--------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 298 cLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEI----TLGLHACLQlgrlKDQDKATP 373
Cdd:PRK12341 238 -FEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIenmrNMVYKVAWQ----ADNGQSLR 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 390190197 374 EMVSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 437
Cdd:PRK12341 313 TSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQI 376
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
185-276 |
1.21e-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: 94.65 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 185 CFGLTEPNHGSDPGGMETRARhNPSNQSYTLSGTKTWITNSPVADLFIVWARCE----DNCIRGFILEKGMRGLSAPRIE 260
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAA-DGDGGGWVLNGTKWWITNAGIADLFLVLARTGgddrHGGISLFLVPKDAPGVSVRRIE 79
|
90
....*....|....*.
gi 390190197 261 GKFSLRASATGMIIMD 276
Cdd:pfam02770 80 TKLGVRGLPTGELVFD 95
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
65-437 |
5.34e-23 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 99.91 E-value: 5.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 65 LEEQLTADEKLIRDTFRNY-CQERLMSRILLANRNEVFHRDIVYEMGELG---VLGPTIKGYGCAGVSSVA--------Y 132
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGidsLLIPEEHGGLDAGFVTLAavwmelgrL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 133 GLLTRELERVDSGYRSMMSvqsslvmhpiytYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRarHNPSNQS 212
Cdd:PRK03354 81 GAPTYVLYQLPGGFNTFLR------------EGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTT--YTRRNGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 213 YTLSGTKTWITNSPVADLFIVWARCEDNCIRG----FILEKGMRGLSAPRIEgKFSLRASATGMIIMDSVEVPEENVlpn 288
Cdd:PRK03354 147 VYLNGSKCFITSSAYTPYIVVMARDGASPDKPvyteWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDM--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 289 vsslagpFGC-----------LNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLH 357
Cdd:PRK03354 223 -------FGRegngfnrvkeeFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 358 ACLQLGRLKDQDKATPEMVSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 437
Cdd:PRK03354 296 MLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAV 375
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
161-437 |
8.00e-22 |
|
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: 97.06 E-value: 8.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 161 IYTYGSEEQRQkYLPGLA----KGELLGCFGLTEPNHGSDPGGMETRARHNPSNqSYTLSGTKtWITNSPVADLFIVWAR 236
Cdd:cd01154 123 LRKYGPEELKQ-YLPGLLsdryKTGLLGGTWMTEKQGGSDLGANETTAERSGGG-VYRLNGHK-WFASAPLADAALVLAR 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 237 CED--NCIRGF-------ILEKGMR-GLSAPRIEGKFSLRASATGMIIMDSVEV----PEENVLPNVSSLagpfgcLNTA 302
Cdd:cd01154 200 PEGapAGARGLslflvprLLEDGTRnGYRIRRLKDKLGTRSVATGEVEFDDAEAyligDEGKGIYYILEM------LNIS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 303 RYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLkdQDKATPE-------- 374
Cdd:cd01154 274 RLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARA--FDRAAADkpveahma 351
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 390190197 375 --MVSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 437
Cdd:cd01154 352 rlATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVL 416
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
53-424 |
2.12e-18 |
|
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: 87.77 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 53 SRPVFDWKD-PLILEEQLTADeKLIRDTFRNYCQERLMSRILLAN---RNEVFH------RDIVYEMGELGVLGPTiKGY 122
Cdd:cd01150 8 ASATFDWKAlTHILEGGEENL-RRKREVERELESDPLFQRELPSKhlsREELYEelkrkaKTDVERMGELMADDPE-KML 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 123 GCagvssvaygllTRELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMET 202
Cdd:cd01150 86 AL-----------TNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLET 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 203 RARHNPSNQSY-----TLSGTKTWITNSPV-ADLFIVWAR--CEDNC--IRGFILE-------KGMRGLSAPRIEGKFSL 265
Cdd:cd01150 155 TATYDPLTQEFvintpDFTATKWWPGNLGKtATHAVVFAQliTPGKNhgLHAFIVPirdpkthQPLPGVTVGDIGPKMGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 266 RASATGMIIMDSVEVPEEN-------VLPN---VSSLAGP-------FGCLNTARYGITWGVLGAAEFCLHTARQYALDR 328
Cdd:cd01150 235 NGVDNGFLQFRNVRIPRENllnrfgdVSPDgtyVSPFKDPnkrygamLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 329 IQFG-------VPLARNQLVQKKLADML----------TEITLGLHAClQLGRLKDQDKATPEM---VSMLKRNN---CG 385
Cdd:cd01150 315 RQFGpkpsdpeVQILDYQLQQYRLFPQLaaayafhfaaKSLVEMYHEI-IKELLQGNSELLAELhalSAGLKAVAtwtAA 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 390190197 386 KALDIARQArdiLGGNGISDE--YHVIRhAMNlEAVNTYEG 424
Cdd:cd01150 394 QGIQECREA---CGGHGYLAMnrLPTLR-DDN-DPFCTYEG 429
