|
Name |
Accession |
Description |
Interval |
E-value |
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
52-438 |
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: 738.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 52 FDWRDALQLEKLLTPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTIKGYGCAGTTYVAYGLLA 131
Cdd:cd01151 1 FNWEDPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGYGCAGLSSVAYGLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 132 REIERVDSGYRSVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSsrKTYTLN 211
Cdd:cd01151 81 REVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDG--GGYKLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 212 GSKTWITNSPVADLCVVWAVC-HDGKIRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVSGLAGP 290
Cdd:cd01151 159 GSKTWITNSPIADVFVVWARNdETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 291 FGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDKETPEM 370
Cdd:cd01151 239 FKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQ 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1488385013 371 ISMLKRNSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAITGLQAF 438
Cdd:cd01151 319 ISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
64-437 |
4.27e-128 |
|
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: 375.33 E-value: 4.27e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 64 LTPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDSGYR 142
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIpEEYGGLGLSLVELALVLEELARADASLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 143 SVMSVQSSlVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSsrKTYTLNGSKTWITNSPV 222
Cdd:COG1960 85 LPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDG--DGYVLNGQKTFITNAPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 223 ADLCVVWAVCHDGK----IRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVS-GLAGPFGCLNNA 297
Cdd:COG1960 162 ADVILVLARTDPAAghrgISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGkGFKIAMSTLNAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 298 RYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDKETPEMISMLKRN 377
Cdd:COG1960 242 RLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLF 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 378 SCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAITGLQA 437
Cdd:COG1960 322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
66-430 |
8.61e-95 |
|
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: 288.41 E-value: 8.61e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 66 PEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVlgptikgygcagttyvaygllareiervdsgyrsvm 145
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLG------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 146 svqsslvMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYnsSRKTYTLNGSKTWITNSPVADL 225
Cdd:cd00567 45 -------AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARK--DGDGYVLNGRKIFISNGGDADL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 226 CVVWAVCHD-----GKIRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKV-SGLAGPFGCLNNARY 299
Cdd:cd00567 116 FIVLARTDEegpghRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEgGGFELAMKGLNVGRL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 300 GISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDK-ETPEMISMLKRNS 378
Cdd:cd00567 196 LLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPdEARLEAAMAKLFA 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1488385013 379 CGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGR 430
Cdd:cd00567 276 TEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
66-432 |
1.21e-91 |
|
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: 281.85 E-value: 1.21e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 66 PEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDSGYRSV 144
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIpEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 145 MSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRktYTLNGSKTWITNSPVAD 224
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDD--YVLNGSKMWITNGGEAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 225 LCVVWAVCHDGK----IRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVS-GLAGPFGCLNNARY 299
Cdd:cd01158 159 FYIVFAVTDPSKgyrgITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGeGFKIAMQTLDGGRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 300 GISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDKETPEMISMLKRNSC 379
Cdd:cd01158 239 GIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFAS 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1488385013 380 GKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAI 432
Cdd:cd01158 319 EVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
56-438 |
5.03e-90 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 279.04 E-value: 5.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 56 DALQLEKLLTPEEIMMRDSFRAYCQEKLMPriLMANRNEV--FHREIVSEMGTLGVLGPTIKGYGCAGTTYVAYGLLARE 133
Cdd:PLN02526 21 DYYQFDDLLTPEEQALRKRVRECMEKEVAP--IMTEYWEKaeFPFHIIPKLGSLGIAGGTIKGYGCPGLSITASAIATAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 134 IERVDSGYRSVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAqynssRKT---YTL 210
Cdd:PLN02526 99 VARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTA-----TKVeggWIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 211 NGSKTWITNSPVADLCVVWAVCHD-GKIRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVSGLAG 289
Cdd:PLN02526 174 NGQKRWIGNSTFADVLVIFARNTTtNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSFQD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 290 PFGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEItiglQACLQLG----RLKDEDK 365
