|
Name |
Accession |
Description |
Interval |
E-value |
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
40-426 |
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 1488385015 40 FDWRDALQLEKLLTPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTIKGYGCAGTTYVAYGLLA 119
Cdd:cd01151 1 FNWEDPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGYGCAGLSSVAYGLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 120 REIERVDSGYRSVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSsrKTYTLN 199
Cdd:cd01151 81 REVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDG--GGYKLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 200 GSKTWITNSPVADLCVVWAVC-HDGKIRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVSGLAGP 278
Cdd:cd01151 159 GSKTWITNSPIADVFVVWARNdETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 279 FGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDKETPEM 358
Cdd:cd01151 239 FKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQ 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1488385015 359 ISMLKRNSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAITGLQAF 426
Cdd:cd01151 319 ISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
52-425 |
1.26e-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: 373.79 E-value: 1.26e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 52 LTPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDSGYR 130
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIpEEYGGLGLSLVELALVLEELARADASLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 131 SVMSVQSSlVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSsrKTYTLNGSKTWITNSPV 210
Cdd:COG1960 85 LPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDG--DGYVLNGQKTFITNAPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 211 ADLCVVWAVCHDGK----IRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVS-GLAGPFGCLNNA 285
Cdd:COG1960 162 ADVILVLARTDPAAghrgISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGkGFKIAMSTLNAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 286 RYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDKETPEMISMLKRN 365
Cdd:COG1960 242 RLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLF 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 366 SCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAITGLQA 425
Cdd:COG1960 322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
54-418 |
2.16e-94 |
|
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: 286.87 E-value: 2.16e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 54 PEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVlgptikgygcagttyvaygllareiervdsgyrsvm 133
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLG------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 134 svqsslvMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYnsSRKTYTLNGSKTWITNSPVADL 213
Cdd:cd00567 45 -------AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARK--DGDGYVLNGRKIFISNGGDADL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 214 CVVWAVCHD-----GKIRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKV-SGLAGPFGCLNNARY 287
Cdd:cd00567 116 FIVLARTDEegpghRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEgGGFELAMKGLNVGRL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 288 GISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDK-ETPEMISMLKRNS 366
Cdd:cd00567 196 LLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPdEARLEAAMAKLFA 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1488385015 367 CGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGR 418
Cdd:cd00567 276 TEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
54-420 |
7.03e-92 |
|
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: 282.23 E-value: 7.03e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 54 PEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDSGYRSV 132
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIpEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 133 MSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRktYTLNGSKTWITNSPVAD 212
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDD--YVLNGSKMWITNGGEAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 213 LCVVWAVCHDGK----IRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVS-GLAGPFGCLNNARY 287
Cdd:cd01158 159 FYIVFAVTDPSKgyrgITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGeGFKIAMQTLDGGRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 288 GISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDKETPEMISMLKRNSC 367
Cdd:cd01158 239 GIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFAS 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1488385015 368 GKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAI 420
Cdd:cd01158 319 EVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
44-426 |
3.45e-90 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 279.04 E-value: 3.45e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 44 DALQLEKLLTPEEIMMRDSFRAYCQEKLMPriLMANRNEV--FHREIVSEMGTLGVLGPTIKGYGCAGTTYVAYGLLARE 121
Cdd:PLN02526 21 DYYQFDDLLTPEEQALRKRVRECMEKEVAP--IMTEYWEKaeFPFHIIPKLGSLGIAGGTIKGYGCPGLSITASAIATAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 122 IERVDSGYRSVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAqynssRKT---YTL 198
Cdd:PLN02526 99 VARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTA-----TKVeggWIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 199 NGSKTWITNSPVADLCVVWAVCHD-GKIRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVSGLAG 277
Cdd:PLN02526 174 NGQKRWIGNSTFADVLVIFARNTTtNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSFQD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 278 PFGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEItiglQACLQLG----RLKDEDK 353