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
133-328 |
3.72e-14 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 74.52 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 133 GLLTRELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNpSNQS 212
Cdd:PTZ00456 132 GFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPS-ADGS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 213 YTLSGTKTWIT----NSPVADLFIVWARCEDNCIRGfileKGMRGLSAPR-------------------IEGKFSLRASA 269
Cdd:PTZ00456 211 YKITGTKIFISagdhDLTENIVHIVLARLPNSLPTT----KGLSLFLVPRhvvkpdgsletaknvkcigLEKKMGIKGSS 286
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 390190197 270 TG-MIIMDSVE--VPEENvlpnvSSLAGPFGCLNTARYGITWGVLGAAEFCLHTARQYALDR 328
Cdd:PTZ00456 287 TCqLSFENSVGylIGEPN-----AGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARER 343
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
156-405 |
4.98e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 71.14 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 156 LVMHpiytYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGME-----TRARHN-PSNQSYTLSGTKTWITNSPVAD 229
Cdd:PRK13026 170 LLTH----YGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEgEEVLGLRLTWDKRYITLAPVAT 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 230 LFIVWARCEDNciRGFILEKGMRGL-------SAPRIE-GKfslRASATGMIIMD------SVEVPEENVlpnvssLAGP 295
Cdd:PRK13026 246 VLGLAFKLRDP--DGLLGDKKELGItcaliptDHPGVEiGR---RHNPLGMAFMNgttrgkDVFIPLDWI------IGGP 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 296 ----------FGCLNTARyGITWGVLGAA--EFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTeITLGLHACLQLG 363
Cdd:PRK13026 315 dyagrgwrmlVECLSAGR-GISLPALGTAsgHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAG-NTYLLEAARRLT 392
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 390190197 364 RLKDQDKATPEMVS-MLKRNNCGKALDIARQARDILGGNGISD 405
Cdd:PRK13026 393 TTGLDLGVKPSVVTaIAKYHMTELARDVVNDAMDIHAGKGIQL 435
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
158-407 |
6.54e-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: 70.11 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 158 MHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPN-HGSDPGGMETRARHNpsNQSYTLSGTKTWITNS--PVADLFIVW 234
Cdd:cd01155 101 MEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERD--GDDYVINGRKWWSSGAgdPRCKIAIVM 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 235 ARCEDNC-----IRGFIL----EKGMRGLSAPRIEGkFSLRASATGMIIMDSVEVPEEN-VLPNVSSLAGPFGCLNTARY 304
Cdd:cd01155 179 GRTDPDGaprhrQQSMILvpmdTPGVTIIRPLSVFG-YDDAPHGHAEITFDNVRVPASNlILGEGRGFEIAQGRLGPGRI 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 305 GITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQ--DKATPEMVSMLKRN 382
Cdd:cd01155 258 HHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTvgNKAARKEIAMIKVA 337
|
250 260
....*....|....*....|....*
gi 390190197 383 NCGKALDIARQARDILGGNGISDEY 407
Cdd:cd01155 338 APRMALKIIDRAIQVHGAAGVSQDT 362
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
101-236 |
1.27e-12 |
|
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: 68.91 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 101 FHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYRSMMSVQSSLVmHPIYTYGSEEQRQKYLPGLAK 179
Cdd:cd01152 36 DRRRWQRALAAAGWAAPGWpKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAG-PTILAYGTDEQKRRFLPPILS 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 390190197 180 GELLGCFGLTEPNHGSDPGGMETRARHNpsNQSYTLSGTKTWITNSPVADLFIVWAR 236
Cdd:cd01152 115 GEEIWCQGFSEPGAGSDLAGLRTRAVRD--GDDWVVNGQKIWTSGAHYADWAWLLVR 169
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
156-200 |
9.84e-12 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 67.15 E-value: 9.84e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 390190197 156 LVMHpiytYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGM 200
Cdd:PRK09463 171 LLLH----YGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSI 211
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
150-357 |
1.23e-11 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 66.81 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 150 MSVQSSLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSNQSYTLS-----GTKTWITN 224
Cdd:PLN02636 141 LGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINtpndgAIKWWIGN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 225 SPVADLFI-VWARC----------EDNCIRGFILE-KGMRGLSA-PRIE-----GKFSLRASATGMIIMDSVEVPEENV- 285
Cdd:PLN02636 221 AAVHGKFAtVFARLklpthdskgvSDMGVHAFIVPiRDMKTHQVlPGVEirdcgHKVGLNGVDNGALRFRSVRIPRDNLl 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 286 ---------------LPNVSS-LAGPFGCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVP------LARNQLVQK 343
Cdd:PLN02636 301 nrfgdvsrdgkytssLPTINKrFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQH 380
|
250
....*....|....