Cdd:PLN02526 254 TNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNI----QAMFLVGwrlcKLYESGK 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1488385013 366 ETPEMISMLKRNSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAITGLQAF 438
Cdd:PLN02526 330 MTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIASF 402
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
64-432 |
6.98e-71 |
|
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: 228.45 E-value: 6.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 64 LTPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDSGYR 142
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITApEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 143 SVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRktYTLNGSKTWITNSPV 222
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDR--YVLNGSKMWITNGPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 223 ADLCVVWA----VCHDGKIRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVSG-----LAGpfgc 293
Cdd:cd01156 160 ADTLVVYAktdpSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKgvyvlMSG---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 294 LNNARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEitigLQACLQL----GRLKDEDKETPE 369
Cdd:cd01156 236 LDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTR----LNASRSYlytvAKACDRGNMDPK 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1488385013 370 MISMLKRNSCGKALEIARQARDMLGGNGIADEYHVIRHvmnLEAVNTYE---GTHDIHALILGRAI 432
Cdd:cd01156 312 DAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRL---LRDAKLYEigaGTSEIRRMVIGREL 374
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
41-436 |
8.29e-65 |
|
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: 213.87 E-value: 8.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 41 LVNGSKVPKAQFDWRDALQLEKLLTPEEIMmrDSFRAYCQEKLMPRILMANRNEVFHR-EIVSEMGTLGVLGPtiKGYGC 119
Cdd:cd01161 6 MFLGDIVTKQVFPYPSVLTEEQTEELNMLV--GPVEKFFEEVNDPAKNDQLEKIPRKTlTQLKELGLFGLQVP--EEYGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 120 AGTTYVAYGLLArEIERVDSGYRSVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRA 199
Cdd:cd01161 82 LGLNNTQYARLA-EIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 200 QYNSSRKTYTLNGSKTWITNSPVADLCVVWA----VCHDG----KIRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIME 271
Cdd:cd01161 161 VLSEDGKHYVLNGSKIWITNGGIADIFTVFAktevKDATGsvkdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 272 DVEVPEENLLPKV-SGLAGPFGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADM-----LT 345
Cdd:cd01161 241 DVKIPVENVLGEVgDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMailqyAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 346 EITIGLQACLQLGRLKDEDKETPEMISMLKRNScgkALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHA 425
Cdd:cd01161 321 ESMAYMTSGNMDRGLKAEYQIEAAISKVFASEA---AWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILR 397
|
410
....*....|.
gi 1488385013 426 LILgrAITGLQ 436
Cdd:cd01161 398 LFI--ALTGLQ 406
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
66-432 |
6.74e-59 |
|
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: 197.34 E-value: 6.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 66 PEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVdSGYRSV 144
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFpEEYGGIGGDLLSAAVLWEELARA-GGSGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 145 MSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRktYTLNGSKTWITNSPVAD 224
Cdd:cd01160 80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDH--YVLNGSKTFITNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 225 LCVVWAVChDGKIRG------FLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVS-GLAGPFGCLNNA 297
Cdd:cd01160 158 VVIVVART-GGEARGaggislFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENkGFYYLMQNLPQE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 298 RYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIG---LQACLQLgrlkDEDKETPEM-ISM 373
Cdd:cd01160 237 RLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTrafLDNCAWR----HEQGRLDVAeASM 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 374 LKrNSCGKAL-EIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAI 432
Cdd:cd01160 313 AK-YWATELQnRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
64-434 |
2.24e-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: 180.33 E-value: 2.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 64 LTPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTIKG-YGCAGTTYVAYGLLAREIERVDSGYR 142
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDdVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 143 SVMSVQSsLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRktYTLNGSKTWITNSPV 222
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDH--YVLNGSKAFISGAGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 223 ADLCVVwaVCHDGK-----IRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLL-PKVSGLAGPFGCLNN 296
Cdd:cd01162 158 SDVYVV--MARTGGegpkgISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLgGEGQGFGIAMAGLNG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 297 ARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEitigLQACLQLGR-----LKDEDKETPEMI 371
Cdd:cd01162 236 GRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATE----LVASRLMVRraasaLDRGDPDAVKLC 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1488385013 372 SMLKRNSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAITG 434
Cdd:cd01162 312 AMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
63-430 |
1.74e-50 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 175.84 E-value: 1.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 63 LLTPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREI--VSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDS 139
