|
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: 748.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 57 FDWKDPLVLEEQLTADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTIKGYGCAGVSSVAYGLLT 136
Cdd:cd01151 1 FNWEDPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGYGCAGLSSVAYGLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 137 RELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARhnPSNKSYTLS 216
Cdd:cd01151 81 REVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRAR--KDGGGYKLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 217 GTKTWITNSPVADLFVVWARC-EDNCIRGFLLEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVSSLAGP 295
Cdd:cd01151 159 GSKTWITNSPIADVFVVWARNdETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 296 FGCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEM 375
Cdd:cd01151 239 FKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQ 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157820807 376 VSLLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITGIQAF 443
Cdd:cd01151 319 ISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
68-439 |
2.80e-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: 373.41 E-value: 2.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 68 QLTADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGY 146
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIpEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 147 RSMMSVQSSlVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARhnPSNKSYTLSGTKTWITNSP 226
Cdd:COG1960 84 ALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV--RDGDGYVLNGQKTFITNAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 227 VADLFVVWARCEDNC----IRGFLLEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVS-SLAGPFGCLNT 301
Cdd:COG1960 161 VADVILVLARTDPAAghrgISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGkGFKIAMSTLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 302 ARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSLLKR 381
Cdd:COG1960 241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 157820807 382 NNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITG 439
Cdd:COG1960 321 FATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
74-435 |
1.72e-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: 285.33 E-value: 1.72e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 74 KLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVlgptikgygcagvssvayglltrelervdsgyrsmmsvq 153
Cdd:cd00567 4 RELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLG--------------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 154 sslvMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARhnPSNKSYTLSGTKTWITNSPVADLFVV 233
Cdd:cd00567 45 ----AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTAR--KDGDGYVLNGRKIFISNGGDADLFIV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 234 WARCEDN-----CIRGFLLEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNV-SSLAGPFGCLNTARYGIT 307
Cdd:cd00567 119 LARTDEEgpghrGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEgGGFELAMKGLNVGRLLLA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 308 WGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKA-TPEMVSLLKRNNCGK 386
Cdd:cd00567 199 AVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKLFATEA 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 157820807 387 ALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGR 435
Cdd:cd00567 279 AREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
65-443 |
1.27e-91 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 283.67 E-value: 1.27e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 65 LEEQLTADEKLIRDTFRNyCQERLMSRILLANRNEV---FHrdIVYEMGELGVLGPTIKGYGCAGVSSVAYGLLTRELER 141
Cdd:PLN02526 25 FDDLLTPEEQALRKRVRE-CMEKEVAPIMTEYWEKAefpFH--IIPKLGSLGIAGGTIKGYGCPGLSITASAIATAEVAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 142 VDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARHNPSnkSYTLSGTKTW 221
Cdd:PLN02526 102 VDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEG--GWILNGQKRW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 222 ITNSPVADLFVVWAR-CEDNCIRGFLLEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVSSLAGPFGCLN 300
Cdd:PLN02526 180 IGNSTFADVLVIFARnTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSFQDTNKVLA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 301 TARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSLLK 380
Cdd:PLN02526 260 VSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGK 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157820807 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 |
5.23e-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: 272.99 E-value: 5.23e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 72 DEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYRSMM 150
Cdd:cd01158 2 EHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIpEEYGGAGLDFLAYAIAIEELAKVDASVAVIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 151 SVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARHNPSNksYTLSGTKTWITNSPVADL 230