Cdd:PLN02526 254 TNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNI----QAMFLVGwrlcKLYESGK 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1488385015 354 ETPEMISMLKRNSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAITGLQAF 426
Cdd:PLN02526 330 MTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIASF 402
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
52-420 |
4.46e-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: 228.83 E-value: 4.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 52 LTPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDSGYR 130
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITApEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 131 SVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRktYTLNGSKTWITNSPV 210
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDR--YVLNGSKMWITNGPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 211 ADLCVVWA----VCHDGKIRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVSG-----LAGpfgc 281
Cdd:cd01156 160 ADTLVVYAktdpSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKgvyvlMSG---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 282 LNNARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEitigLQACLQL----GRLKDEDKETPE 357
Cdd:cd01156 236 LDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTR----LNASRSYlytvAKACDRGNMDPK 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1488385015 358 MISMLKRNSCGKALEIARQARDMLGGNGIADEYHVIRHvmnLEAVNTYE---GTHDIHALILGRAI 420
Cdd:cd01156 312 DAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRL---LRDAKLYEigaGTSEIRRMVIGREL 374
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
34-424 |
6.38e-64 |
|
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: 6.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 34 KVPKAQFDWRDALQLEKLLTPEEIMmrDSFRAYCQEKLMPRILMANRNEVFHR-EIVSEMGTLGVLGPtiKGYGCAGTTY 112
Cdd:cd01161 11 IVTKQVFPYPSVLTEEQTEELNMLV--GPVEKFFEEVNDPAKNDQLEKIPRKTlTQLKELGLFGLQVP--EEYGGLGLNN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 113 VAYGLLArEIERVDSGYRSVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSS 192
Cdd:cd01161 87 TQYARLA-EIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSED 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 193 RKTYTLNGSKTWITNSPVADLCVVWA----VCHDG----KIRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVP 264
Cdd:cd01161 166 GKHYVLNGSKIWITNGGIADIFTVFAktevKDATGsvkdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 265 EENLLPKV-SGLAGPFGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADM-----LTEITIG 338
Cdd:cd01161 246 VENVLGEVgDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMailqyATESMAY 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 339 LQACLQLGRLKDEDKETPEMISMLKRNScgkALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILgr 418
Cdd:cd01161 326 MTSGNMDRGLKAEYQIEAAISKVFASEA---AWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI-- 400
|
....*.
gi 1488385015 419 AITGLQ 424
Cdd:cd01161 401 ALTGLQ 406
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
54-420 |
4.95e-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: 4.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 54 PEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVdSGYRSV 132
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFpEEYGGIGGDLLSAAVLWEELARA-GGSGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 133 MSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRktYTLNGSKTWITNSPVAD 212
Cdd:cd01160 80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDH--YVLNGSKTFITNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 213 LCVVWAVChDGKIRG------FLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVS-GLAGPFGCLNNA 285
Cdd:cd01160 158 VVIVVART-GGEARGaggislFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENkGFYYLMQNLPQE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 286 RYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIG---LQACLQLgrlkDEDKETPEM-ISM 361
Cdd:cd01160 237 RLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTrafLDNCAWR----HEQGRLDVAeASM 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 362 LKrNSCGKAL-EIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAI 420
Cdd:cd01160 313 AK-YWATELQnRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
52-422 |
2.37e-52 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 179.95 E-value: 2.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 52 LTPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTIKG-YGCAGTTYVAYGLLAREIERVDSGYR 130
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDdVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 131 SVMSVQSsLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRktYTLNGSKTWITNSPV 210
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDH--YVLNGSKAFISGAGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 211 ADLCVVwaVCHDGK-----IRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLL-PKVSGLAGPFGCLNN 284
Cdd:cd01162 158 SDVYVV--MARTGGegpkgISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLgGEGQGFGIAMAGLNG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 285 ARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEitigLQACLQLGR-----LKDEDKETPEMI 359
Cdd:cd01162 236 GRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATE----LVASRLMVRraasaLDRGDPDAVKLC 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1488385015 360 SMLKRNSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAITG 422
Cdd:cd01162 312 AMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
51-418 |
1.08e-50 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 176.22 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 51 LLTPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREI--VSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDS 127