Cdd:PLN02519 25 LFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITApEEYGGLGLGYLYHCIAMEEISRASG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 140 GYRSVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQynSSRKTYTLNGSKTWITN 219
Cdd:PLN02519 105 SVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAE--RVDGGYVLNGNKMWCTN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 220 SPVADLCVVWA----VCHDGKIRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVS-GLAGPFGCL 294
Cdd:PLN02519 183 GPVAQTLVVYAktdvAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGkGVYVMMSGL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 295 NNARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDKETPEMISML 374
Cdd:PLN02519 263 DLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGV 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1488385013 375 KRNSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGR 430
Cdd:PLN02519 343 ILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGR 398
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
65-346 |
8.08e-46 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 163.57 E-value: 8.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 65 TPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDSGYRS 143
Cdd:PTZ00461 38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVpEADGGAGMDAVAAVIIHHELSKYDPGFCL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 144 VMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRKtYTLNGSKTWITNSPVA 223
Cdd:PTZ00461 118 AYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGN-YVLNGSKIWITNGTVA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 224 DLCVVWAVChDGKIRGFLLERGMKGLST-PKIEgKFSLRASLTGMIIMEDVEVPEENLL-PKVSGLAGPFGCLNNARYGI 301
Cdd:PTZ00461 197 DVFLIYAKV-DGKITAFVVERGTKGFTQgPKID-KCGMRASHMCQLFFEDVVVPAENLLgEEGKGMVGMMRNLELERVTL 274
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1488385013 302 SWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTE 346
Cdd:PTZ00461 275 AAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYAD 319
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
65-176 |
6.93e-41 |
|
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: 141.45 E-value: 6.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 65 TPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDSGYRS 143
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIpEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 1488385013 144 VMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGE 176
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
64-434 |
8.32e-41 |
|
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: 149.27 E-value: 8.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 64 LTPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDSGYR 142
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIpEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 143 SVMSVqSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRktYTLNGSKTWITNSPV 222
Cdd:cd01157 81 TAIEA-NSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDE--YIINGQKMWITNGGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 223 ADLCVVWA------VCHDGK-IRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLL-PKVSGLAGPFGCL 294
Cdd:cd01157 158 ANWYFLLArsdpdpKCPASKaFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLiGEGAGFKIAMGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 295 NNARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDKETPEMISML 374
Cdd:cd01157 238 DKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 375 KRNSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAITG 434
Cdd:cd01157 318 KAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
117-433 |
1.96e-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: 115.95 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 117 YGCAGTTYVAYGLLAREIERVDSGyrSVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSME 196
Cdd:cd01153 59 YGGQGLPITVYSALAEIFSRGDAP--LMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 197 TRAQYnSSRKTYTLNGSKTWITNSpvadlcvvwavCHDG--KIRGFLLER------GMKGLS---TPK------------ 253
Cdd:cd01153 137 TKAVY-QADGSWRINGVKRFISAG-----------EHDMseNIVHLVLARsegappGVKGLSlflVPKflddgerngvtv 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 254 --IEGKFSLRASLTGMIIMEDVEVP---EENllpkvSGLAGPFGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRA 328
Cdd:cd01153 205 arIEEKMGLHGSPTCELVFDNAKGEligEEG-----MGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 329 PLA-------------RNQLIQKKL-------ADM--LTEITIGLQACLQLGRLKDEDKETPEMISMLKRNSCGKALEIA 386
Cdd:cd01153 280 LIKaapavtiihhpdvRRSLMTQKAyaegsraLDLytATVQDLAERKATEGEDRKALSALADLLTPVVKGFGSEAALEAV 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1488385013 387 RQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHAL-ILGRAIT 433
Cdd:cd01153 360 SDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALdLIGRKIV 407
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
285-432 |
6.01e-28 |
|
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: 108.11 E-value: 6.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 285 SGLAGPFGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDED 364
Cdd:pfam00441 2 RGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1488385013 365 KETPEMISMLKRNSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAI 432
Cdd:pfam00441 82 GPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
180-271 |
2.06e-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: 93.88 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 180 CFGLTEPNHGSDPGSMETRAqYNSSRKTYTLNGSKTWITNSPVADLCVVWAVCH----DGKIRGFLLERGMKGLSTPKIE 255
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLNGTKWWITNAGIADLFLVLARTGgddrHGGISLFLVPKDAPGVSVRRIE 79
|
90
....*....|....*.