Cdd:cd01158 82 SVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDD--YVLNGSKMWITNGGEADF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 231 FVVWARCED----NCIRGFLLEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLpnvsslaGPFG--------C 298
Cdd:cd01158 160 YIVFAVTDPskgyRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENIL-------GEEGegfkiamqT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 299 LNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSL 378
Cdd:cd01158 233 LDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAM 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 157820807 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 |
6.89e-67 |
|
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: 218.43 E-value: 6.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 69 LTADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYR 147
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITApEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 148 SMMSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARHNPSNksYTLSGTKTWITNSPV 227
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDR--YVLNGSKMWITNGPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 228 ADLFVVWARCEDNC----IRGFLLEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVSS-----LAGpfgc 298
Cdd:cd01156 160 ADTLVVYAKTDPSAgahgITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKgvyvlMSG---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 299 LNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEitlgLHACLQL----GRLKDQDKATPE 374
Cdd:cd01156 236 LDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTR----LNASRSYlytvAKACDRGNMDPK 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157820807 375 MVSLLKRNNCGKALDIARQARDILGGNGISDEYHVIRHamnLEAVNTYE---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 |
1.03e-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: 211.17 E-value: 1.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 47 IRSVKSSRPVFdwKDPLVLEEQLTADEKLIRDTFRNYCQERLMSRILlaNRNEVFHRDIVYEMGELGVLGPTI-KGYGCA 125
Cdd:cd01161 7 FLGDIVTKQVF--PYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKN--DQLEKIPRKTLTQLKELGLFGLQVpEEYGGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 126 GVSSVAYGLLTrELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRAR 205
Cdd:cd01161 83 GLNNTQYARLA-EIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 206 HNPSNKSYTLSGTKTWITNSPVADLFVVWARCEDNCIRG--------FLLEKGMRGLSAPRIEGKFSLRASATGMIIMDS 277
Cdd:cd01161 162 LSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGsvkdkitaFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 278 VEVPEENVLPNVSS---LAgpFGCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITL 354
Cdd:cd01161 242 VKIPVENVLGEVGDgfkVA--MNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 355 GLHACLQLGRLKDQD-KATPEMVSLLKRNNCGKALD-IARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALI 432
Cdd:cd01161 320 TESMAYMTSGNMDRGlKAEYQIEAAISKVFASEAAWlVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLF 399
|
....*....
gi 157820807 433 LgrAITGIQ 441
Cdd:cd01161 400 I--ALTGLQ 406
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
69-439 |
1.41e-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: 180.72 E-value: 1.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 69 LTADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTIKG-YGCAGVSSVAYGLLTRELERVDSGYR 147
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDdVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 148 SMMSVQSsLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARHnpSNKSYTLSGTKTWITNSPV 227
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVR--EGDHYVLNGSKAFISGAGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 228 ADLFVVWARCEDNCIRG---FLLEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPN-----VSSLAGpfgcL 299
Cdd:cd01162 158 SDVYVVMARTGGEGPKGiscFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGegqgfGIAMAG----L 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 300 NTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEIT----LGLHACLQLgrlkdqDKATPEM 375
Cdd:cd01162 234 NGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVasrlMVRRAASAL------DRGDPDA 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157820807 376 VSLL---KRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITG 439
Cdd:cd01162 308 VKLCamaKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
71-437 |
9.36e-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: 178.46 E-value: 9.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 71 ADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVdSGYRSM 149
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFpEEYGGIGGDLLSAAVLWEELARA-GGSGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 150 MSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARHNPSNksYTLSGTKTWITNSPVAD 229
Cdd:cd01160 80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDH--YVLNGSKTFITNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 230 LFVVWARCEDNC-----IRGFLLEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVS-SLAGPFGCLNTAR 303