Cdd:PLN02519 25 LFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITApEEYGGLGLGYLYHCIAMEEISRASG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 128 GYRSVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQynSSRKTYTLNGSKTWITN 207
Cdd:PLN02519 105 SVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAE--RVDGGYVLNGNKMWCTN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 208 SPVADLCVVWA----VCHDGKIRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVS-GLAGPFGCL 282
Cdd:PLN02519 183 GPVAQTLVVYAktdvAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGkGVYVMMSGL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 283 NNARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDKETPEMISML 362
Cdd:PLN02519 263 DLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGV 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1488385015 363 KRNSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGR 418
Cdd:PLN02519 343 ILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGR 398
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
53-334 |
5.48e-46 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 163.95 E-value: 5.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 53 TPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDSGYRS 131
Cdd:PTZ00461 38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVpEADGGAGMDAVAAVIIHHELSKYDPGFCL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 132 VMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRKtYTLNGSKTWITNSPVA 211
Cdd:PTZ00461 118 AYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGN-YVLNGSKIWITNGTVA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 212 DLCVVWAVChDGKIRGFLLERGMKGLST-PKIEgKFSLRASLTGMIIMEDVEVPEENLL-PKVSGLAGPFGCLNNARYGI 289
Cdd:PTZ00461 197 DVFLIYAKV-DGKITAFVVERGTKGFTQgPKID-KCGMRASHMCQLFFEDVVVPAENLLgEEGKGMVGMMRNLELERVTL 274
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1488385015 290 SWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTE 334
Cdd:PTZ00461 275 AAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYAD 319
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
52-422 |
4.16e-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: 150.04 E-value: 4.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 52 LTPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDSGYR 130
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIpEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 131 SVMSVqSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRktYTLNGSKTWITNSPV 210
Cdd:cd01157 81 TAIEA-NSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDE--YIINGQKMWITNGGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 211 ADLCVVWA------VCHDGK-IRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLL-PKVSGLAGPFGCL 282
Cdd:cd01157 158 ANWYFLLArsdpdpKCPASKaFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLiGEGAGFKIAMGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 283 NNARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDKETPEMISML 362
Cdd:cd01157 238 DKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 363 KRNSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAITG 422
Cdd:cd01157 318 KAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
53-164 |
5.84e-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: 5.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 53 TPEEIMMRDSFRAYCQEKLMPRILMANRNEVFHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDSGYRS 131
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIpEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 1488385015 132 VMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGE 164
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
105-421 |
2.30e-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: 115.56 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 105 YGCAGTTYVAYGLLAREIERVDSGyrSVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSME 184
Cdd:cd01153 59 YGGQGLPITVYSALAEIFSRGDAP--LMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 185 TRAQYnSSRKTYTLNGSKTWITNSpvadlcvvwavCHDG--KIRGFLLER------GMKGLS---TPK------------ 241
Cdd:cd01153 137 TKAVY-QADGSWRINGVKRFISAG-----------EHDMseNIVHLVLARsegappGVKGLSlflVPKflddgerngvtv 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 242 --IEGKFSLRASLTGMIIMEDVEVP---EENllpkvSGLAGPFGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRA 316
Cdd:cd01153 205 arIEEKMGLHGSPTCELVFDNAKGEligEEG-----MGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 317 PLA-------------RNQLIQKKL-------ADM--LTEITIGLQACLQLGRLKDEDKETPEMISMLKRNSCGKALEIA 374
Cdd:cd01153 280 LIKaapavtiihhpdvRRSLMTQKAyaegsraLDLytATVQDLAERKATEGEDRKALSALADLLTPVVKGFGSEAALEAV 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1488385015 375 RQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHAL-ILGRAIT 421
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 ... |
273-420 |
1.05e-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: 107.34 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 273 SGLAGPFGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDED 352
Cdd:pfam00441 2 RGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1488385015 353 KETPEMISMLKRNSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAI 420
Cdd:pfam00441 82 GPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
168-259 |
1.87e-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: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 168 CFGLTEPNHGSDPGSMETRAqYNSSRKTYTLNGSKTWITNSPVADLCVVWAVCH----DGKIRGFLLERGMKGLSTPKIE 243
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLNGTKWWITNAGIADLFLVLARTGgddrHGGISLFLVPKDAPGVSVRRIE 79
|
90
....*....|....*.