gi 1488385013 256 GKFSLRASLTGMIIME 271
Cdd:pfam02770 80 TKLGVRGLPTGELVFD 95
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
150-432 |
2.23e-23 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 100.96 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 150 SLVMHPIYAYGTEKQKQK-YLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSrKTYtLNGSKTWITNSPVADLCVV 228
Cdd:PRK12341 90 GQCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNG-KVY-LNGQKTFITGAKEYPYMLV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 229 WAVCHDGK-----IRGFLLERGMKGLSTPKIEgKFSLRASLTGMIIMEDVEVPEENLLPKVS-GLAGPFGCLNNARYGIS 302
Cdd:PRK12341 168 LARDPQPKdpkkaFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGmGFLNVMYNFEMERLINA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 303 WGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEI----TIGLQACLQlgrlkdEDKETPEMIS--MLKR 376
Cdd:PRK12341 247 ARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIenmrNMVYKVAWQ------ADNGQSLRTSaaLAKL 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1488385013 377 NSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAI 432
Cdd:PRK12341 321 YCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQI 376
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
160-432 |
7.77e-22 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 96.44 E-value: 7.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 160 GTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETraQYNSSRKTYTLNGSKTWITNSPVADLCVVWAVCHDGKIRG 239
Cdd:PRK03354 101 GTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKT--TYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 240 ----FLLERGMKGLSTPKIEgKFSLRASLTGMIIMEDVEVPEENLLPKV-SGLAGPFGCLNNARYGISWGALGAAEFCMH 314
Cdd:PRK03354 179 vyteWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREgNGFNRVKEEFDHERFLVALTNYGTAMCAFE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 315 TARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDKETPEMISMLKRNSCGKALEIARQARDMLG 394
Cdd:PRK03354 258 DAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLG 337
|
250 260 270
....*....|....*....|....*....|....*...
gi 1488385013 395 GNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAI 432
Cdd:PRK03354 338 GVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAV 375
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
156-432 |
3.76e-18 |
|
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: 85.89 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 156 IYAYGTEKQKQkYLPGLA----KGELLGCFGLTEPNHGSDPGSMETRAQYNSSrKTYTLNGSKtWITNSPVADLCVVWA- 230
Cdd:cd01154 123 LRKYGPEELKQ-YLPGLLsdryKTGLLGGTWMTEKQGGSDLGANETTAERSGG-GVYRLNGHK-WFASAPLADAALVLAr 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 231 -VCHDGKIRG---FLLER-----GMKGLSTPKIEGKFSLRASLTGMIIMEDVEVpeENLLPKVSGLAGPFGCLNNARYGI 301
Cdd:cd01154 200 pEGAPAGARGlslFLVPRlledgTRNGYRIRRLKDKLGTRSVATGEVEFDDAEA--YLIGDEGKGIYYILEMLNISRLDN 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 302 SWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDE---DKETPEMIS-----M 373
Cdd:cd01154 278 AVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRaaaDKPVEAHMArlatpV 357
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1488385013 374 LKRNSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAI 432
Cdd:cd01154 358 AKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVL 416
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
66-394 |
1.29e-15 |
|
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: 78.16 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 66 PEEIMMRDSFRAYCQEKLMPRILMANRNEV-----FHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDS 139
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPELREESALGYregreDRRRWQRALAAAGWAAPGWpKEYGGRGASLMEQLIFREEMAAAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 140 GYRSVMSVQSSLVmHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRktYTLNGSKTWITN 219
Cdd:cd01152 81 PVPFNQIGIDLAG-PTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDD--WVVNGQKIWTSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 220 SPVADLCVVWAVC------HDGkIRGFLLErgmkgLSTPKIEGKfSLRaSLTG-----MIIMEDVEVPEENLLPKV-SGL 287
Cdd:cd01152 158 AHYADWAWLLVRTdpeapkHRG-ISILLVD-----MDSPGVTVR-PIR-SINGgeffnEVFLDDVRVPDANRVGEVnDGW 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 288 AGPFGCLNNARygISWGALGAAEFCMHTARQYTLDRmqFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDKET 367
Cdd:cd01152 230 KVAMTTLNFER--VSIGGSAATFFELLLARLLLLTR--DGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPP 305
|
330 340
....*....|....*....|....*..