Cdd:cd01160 158 VVIVVARTGGEArgaggISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENkGFYYLMQNLPQER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 304 YGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLG---LHACLQLGRLKDQDKATPEMVsllk 380
Cdd:cd01160 238 LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTrafLDNCAWRHEQGRLDVAEASMA---- 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 157820807 381 RNNCGKALD-IARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 437
Cdd:cd01160 314 KYWATELQNrVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
69-439 |
1.74e-46 |
|
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: 164.68 E-value: 1.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 69 LTADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYR 147
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIpEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 148 SMMSVqSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARHNpsNKSYTLSGTKTWITNSPV 227
Cdd:cd01157 81 TAIEA-NSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKK--GDEYIINGQKMWITNGGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 228 ADLFVVWARCEDN-------CIRGFLLEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLpnVSSLAG---PFG 297
Cdd:cd01157 158 ANWYFLLARSDPDpkcpaskAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVL--IGEGAGfkiAMG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 298 CLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVS 377
Cdd:cd01157 236 AFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYAS 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157820807 378 LLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITG 439
Cdd:cd01157 316 IAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
77-435 |
5.35e-46 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 164.28 E-value: 5.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 77 RDTFRNYCQERLMSRILLANRNEVFHRDIVY--EMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYRSMMSVQ 153
Cdd:PLN02519 34 KESVQQFAQENIAPHAAAIDATNSFPKDVNLwkLMGDFNLHGITApEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 154 SSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRArhNPSNKSYTLSGTKTWITNSPVADLFVV 233
Cdd:PLN02519 114 SNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKA--ERVDGGYVLNGNKMWCTNGPVAQTLVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 234 WARCEDNC----IRGFLLEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVS-SLAGPFGCLNTARYGITW 308
Cdd:PLN02519 192 YAKTDVAAgskgITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGkGVYVMMSGLDLERLVLAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 309 GVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSLLKRNNCGKAL 388
Cdd:PLN02519 272 GPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERAT 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 157820807 389 DIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGR 435
Cdd:PLN02519 352 QVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGR 398
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
19-351 |
1.38e-43 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 157.79 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 19 LLSRKLGLRFSrvPRTWSSAAAHTektqirsvKSSRPVFDWKDPlvleeqlTADEKLIRDTFRNYCQERLMSRILLANRN 98
Cdd:PTZ00461 4 VLQSSLGRRSA--TCGWTAAATMT--------SASRAFMDLYNP-------TPEHAALRETVAKFSREVVDKHAREDDIN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 99 EVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPRL 177
Cdd:PTZ00461 67 MHFNRDLFKQLGDLGVMGVTVpEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 178 AKGELLGCFGLTEPNHGSDPGSMETRARHNpSNKSYTLSGTKTWITNSPVADLFVVWARCeDNCIRGFLLEKGMRGLS-A 256
Cdd:PTZ00461 147 LTGEHVGAMGMSEPGAGTDVLGMRTTAKKD-SNGNYVLNGSKIWITNGTVADVFLIYAKV-DGKITAFVVERGTKGFTqG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 257 PRIEgKFSLRASATGMIIMDSVEVPEENVL-PNVSSLAGPFGCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPL 335
Cdd:PTZ00461 225 PKID-KCGMRASHMCQLFFEDVVVPAENLLgEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPI 303
|
330
....*....|....*.
gi 157820807 336 ARNQLVQKKLADMLTE 351
Cdd:PTZ00461 304 SNFGQIQRYIAEGYAD 319
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
70-181 |
3.06e-40 |
|
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: 139.91 E-value: 3.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 70 TADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYRS 148
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIpEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 157820807 149 MMSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGE 181
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
161-438 |
8.46e-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: 114.02 E-value: 8.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 161 IYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARHNpSNKSYTLSGTKTWITN--SPVAD--LFVVWAR 236
Cdd:cd01153 96 LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQ-ADGSWRINGVKRFISAgeHDMSEniVHLVLAR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 237 CEDNC--IRG---FLLEK----GMR-GLSAPRIEGKFSLRASATGMIIMDSVEVP---EENvlpnvSSLAGPFGCLNTAR 303