gi 1488385015 244 GKFSLRASLTGMIIME 259
Cdd:pfam02770 80 TKLGVRGLPTGELVFD 95
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
138-420 |
2.25e-23 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 100.96 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 138 SLVMHPIYAYGTEKQKQK-YLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSrKTYtLNGSKTWITNSPVADLCVV 216
Cdd:PRK12341 90 GQCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNG-KVY-LNGQKTFITGAKEYPYMLV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 217 WAVCHDGK-----IRGFLLERGMKGLSTPKIEgKFSLRASLTGMIIMEDVEVPEENLLPKVS-GLAGPFGCLNNARYGIS 290
Cdd:PRK12341 168 LARDPQPKdpkkaFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGmGFLNVMYNFEMERLINA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 291 WGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEI----TIGLQACLQlgrlkdEDKETPEMIS--MLKR 364
Cdd:PRK12341 247 ARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIenmrNMVYKVAWQ------ADNGQSLRTSaaLAKL 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1488385015 365 NSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAI 420
Cdd:PRK12341 321 YCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQI 376
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
148-420 |
6.94e-22 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 96.44 E-value: 6.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 148 GTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETraQYNSSRKTYTLNGSKTWITNSPVADLCVVWAVCHDGKIRG 227
Cdd:PRK03354 101 GTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKT--TYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 228 ----FLLERGMKGLSTPKIEgKFSLRASLTGMIIMEDVEVPEENLLPKV-SGLAGPFGCLNNARYGISWGALGAAEFCMH 302
Cdd:PRK03354 179 vyteWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREgNGFNRVKEEFDHERFLVALTNYGTAMCAFE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 303 TARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDKETPEMISMLKRNSCGKALEIARQARDMLG 382
Cdd:PRK03354 258 DAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLG 337
|
250 260 270
....*....|....*....|....*....|....*...
gi 1488385015 383 GNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAI 420
Cdd:PRK03354 338 GVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAV 375
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
144-420 |
4.17e-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: 4.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 144 IYAYGTEKQKQkYLPGLA----KGELLGCFGLTEPNHGSDPGSMETRAQYNSSrKTYTLNGSKtWITNSPVADLCVVWA- 218
Cdd:cd01154 123 LRKYGPEELKQ-YLPGLLsdryKTGLLGGTWMTEKQGGSDLGANETTAERSGG-GVYRLNGHK-WFASAPLADAALVLAr 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 219 -VCHDGKIRG---FLLER-----GMKGLSTPKIEGKFSLRASLTGMIIMEDVEVpeENLLPKVSGLAGPFGCLNNARYGI 289
Cdd:cd01154 200 pEGAPAGARGlslFLVPRlledgTRNGYRIRRLKDKLGTRSVATGEVEFDDAEA--YLIGDEGKGIYYILEMLNISRLDN 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 290 SWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDE---DKETPEMIS-----M 361
Cdd:cd01154 278 AVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRaaaDKPVEAHMArlatpV 357
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1488385015 362 LKRNSCGKALEIARQARDMLGGNGIADEYHVIRHVMNLEAVNTYEGTHDIHALILGRAI 420
Cdd:cd01154 358 AKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVL 416
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
54-382 |
1.37e-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: 77.77 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 54 PEEIMMRDSFRAYCQEKLMPRILMANRNEV-----FHREIVSEMGTLGVLGPTI-KGYGCAGTTYVAYGLLAREIERVDS 127
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPELREESALGYregreDRRRWQRALAAAGWAAPGWpKEYGGRGASLMEQLIFREEMAAAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 128 GYRSVMSVQSSLVmHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRktYTLNGSKTWITN 207
Cdd:cd01152 81 PVPFNQIGIDLAG-PTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDD--WVVNGQKIWTSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 208 SPVADLCVVWAVC------HDGkIRGFLLErgmkgLSTPKIEGKfSLRaSLTG-----MIIMEDVEVPEENLLPKV-SGL 275
Cdd:cd01152 158 AHYADWAWLLVRTdpeapkHRG-ISILLVD-----MDSPGVTVR-PIR-SINGgeffnEVFLDDVRVPDANRVGEVnDGW 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 276 AGPFGCLNNARygISWGALGAAEFCMHTARQYTLDRmqFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDEDKET 355
Cdd:cd01152 230 KVAMTTLNFER--VSIGGSAATFFELLLARLLLLTR--DGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPP 305
|
330 340
....*....|....*....|....*..