gi 1488385013 368 PEMISMLKRNSCGKALEIARQARDMLG 394
Cdd:cd01152 306 GAEASIAKLFGSELAQELAELALELLG 332
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
130-419 |
7.76e-15 |
|
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: 76.60 E-value: 7.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 130 LAREIERVDSGYRSVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRKTYT 209
Cdd:cd01150 87 LTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 210 LN-----GSKTWITNSPV-ADLCVVWA-VCHDGKIRG---FLLE-RGMKGLST-PKIE-----GKFSLRASLTGMIIMED 272
Cdd:cd01150 167 INtpdftATKWWPGNLGKtATHAVVFAqLITPGKNHGlhaFIVPiRDPKTHQPlPGVTvgdigPKMGLNGVDNGFLQFRN 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 273 VEVPEENLLPK-----------------VSGLAGPFGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRAP------ 329
Cdd:cd01150 247 VRIPRENLLNRfgdvspdgtyvspfkdpNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKpsdpev 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 330 ---------------LARNQLI---QKKLADMLTEITIGLQAclqlgRLKDEDKETPEMISMLK---RNSCGKALEIARQ 388
Cdd:cd01150 327 qildyqlqqyrlfpqLAAAYAFhfaAKSLVEMYHEIIKELLQ-----GNSELLAELHALSAGLKavaTWTAAQGIQECRE 401
|
330 340 350
....*....|....*....|....*....|...
gi 1488385013 389 ArdmLGGNGIADE--YHVIRhVMNlEAVNTYEG 419
Cdd:cd01150 402 A---CGGHGYLAMnrLPTLR-DDN-DPFCTYEG 429
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
151-223 |
9.54e-15 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 76.39 E-value: 9.54e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1488385013 151 LVMHpiyaYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSME-----TRAQYNSSRKTY-TLNGSKTWITNSPVA 223
Cdd:PRK09463 171 LLLH----YGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLGmRLTWNKRYITLAPIA 245
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
143-400 |
2.73e-14 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 74.99 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 143 SVMsVQSSL-----VMHpiyaYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSME-----TRAQYNsSRKT--YTL 210
Cdd:PRK13026 158 TVM-VPNSLgpgelLTH----YGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFE-GEEVlgLRL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 211 NGSKTWITNSPVADLCVVWAVCHDGKirGFLLERGMKGL-------STPKIE-GKfslRASLTGMIIM------EDVEVP 276
Cdd:PRK13026 232 TWDKRYITLAPVATVLGLAFKLRDPD--GLLGDKKELGItcaliptDHPGVEiGR---RHNPLGMAFMngttrgKDVFIP 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 277 EENLL--PKVSGLagpfG------CLNNARyGISWGALGAA--EFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTe 346
Cdd:PRK13026 307 LDWIIggPDYAGR----GwrmlveCLSAGR-GISLPALGTAsgHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAG- 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1488385013 347 ITIGLQACLQLGRLKDEDKETPEMIS-MLKRNscgkALEIARQ----ARDMLGGNGIAD 400
Cdd:PRK13026 381 NTYLLEAARRLTTTGLDLGVKPSVVTaIAKYH----MTELARDvvndAMDIHAGKGIQL 435
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
117-328 |
3.31e-12 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 68.36 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 117 YGCAGTTYvAYGLLAREIERVDSGYRSVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSME 196
Cdd:PTZ00456 122 YGGQALPL-SVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 197 TRAQyNSSRKTYTLNGSKTWIT----NSPVADLCVVWAVCHDGK-----IRGFLLERGMK----GLSTPK------IEGK 257