gi 390190197 344 KLADMLTEiTLGLH 357
Cdd:PLN02636 381 KLMPMLAS-TYAFH 393
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
165-290 |
7.01e-11 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 64.47 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 165 GSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSN-----QSYTLSGTKTWITN-SPVADLFIVWARC- 237
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTdefviHSPTLTSSKWWPGGlGKVSTHAVVYARLi 193
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 390190197 238 ---EDNCIRGFILE-------KGMRGLSAPRIEGKFSLRASAT---GMIIMDSVEVPEENVLPNVS 290
Cdd:PLN02443 194 tngKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTmdnGFLRFDHVRIPRDQMLMRLS 259
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
161-333 |
1.44e-05 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 47.46 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 161 IYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSNQSYTL-----SGTKTWITNSPV-ADLFIVW 234
Cdd:PLN02312 164 IKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVIntpceSAQKYWIGGAANhATHTIVF 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 235 ARCEDN----CIRGFILE-KGMRGLSAPRIE-----GKFSLRASATGMIIMDSVEVPEEN-------VLPN---VSSLAG 294
Cdd:PLN02312 244 SQLHINgkneGVHAFIAQiRDQDGNICPNIRiadcgHKIGLNGVDNGRIWFDNLRIPRENllnsvadVSPDgkyVSAIKD 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 390190197 295 P---FGC----LNTARYGITWGVLGAAEFCLHTARQYALDRIQFGV 333
Cdd:PLN02312 324 PdqrFGAflapLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAFSV 369
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
197-439 |
1.88e-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: 46.57 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 197 PGGMETRArhnpsNQSYTLSGTKTWITNSPVADLFIVWARCEDNC----IRGFILEKgmrglSAPRIEGKFS---LRASA 269
Cdd:cd01159 109 PGGRAERV-----DGGYRVSGTWPFASGCDHADWILVGAIVEDDDggplPRAFVVPR-----AEYEIVDTWHvvgLRGTG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 270 TGMIIMDSVEVPEENVLPNVSSLAGPFGCLNTARYGITWG----------VLGAAEFCLHTARQYALDRIQ---FGVPLA 336
Cdd:cd01159 179 SNTVVVDDVFVPEHRTLTAGDMMAGDGPGGSTPVYRMPLRqvfplsfaavSLGAAEGALAEFLELAGKRVRqygAAVKMA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 337 RNQLVQKKLADMLTEITlglHACLQLGRLKDQ-------DKATPEMVSMLKRNNCGKALDIARQARDIL----GGNGISD 405
Cdd:cd01159 259 EAPITQLRLAEAAAELD---AARAFLERATRDlwahalaGGPIDVEERARIRRDAAYAAKLSAEAVDRLfhaaGGSALYT 335
|
250 260 270
....*....|....*....|....*....|....*....
gi 390190197 406 EYHVIR-----HAMNLEAVNTYEGThdihALILGRAITG 439
Cdd:cd01159 336 ASPLQRiwrdiHAAAQHAALNPETA----AEAYGRALLG 370
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
103-412 |
2.43e-04 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 43.63 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 103 RDIVYEMGELGVLGPTIKGYGCAGVSSVAYGLLTRELERvdsgyrSMMSVQ-------SSLVMHPIYTYGSEEQRQKYLP 175
Cdd:PLN02876 470 RKLLFEDNKHMVSGDSADQLLGAGLSNLEYGYLCEIMGR------SVWAPQvfncgapDTGNMEVLLRYGNKEQQLEWLI 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 176 GLAKGELLGCFGLTEPN-HGSDPGGMETRARHnpSNQSYTLSGTKTWITNS--PVADLFIVWARCEDNCI----RGFIL- 247
Cdd:PLN02876 544 PLLEGKIRSGFAMTEPQvASSDATNIECSIRR--QGDSYVINGTKWWTSGAmdPRCRVLIVMGKTDFNAPkhkqQSMILv 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 248 EKGMRGLSAPRIEGKFSLRASATGM--IIMDSVEVPEENVLPNVS---SLAGpfGCLNTARYGITWGVLGAAEFCLHTAR 322
Cdd:PLN02876 622 DIQTPGVQIKRPLLVFGFDDAPHGHaeISFENVRVPAKNILLGEGrgfEIAQ--GRLGPGRLHHCMRLIGAAERGMQLMV 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390190197 323 QYALDRIQFGVPLARNQLVQKKLADMLTEIT----LGLHACLQLGRLKDQD-KATPEMVSMLKRNNCGKALDIARQardI 397
Cdd:PLN02876 700 QRALSRKAFGKLIAQHGSFLSDLAKCRVELEqtrlLVLEAADQLDRLGNKKaRGIIAMAKVAAPNMALKVLDMAMQ---V 776
|
330
....*....|....*
gi 390190197 398 LGGNGISDEYhVIRH 412
Cdd:PLN02876 777 HGAAGVSSDT-VLAH 790
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
151-221 |
1.67e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 40.98 E-value: 1.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 390190197 151 SVQSSLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSNQSYTL-----SGTKTW 221
Cdd:PTZ00460 96 TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIhtpsvEAVKFW 171
|
|
| |