Cdd:cd01153 175 SEGAPpgVKGlslFLVPKflddGERnGVTVARIEEKMGLHGSPTCELVFDNAKGEligEEG-----MGLAQMFAMMNGAR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 304 YGITWGVLGAAEFCLHTARQYALDRIQFGVPLA-------------RNQLVQKKL-------ADM--LTEITLGLHACLQ 361
Cdd:cd01153 250 LGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKaapavtiihhpdvRRSLMTQKAyaegsraLDLytATVQDLAERKATE 329
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157820807 362 LGRLKDQDKATPEMVSLLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHAL-ILGRAIT 438
Cdd:cd01153 330 GEDRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALdLIGRKIV 407
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
297-437 |
8.89e-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: 105.03 E-value: 8.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 297 GCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMV 376
Cdd:pfam00441 9 ETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGAEA 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157820807 377 SLLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 437
Cdd:pfam00441 89 SMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
155-437 |
1.06e-25 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 107.89 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 155 SLVMHPIYTYGSEEQ-RQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARHNpSNKSYtLSGTKTWITNSPVADLFVV 233
Cdd:PRK12341 90 GQCIHSMRRFGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRK-NGKVY-LNGQKTFITGAKEYPYMLV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 234 WAR-CED----NCIRGFLLEKGMRGLSAPRIEgKFSLRASATGMIIMDSVEVPEE-----------NVLPNvsslagpfg 297
Cdd:PRK12341 168 LARdPQPkdpkKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESdlvgeegmgflNVMYN--------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 298 cLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEI----TLGLHACLQlgrlKDQDKATP 373
Cdd:PRK12341 238 -FEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIenmrNMVYKVAWQ----ADNGQSLR 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157820807 374 EMVSLLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 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 |
6.74e-24 |
|
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: 95.04 E-value: 6.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 185 CFGLTEPNHGSDPGSMETRARhNPSNKSYTLSGTKTWITNSPVADLFVVWARCE----DNCIRGFLLEKGMRGLSAPRIE 260
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAA-DGDGGGWVLNGTKWWITNAGIADLFLVLARTGgddrHGGISLFLVPKDAPGVSVRRIE 79
|
90
....*....|....*.
gi 157820807 261 GKFSLRASATGMIIMD 276
Cdd:pfam02770 80 TKLGVRGLPTGELVFD 95
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
65-437 |
1.26e-23 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 101.83 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 65 LEEQLTADEKLIRDTFRNY-CQERLMSRILLANRNEVFHRDIVYEMGELG---VLGPTIKGYGCAGVSSVA--------Y 132
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGidsLLIPEEHGGLDAGFVTLAavwmelgrL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 133 GLLTRELERVDSGYRSMMSvqsslvmhpiytYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETR-ARHNpsNK 211
Cdd:PRK03354 81 GAPTYVLYQLPGGFNTFLR------------EGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTyTRRN--GK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 212 SYtLSGTKTWITNSPVADLFVVWARCEDNCIRG----FLLEKGMRGLSAPRIEgKFSLRASATGMIIMDSVEVPEENVlp 287
Cdd:PRK03354 147 VY-LNGSKCFITSSAYTPYIVVMARDGASPDKPvyteWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDM-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 288 nvsslagpFGC-----------LNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGL 356
Cdd:PRK03354 223 --------FGRegngfnrvkeeFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 357 HACLQLGRLKDQDKATPEMVSLLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRA 436
Cdd:PRK03354 295 NMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRA 374
|
.
gi 157820807 437 I 437
Cdd:PRK03354 375 V 375
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
161-437 |
3.49e-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: 98.21 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 161 IYTYGSEEQRQkYLPRLA----KGELLGCFGLTEPNHGSDPGSMETRARHNPSnKSYTLSGTKtWITNSPVADLFVVWAR 236
Cdd:cd01154 123 LRKYGPEELKQ-YLPGLLsdryKTGLLGGTWMTEKQGGSDLGANETTAERSGG-GVYRLNGHK-WFASAPLADAALVLAR 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 237 CED--NCIRG---FL----LEKGMR-GLSAPRIEGKFSLRASATGMIIMDSVEV----PEENVLPNVSSLagpfgcLNTA 302
Cdd:cd01154 200 PEGapAGARGlslFLvprlLEDGTRnGYRIRRLKDKLGTRSVATGEVEFDDAEAyligDEGKGIYYILEM------LNIS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 303 RYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLkdQDKATPE-------- 374
Cdd:cd01154 274 RLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARA--FDRAAADkpveahma 351
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157820807 375 --MVSLLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAI 437
Cdd:cd01154 352 rlATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVL 416
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
53-424 |
4.20e-17 |
|