gi 1488385015 356 PEMISMLKRNSCGKALEIARQARDMLG 382
Cdd:cd01152 306 GAEASIAKLFGSELAQELAELALELLG 332
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
123-407 |
8.73e-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: 76.21 E-value: 8.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 123 ERVDSGYRSVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRKTYTLN--- 199
Cdd:cd01150 92 GGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFVINtpd 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 200 --GSKTWITNSPV-ADLCVVWA-VCHDGKIRG---FLLE-RGMKGLST-PKIE-----GKFSLRASLTGMIIMEDVEVPE 265
Cdd:cd01150 172 ftATKWWPGNLGKtATHAVVFAqLITPGKNHGlhaFIVPiRDPKTHQPlPGVTvgdigPKMGLNGVDNGFLQFRNVRIPR 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 266 ENLLPK-----------------VSGLAGPFGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRAP----------- 317
Cdd:cd01150 252 ENLLNRfgdvspdgtyvspfkdpNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKpsdpevqildy 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 318 ----------LARNQLI---QKKLADMLTEITIGLQAclqlgRLKDEDKETPEMISMLK---RNSCGKALEIARQArdmL 381
Cdd:cd01150 332 qlqqyrlfpqLAAAYAFhfaAKSLVEMYHEIIKELLQ-----GNSELLAELHALSAGLKavaTWTAAQGIQECREA---C 403
|
330 340
....*....|....*....|....*...
gi 1488385015 382 GGNGIADE--YHVIRhVMNlEAVNTYEG 407
Cdd:cd01150 404 GGHGYLAMnrLPTLR-DDN-DPFCTYEG 429
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
139-211 |
9.78e-15 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 76.39 E-value: 9.78e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1488385015 139 LVMHpiyaYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSME-----TRAQYNSSRKTY-TLNGSKTWITNSPVA 211
Cdd:PRK09463 171 LLLH----YGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLGmRLTWNKRYITLAPIA 245
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
131-388 |
2.88e-14 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 74.99 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 131 SVMsVQSSL-----VMHpiyaYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSME-----TRAQYNsSRKT--YTL 198
Cdd:PRK13026 158 TVM-VPNSLgpgelLTH----YGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFE-GEEVlgLRL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 199 NGSKTWITNSPVADLCVVWAVCHDGKirGFLLERGMKGL-------STPKIE-GKfslRASLTGMIIM------EDVEVP 264
Cdd:PRK13026 232 TWDKRYITLAPVATVLGLAFKLRDPD--GLLGDKKELGItcaliptDHPGVEiGR---RHNPLGMAFMngttrgKDVFIP 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 265 EENLL--PKVSGLagpfG------CLNNARyGISWGALGAA--EFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTe 334
Cdd:PRK13026 307 LDWIIggPDYAGR----GwrmlveCLSAGR-GISLPALGTAsgHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAG- 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1488385015 335 ITIGLQACLQLGRLKDEDKETPEMIS-MLKRNscgkALEIARQ----ARDMLGGNGIAD 388
Cdd:PRK13026 381 NTYLLEAARRLTTTGLDLGVKPSVVTaIAKYH----MTELARDvvndAMDIHAGKGIQL 435
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
105-316 |
3.33e-12 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 68.36 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 105 YGCAGTTYvAYGLLAREIERVDSGYRSVMSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSME 184
Cdd:PTZ00456 122 YGGQALPL-SVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 185 TRAQyNSSRKTYTLNGSKTWIT----NSPVADLCVVWAVCHDGK-----IRGFLLERGMK----GLSTPK------IEGK 245