Cdd:PTZ00456 201 TKAE-PSADGSYKITGTKIFISagdhDLTENIVHIVLARLPNSLpttkgLSLFLVPRHVVkpdgSLETAKnvkcigLEKK 279
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1488385013 258 FSLRASLTGMIIMEDVE---VPEENllpkvSGLAGPFGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRA 328
Cdd:PTZ00456 280 MGIKGSSTCQLSFENSVgylIGEPN-----AGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMRA 348
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
145-344 |
7.28e-12 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 67.58 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 145 MSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRKTYTLN-----GSKTWITN 219
Cdd:PLN02636 141 LGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINtpndgAIKWWIGN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 220 SPV-ADLCVVWA----VCHDGK------IRGFLLE-RGMKGLST-PKIE-----GKFSLRASLTGMIIMEDVEVPEENL- 280
Cdd:PLN02636 221 AAVhGKFATVFArlklPTHDSKgvsdmgVHAFIVPiRDMKTHQVlPGVEirdcgHKVGLNGVDNGALRFRSVRIPRDNLl 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 281 ---------------LPKVSG-LAGPFGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRAP------LARNQLIQK 338
Cdd:PLN02636 301 nrfgdvsrdgkytssLPTINKrFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQH 380
|
....*.
gi 1488385013 339 KLADML 344
Cdd:PLN02636 381 KLMPML 386
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
153-402 |
1.72e-10 |
|
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: 62.41 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 153 MHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPN-HGSDPGSMETRAQYNSSrkTYTLNGSKTWITNSPVADlCVVWAV 231
Cdd:cd01155 101 MEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGD--DYVINGRKWWSSGAGDPR-CKIAIV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 232 ChdGKIRGFLLERGMKG------LSTPKIEGKFSLraSLTGM---------IIMEDVEVPEENL-LPKVSGLAGPFGCLN 295
Cdd:cd01155 178 M--GRTDPDGAPRHRQQsmilvpMDTPGVTIIRPL--SVFGYddaphghaeITFDNVRVPASNLiLGEGRGFEIAQGRLG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 296 NARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDE--DKETPEMISM 373
Cdd:cd01155 254 PGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTvgNKAARKEIAM 333
|
250 260
....*....|....*....|....*....
gi 1488385013 374 LKRNSCGKALEIARQARDMLGGNGIADEY 402
Cdd:cd01155 334 IKVAAPRMALKIIDRAIQVHGAAGVSQDT 362
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
98-320 |
1.05e-07 |
|
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: 53.48 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 98 REIVSEMGTLGVLGPtiKGYGCAGTTYVAYGLLAREIERVDS------GYRSVMSVQSSLVmhpiyayGTEKQKQKYLPG 171
Cdd:cd01163 28 VALLRQSGLGTLRVP--KEYGGLGASLPDLYEVVRELAAADSniaqalRAHFGFVEALLLA-------GPEQFRKRWFGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 172 LAKGELLGCfGLTEpNHGSDPGSMETRAQYNSSrkTYTLNGSKTWITNSPVADLCVVWAVCHDGKIRGFLLERGMKGLST 251
Cdd:cd01163 99 VLNGWIFGN-AVSE-RGSVRPGTFLTATVRDGG--GYVLNGKKFYSTGALFSDWVTVSALDEEGKLVFAAVPTDRPGITV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1488385013 252 PKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVSglAGPFGCLNNARY---------GISWGALG-AAEFCMHTARQYT 320
Cdd:cd01163 175 VDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPN--APDRGTLLTAIYqlvlaavlaGIARAALDdAVAYVRSRTRPWI 251
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
156-285 |
1.33e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 54.07 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 156 IYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRKTY-----TLNGSKTWITN-SPVADLCVVW 229