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: 83.53 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 53 SRPVFDWKDPLVLEEQLTADEKLIRDTFRNYCQERLMSRILLAN---RNEVFH------RDIVYEMGELGVLGPTiKGYG 123
Cdd:cd01150 8 ASATFDWKALTHILEGGEENLRRKREVERELESDPLFQRELPSKhlsREELYEelkrkaKTDVERMGELMADDPE-KMLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 124 CagvssvaygllTRELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETR 203
Cdd:cd01150 87 L-----------TNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 204 ARHNPSNKSY-----TLSGTKTWITNSPV-ADLFVVWAR--CEDNC--IRGFLLE-------KGMRGLSAPRIEGKFSLR 266
Cdd:cd01150 156 ATYDPLTQEFvintpDFTATKWWPGNLGKtATHAVVFAQliTPGKNhgLHAFIVPirdpkthQPLPGVTVGDIGPKMGLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 267 ASATGMIIMDSVEVPEEN-------VLPN---VSSLAGP-------FGCLNTARYGITWGVLGAAEFCLHTARQYALDRI 329
Cdd:cd01150 236 GVDNGFLQFRNVRIPRENllnrfgdVSPDgtyVSPFKDPnkrygamLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 330 QFG-------VPLARNQLVQKKLADML----------TEITLGLHAClQLGRLKDQDKATPEMVSL---LKRNN---CGK 386
Cdd:cd01150 316 QFGpkpsdpeVQILDYQLQQYRLFPQLaaayafhfaaKSLVEMYHEI-IKELLQGNSELLAELHALsagLKAVAtwtAAQ 394
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 157820807 387 ALDIARQArdiLGGNGISDE--YHVIRhAMNlEAVNTYEG 424
Cdd:cd01150 395 GIQECREA---CGGHGYLAMnrLPTLR-DDN-DPFCTYEG 429
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
133-328 |
3.86e-15 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 77.60 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 133 GLLTRELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARHNpSNKS 212
Cdd:PTZ00456 132 GFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPS-ADGS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 213 YTLSGTKTWIT----NSPVADLFVVWARCEDNC-----IRGFLLEKGM----------RGLSAPRIEGKFSLRASATG-M 272
Cdd:PTZ00456 211 YKITGTKIFISagdhDLTENIVHIVLARLPNSLpttkgLSLFLVPRHVvkpdgsletaKNVKCIGLEKKMGIKGSSTCqL 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 157820807 273 IIMDSVE--VPEENvlpnvSSLAGPFGCLNTARYGITWGVLGAAEFCLHTARQYALDR 328
Cdd:PTZ00456 291 SFENSVGylIGEPN-----AGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARER 343
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
156-405 |
4.10e-14 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 74.61 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 156 LVMHpiytYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSME-----TRARHNPSNK-SYTLSGTKTWITNSPVAD 229
Cdd:PRK13026 170 LLTH----YGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEVlGLRLTWDKRYITLAPVAT 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 230 LFVVWARCEDNciRGFLLEKGMRGL-------SAPRIE-GKfslRASATGMIIMD------SVEVPEENVlpnvssLAGP 295
Cdd:PRK13026 246 VLGLAFKLRDP--DGLLGDKKELGItcaliptDHPGVEiGR---RHNPLGMAFMNgttrgkDVFIPLDWI------IGGP 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 296 ----------FGCLNTARyGITWGVLGAA--EFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTeITLGLHACLQLG 363
Cdd:PRK13026 315 dyagrgwrmlVECLSAGR-GISLPALGTAsgHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAG-NTYLLEAARRLT 392
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 157820807 364 RLKDQDKATPEMVS-LLKRNNCGKALDIARQARDILGGNGISD 405
Cdd:PRK13026 393 TTGLDLGVKPSVVTaIAKYHMTELARDVVNDAMDIHAGKGIQL 435
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
156-200 |
2.82e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 71.77 E-value: 2.82e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 157820807 156 LVMHpiytYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSM 200
Cdd:PRK09463 171 LLLH----YGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSI 211
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
101-229 |
1.22e-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: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 101 FHRDIVYEMGELGVLGPTI-KGYGCAGVSSVAYGLLTRELERVDSGYRSMMSVQSSLVmHPIYTYGSEEQRQKYLPRLAK 179
Cdd:cd01152 36 DRRRWQRALAAAGWAAPGWpKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAG-PTILAYGTDEQKRRFLPPILS 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 157820807 180 GELLGCFGLTEPNHGSDPGSMETRARHNpsNKSYTLSGTKTWITNSPVAD 229
Cdd:cd01152 115 GEEIWCQGFSEPGAGSDLAGLRTRAVRD--GDDWVVNGQKIWTSGAHYAD 162
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
158-407 |
1.21e-11 |
|
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: 65.87 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 158 MHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPN-HGSDPGSMETRARHNpsNKSYTLSGTKTWITNS--PVADLFVVW 234
Cdd:cd01155 101 MEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERD--GDDYVINGRKWWSSGAgdPRCKIAIVM 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 235 ARCEDNCIRG------FLLEKGMRGLSAPRIEGKFSLRASATGM--IIMDSVEVPEEN-VLPNVSSLAGPFGCLNTARYG 305
Cdd:cd01155 179 GRTDPDGAPRhrqqsmILVPMDTPGVTIIRPLSVFGYDDAPHGHaeITFDNVRVPASNlILGEGRGFEIAQGRLGPGRIH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 306 ITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQ--DKATPEMVSLLKRNN 383
Cdd:cd01155 259 HCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTvgNKAARKEIAMIKVAA 338
|
250 260
....*....|....*....|....