Cdd:PTZ00456 201 TKAE-PSADGSYKITGTKIFISagdhDLTENIVHIVLARLPNSLpttkgLSLFLVPRHVVkpdgSLETAKnvkcigLEKK 279
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1488385015 246 FSLRASLTGMIIMEDVE---VPEENllpkvSGLAGPFGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRA 316
Cdd:PTZ00456 280 MGIKGSSTCQLSFENSVgylIGEPN-----AGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMRA 348
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
133-332 |
6.78e-12 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 67.58 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 133 MSVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRKTYTLN-----GSKTWITN 207
Cdd:PLN02636 141 LGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINtpndgAIKWWIGN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 208 SPV-ADLCVVWA----VCHDGK------IRGFLLE-RGMKGLST-PKIE-----GKFSLRASLTGMIIMEDVEVPEENL- 268
Cdd:PLN02636 221 AAVhGKFATVFArlklPTHDSKgvsdmgVHAFIVPiRDMKTHQVlPGVEirdcgHKVGLNGVDNGALRFRSVRIPRDNLl 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 269 ---------------LPKVSG-LAGPFGCLNNARYGISWGALGAAEFCMHTARQYTLDRMQFRAP------LARNQLIQK 326
Cdd:PLN02636 301 nrfgdvsrdgkytssLPTINKrFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQH 380
|
....*.
gi 1488385015 327 KLADML 332
Cdd:PLN02636 381 KLMPML 386
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
141-390 |
1.53e-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: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 141 MHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPN-HGSDPGSMETRAQYNSSrkTYTLNGSKTWITNSPVADlCVVWAV 219
Cdd:cd01155 101 MEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGD--DYVINGRKWWSSGAGDPR-CKIAIV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 220 ChdGKIRGFLLERGMKG------LSTPKIEGKFSLraSLTGM---------IIMEDVEVPEENL-LPKVSGLAGPFGCLN 283
Cdd:cd01155 178 M--GRTDPDGAPRHRQQsmilvpMDTPGVTIIRPL--SVFGYddaphghaeITFDNVRVPASNLiLGEGRGFEIAQGRLG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 284 NARYGISWGALGAAEFCMHTARQYTLDRMQFRAPLARNQLIQKKLADMLTEITIGLQACLQLGRLKDE--DKETPEMISM 361
Cdd:cd01155 254 PGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTvgNKAARKEIAM 333
|
250 260
....*....|....*....|....*....
gi 1488385015 362 LKRNSCGKALEIARQARDMLGGNGIADEY 390
Cdd:cd01155 334 IKVAAPRMALKIIDRAIQVHGAAGVSQDT 362
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
86-308 |
9.95e-08 |
|
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: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 86 REIVSEMGTLGVLGPtiKGYGCAGTTYVAYGLLAREIERVDS------GYRSVMSVQSSLVmhpiyayGTEKQKQKYLPG 159
Cdd:cd01163 28 VALLRQSGLGTLRVP--KEYGGLGASLPDLYEVVRELAAADSniaqalRAHFGFVEALLLA-------GPEQFRKRWFGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 160 LAKGELLGCfGLTEpNHGSDPGSMETRAQYNSSrkTYTLNGSKTWITNSPVADLCVVWAVCHDGKIRGFLLERGMKGLST 239
Cdd:cd01163 99 VLNGWIFGN-AVSE-RGSVRPGTFLTATVRDGG--GYVLNGKKFYSTGALFSDWVTVSALDEEGKLVFAAVPTDRPGITV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1488385015 240 PKIEGKFSLRASLTGMIIMEDVEVPEENLLPKVSglAGPFGCLNNARY---------GISWGALG-AAEFCMHTARQYT 308
Cdd:cd01163 175 VDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPN--APDRGTLLTAIYqlvlaavlaGIARAALDdAVAYVRSRTRPWI 251
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
144-273 |
1.26e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 54.07 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 144 IYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRKTY-----TLNGSKTWITN-SPVADLCVVW 217