Cdd:PLN02443 110 IKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFvihspTLTSSKWWPGGlGKVSTHAVVY 189
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 230 A-VCHDGK---IRGFLLE-RGMK------GLSTPKIEGKFSLRASLT---GMIIMEDVEVPEENLLPKVS 285
Cdd:PLN02443 190 ArLITNGKdhgIHGFIVQlRSLDdhsplpGVTVGDIGMKFGNGAYNTmdnGFLRFDHVRIPRDQMLMRLS 259
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
160-326 |
3.56e-06 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 49.39 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 160 GTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRKTYTLN-----GSKTWITNSPV-ADLCVVWAVCH 233
Cdd:PLN02312 168 GTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINtpcesAQKYWIGGAANhATHTIVFSQLH 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 234 -DGKIRG---FLLE-RGMKGLSTPKIE-----GKFSLRASLTGMIIMEDVEVPEENLLPKV----------SGLAGP--- 290
Cdd:PLN02312 248 iNGKNEGvhaFIAQiRDQDGNICPNIRiadcgHKIGLNGVDNGRIWFDNLRIPRENLLNSVadvspdgkyvSAIKDPdqr 327
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1488385013 291 FGC----LNNARYGISWGALGAAEFCMHTARQYTLDRMQF 326
Cdd:PLN02312 328 FGAflapLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
208-434 |
5.85e-04 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 41.95 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 208 YTLNGSKTWITNSPVADlcvvWAVC------HDGK--IRGFLLERgmkglSTPKIEGKFS---LRASLTGMIIMEDVEVP 276
Cdd:cd01159 120 YRVSGTWPFASGCDHAD----WILVgaivedDDGGplPRAFVVPR-----AEYEIVDTWHvvgLRGTGSNTVVVDDVFVP 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 277 EENLLPKVSGLAGPFGCLNNARYGISWG----------ALGAAEFCMHTARQYTLDRMQ---FRAPLARNQLIQKKLADM 343
Cdd:cd01159 191 EHRTLTAGDMMAGDGPGGSTPVYRMPLRqvfplsfaavSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 344 LTEITiglQACLQLGRLKDE-------DKETPEMISMLKRNSCGKALEIARQARDML----GGNGIADEYHVIR-----H 407
Cdd:cd01159 271 AAELD---AARAFLERATRDlwahalaGGPIDVEERARIRRDAAYAAKLSAEAVDRLfhaaGGSALYTASPLQRiwrdiH 347
|
250 260
....*....|....*....|....*..
gi 1488385013 408 VMNLEAVNTYEGThdihALILGRAITG 434
Cdd:cd01159 348 AAAQHAALNPETA----AEAYGRALLG 370
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
146-430 |
1.06e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 41.37 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 146 SVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRKTYTLN-----GSKTWitns 220
Cdd:PTZ00460 96 TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFW---- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 221 P-----VADLCVVWA-VCHDGK----------IRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKV 284
Cdd:PTZ00460 172 PgelgfLCNFALVYAkLIVNGKnkgvhpfmvrIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLARY 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 285 SGLA--GPFGCLNNARygISWGAL------------GAAEFCMHTARQYTLDRMQFR------APLARNQLIQKKLADML 344
Cdd:PTZ00460 252 IKVSedGQVERQGNPK--VSYASMmymrnliidqypRFAAQALTVAIRYSIYRQQFTndnkqeNSVLEYQTQQQKLLPLL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385013 345 TEITIGLQACLQLGRLKDED------------KETPEMISMLKRNSCGKALEIARQARDMLGGNGIAdEYHVIRHVMNLE 412
Cdd:PTZ00460 330 AEFYACIFGGLKIKELVDDNfnrvqkndfsllQLTHAILSAAKANYTYFVSNCAEWCRLSCGGHGYA-HYSGLPAIYFDM 408
|
330
....*....|....*....
gi 1488385013 413 AVN-TYEGTHDIHALILGR 430
Cdd:PTZ00460 409 SPNiTLEGENQIMYLQLAR 427
|
|
| |