gi 157820807 384 CGKALDIARQARDILGGNGISDEY 407
Cdd:cd01155 339 PRMALKIIDRAIQVHGAAGVSQDT 362
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
165-290 |
1.10e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 60.62 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 165 GSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARHNPSNKSY-----TLSGTKTWITN-SPVADLFVVWARC- 237
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFvihspTLTSSKWWPGGlGKVSTHAVVYARLi 193
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157820807 238 ---EDNCIRGFLLE-------KGMRGLSAPRIEGKFSLRASAT---GMIIMDSVEVPEENVLPNVS 290
Cdd:PLN02443 194 tngKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTmdnGFLRFDHVRIPRDQMLMRLS 259
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
150-357 |
1.52e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 60.26 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 150 MSVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARHNPSNKSYTLS-----GTKTWITN 224
Cdd:PLN02636 141 LGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINtpndgAIKWWIGN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 225 SPVADLFV-VWARC----------EDNCIRGFLLE-KGMRGLSA-PRIE-----GKFSLRASATGMIIMDSVEVPEENV- 285
Cdd:PLN02636 221 AAVHGKFAtVFARLklpthdskgvSDMGVHAFIVPiRDMKTHQVlPGVEirdcgHKVGLNGVDNGALRFRSVRIPRDNLl 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 286 ---------------LPNVSS-LAGPFGCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVP------LARNQLVQK 343
Cdd:PLN02636 301 nrfgdvsrdgkytssLPTINKrFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQH 380
|
250
....*....|....
gi 157820807 344 KLADMLTEiTLGLH 357
Cdd:PLN02636 381 KLMPMLAS-TYAFH 393
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
108-419 |
3.74e-06 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 48.86 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 108 EMGELGVLGPtiKGYGCAGVS-SVAYGLLtRELERVDS------GYRSMMSVQSSLVmhpiytyGSEEQRQKYLPRLAKG 180
Cdd:cd01163 33 QSGLGTLRVP--KEYGGLGASlPDLYEVV-RELAAADSniaqalRAHFGFVEALLLA-------GPEQFRKRWFGRVLNG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 181 ELLGCfGLTEpNHGSDPGSMETR-ARHNPSnksYTLSGTKTWITNSPVADLFVVWARCEDNCIRGFLLEKGMRGLSapRI 259
Cdd:cd01163 103 WIFGN-AVSE-RGSVRPGTFLTAtVRDGGG---YVLNGKKFYSTGALFSDWVTVSALDEEGKLVFAAVPTDRPGIT--VV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 260 E--GKFSLRASATGMIIMDSVEVPEENVLPnvSSLAGPFGCLNTARYGI--TWGVLGAAEFCLHTARQYALDR----IQF 331
Cdd:cd01163 176 DdwDGFGQRLTASGTVTFDNVRVEPDEVLP--RPNAPDRGTLLTAIYQLvlAAVLAGIARAALDDAVAYVRSRtrpwIHS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 332 GVPLAR-NQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSLLKRNNC------------GKALDIARQARDIL 398
Cdd:cd01163 254 GAESARdDPYVQQVVGDLAARLHAAEALVLQAARALDAAAAAGTALTAEARGEAalavaaakvvvtRLALDATSRLFEVG 333
|
330 340
....*....|....*....|.