Cdd:PLN02443 110 IKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFvihspTLTSSKWWPGGlGKVSTHAVVY 189
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 218 A-VCHDGK---IRGFLLE-RGMK------GLSTPKIEGKFSLRASLT---GMIIMEDVEVPEENLLPKVS 273
Cdd:PLN02443 190 ArLITNGKdhgIHGFIVQlRSLDdhsplpGVTVGDIGMKFGNGAYNTmdnGFLRFDHVRIPRDQMLMRLS 259
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
148-314 |
3.70e-06 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 49.39 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 148 GTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRKTYTLN-----GSKTWITNSPV-ADLCVVWAVCH 221
Cdd:PLN02312 168 GTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINtpcesAQKYWIGGAANhATHTIVFSQLH 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 222 -DGKIRG---FLLE-RGMKGLSTPKIE-----GKFSLRASLTGMIIMEDVEVPEENLLPKV----------SGLAGP--- 278
Cdd:PLN02312 248 iNGKNEGvhaFIAQiRDQDGNICPNIRiadcgHKIGLNGVDNGRIWFDNLRIPRENLLNSVadvspdgkyvSAIKDPdqr 327
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1488385015 279 FGC----LNNARYGISWGALGAAEFCMHTARQYTLDRMQF 314
Cdd:PLN02312 328 FGAflapLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
196-422 |
7.63e-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: 41.57 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 196 YTLNGSKTWITNSPVADlcvvWAVC------HDGK--IRGFLLERgmkglSTPKIEGKFS---LRASLTGMIIMEDVEVP 264
Cdd:cd01159 120 YRVSGTWPFASGCDHAD----WILVgaivedDDGGplPRAFVVPR-----AEYEIVDTWHvvgLRGTGSNTVVVDDVFVP 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 265 EENLLPKVSGLAGPFGCLNNARYGISWG----------ALGAAEFCMHTARQYTLDRMQ---FRAPLARNQLIQKKLADM 331
Cdd:cd01159 191 EHRTLTAGDMMAGDGPGGSTPVYRMPLRqvfplsfaavSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 332 LTEITiglQACLQLGRLKDE-------DKETPEMISMLKRNSCGKALEIARQARDML----GGNGIADEYHVIR-----H 395
Cdd:cd01159 271 AAELD---AARAFLERATRDlwahalaGGPIDVEERARIRRDAAYAAKLSAEAVDRLfhaaGGSALYTASPLQRiwrdiH 347
|
250 260
....*....|....*....|....*..
gi 1488385015 396 VMNLEAVNTYEGThdihALILGRAITG 422
Cdd:cd01159 348 AAAQHAALNPETA----AEAYGRALLG 370
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
134-418 |
1.02e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 41.37 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 134 SVQSSLVMHPIYAYGTEKQKQKYLPGLAKGELLGCFGLTEPNHGSDPGSMETRAQYNSSRKTYTLN-----GSKTWitns 208
Cdd:PTZ00460 96 TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFW---- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 209 P-----VADLCVVWA-VCHDGK----------IRGFLLERGMKGLSTPKIEGKFSLRASLTGMIIMEDVEVPEENLLPKV 272
Cdd:PTZ00460 172 PgelgfLCNFALVYAkLIVNGKnkgvhpfmvrIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLARY 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 273 SGLA--GPFGCLNNARygISWGAL------------GAAEFCMHTARQYTLDRMQFR------APLARNQLIQKKLADML 332
Cdd:PTZ00460 252 IKVSedGQVERQGNPK--VSYASMmymrnliidqypRFAAQALTVAIRYSIYRQQFTndnkqeNSVLEYQTQQQKLLPLL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488385015 333 TEITIGLQACLQLGRLKDED------------KETPEMISMLKRNSCGKALEIARQARDMLGGNGIAdEYHVIRHVMNLE 400
Cdd:PTZ00460 330 AEFYACIFGGLKIKELVDDNfnrvqkndfsllQLTHAILSAAKANYTYFVSNCAEWCRLSCGGHGYA-HYSGLPAIYFDM 408
|
330
....*....|....*....
gi 1488385015 401 AVN-TYEGTHDIHALILGR 418
Cdd:PTZ00460 409 SPNiTLEGENQIMYLQLAR 427
|
|
|