gi 157820807 399 GGNGISDEYHVIRHAMNLEAV 419
Cdd:cd01163 334 GASATAREHNLDRHWRNARTH 354
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
213-439 |
2.66e-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: 46.19 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 213 YTLSGTKTWITNSPVADLFVVWARCEDNC----IRGFLLekgmrglsaPRIEGKF-------SLRASATGMIIMDSVEVP 281
Cdd:cd01159 120 YRVSGTWPFASGCDHADWILVGAIVEDDDggplPRAFVV---------PRAEYEIvdtwhvvGLRGTGSNTVVVDDVFVP 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 282 EENVLPNVSSLAGPFGCLNTARYGITWG----------VLGAAEFCLHTARQYALDRIQ---FGVPLARNQLVQKKLADM 348
Cdd:cd01159 191 EHRTLTAGDMMAGDGPGGSTPVYRMPLRqvfplsfaavSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 349 LTEITlglHACLQLGRLKDQ-------DKATPEMVSLLKRNNCGKALDIARQARDIL----GGNGISDEYHVIR-----H 412
Cdd:cd01159 271 AAELD---AARAFLERATRDlwahalaGGPIDVEERARIRRDAAYAAKLSAEAVDRLfhaaGGSALYTASPLQRiwrdiH 347
|
250 260
....*....|....*....|....*..
gi 157820807 413 AMNLEAVNTYEGThdihALILGRAITG 439
Cdd:cd01159 348 AAAQHAALNPETA----AEAYGRALLG 370
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
103-412 |
1.72e-04 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 44.02 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 103 RDIVYEMGELGVLGPTIKGYGCAGVSSVAYGLLTRELERvdsgyrSMMSVQ-------SSLVMHPIYTYGSEEQRQKYLP 175
Cdd:PLN02876 470 RKLLFEDNKHMVSGDSADQLLGAGLSNLEYGYLCEIMGR------SVWAPQvfncgapDTGNMEVLLRYGNKEQQLEWLI 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 176 RLAKGELLGCFGLTEPN-HGSDPGSMETRARHnpSNKSYTLSGTKTWITNS--PVADLFVVWARCEDNCIRG-----FLL 247
Cdd:PLN02876 544 PLLEGKIRSGFAMTEPQvASSDATNIECSIRR--QGDSYVINGTKWWTSGAmdPRCRVLIVMGKTDFNAPKHkqqsmILV 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 248 EKGMRGLSAPRIEGKFSLRASATGM--IIMDSVEVPEENVLPNVS---SLAGpfGCLNTARYGITWGVLGAAEFCLHTAR 322
Cdd:PLN02876 622 DIQTPGVQIKRPLLVFGFDDAPHGHaeISFENVRVPAKNILLGEGrgfEIAQ--GRLGPGRLHHCMRLIGAAERGMQLMV 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820807 323 QYALDRIQFGVPLARNQLVQKKLADMLTEIT----LGLHACLQLGRLKDQD-KATPEMVSLLKRNNCGKALDIARQardI 397
Cdd:PLN02876 700 QRALSRKAFGKLIAQHGSFLSDLAKCRVELEqtrlLVLEAADQLDRLGNKKaRGIIAMAKVAAPNMALKVLDMAMQ---V 776
|
330
....*....|....*
gi 157820807 398 LGGNGISDEYhVIRH 412
Cdd:PLN02876 777 HGAAGVSSDT-VLAH 790
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
151-221 |
3.14e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 43.30 E-value: 3.14e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157820807 151 SVQSSLVMHPIYTYGSEEQRQKYLPRLAKGELLGCFGLTEPNHGSDPGSMETRARHNPSNKSYTL-----SGTKTW 221
Cdd:PTZ00460 96 TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIhtpsvEAVKFW 171
|
|
| |
