|
Name |
Accession |
Description |
Interval |
E-value |
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
29-417 |
0e+00 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 748.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 29 FNWQDPLNLESQLTEEEVAIRDAFRGYCQAELQPRVKMANRLETFDKKIMEEIGSLGVLGCTIKGYGCAGVSSVAYGLLT 108
Cdd:cd01151 1 FNWEDPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGYGCAGLSSVAYGLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 109 REVERVDSAYRSAVSVQSSLAMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKYDSKskTYILN 188
Cdd:cd01151 81 REVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGG--GYKLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 189 GSKTWITSAPIADVIVVWAKC-EDGKVRGFLVDRKIsgKGLETPKIEGKFSLRASPTGMILMDEVRVPEEQLLPNVAGFS 267
Cdd:cd01151 159 GSKTWITNSPIADVFVVWARNdETGKIRGFILERGM--KGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 268 GPFSCLNNARYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLADAITEIALGLQACLHVGRLKDQKLHTP 347
Cdd:cd01151 237 GPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATP 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 348 DMISLLKRNNTGKSLDIARQMRDMLGANGISDEYHVIRHVINLESVNTYEGTHDIHALILGRAITGLAAF 417
Cdd:cd01151 317 EQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
40-416 |
1.07e-126 |
|
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: 371.09 E-value: 1.07e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 40 QLTEEEVAIRDAFRGYCQAELQPRVKMANRLETFDKKIMEEIGSLGVLGCTI-KGYGCAGVSSVAYGLLTREVERVDSAY 118
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIpEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 119 RSAVSVQSSlAMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKYDSKskTYILNGSKTWITSAP 198
Cdd:COG1960 84 ALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGD--GYVLNGQKTFITNAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 199 IADVIVVWAKCEDGK----VRGFLVDRKIsgKGLETPKIEGKFSLRASPTGMILMDEVRVPEEQLLPNV-AGFSGPFSCL 273
Cdd:COG1960 161 VADVILVLARTDPAAghrgISLFLVPKDT--PGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEgKGFKIAMSTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 274 NNARYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLADAITEIALGLQACLHVGRLKDQKLHTPDMISLL 353
Cdd:COG1960 239 NAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19920834 354 KRNNTGKSLDIARQMRDMLGANGISDEYHVIRHVINLESVNTYEGTHDIHALILGRAITGLAA 416
Cdd:COG1960 319 KLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
33-417 |
1.80e-90 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 279.43 E-value: 1.80e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 33 DPLNLESQLTEEEVAIRDAFRGYCQAELQPrvKMANRLET--FDKKIMEEIGSLGVLGCTIKGYGCAGVSSVAYGLLTRE 110
Cdd:PLN02526 21 DYYQFDDLLTPEEQALRKRVRECMEKEVAP--IMTEYWEKaeFPFHIIPKLGSLGIAGGTIKGYGCPGLSITASAIATAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 111 VERVDSAYRSAVSVQSSLAMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKydSKSKTYILNGS 190
Cdd:PLN02526 99 VARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTAT--KVEGGWILNGQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 191 KTWITSAPIADVIVVWAK-CEDGKVRGFLVdrKISGKGLETPKIEGKFSLRASPTGMILMDEVRVPEEQLLPNVAGFSGP 269
Cdd:PLN02526 177 KRWIGNSTFADVLVIFARnTTTNQINGFIV--KKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSFQDT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 270 FSCLNNARYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLADAITEIalglQACLHVG----RLKDQKLH 345
Cdd:PLN02526 255 NKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNI----QAMFLVGwrlcKLYESGKM 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19920834 346 TPDMISLLKRNNTGKSLDIARQMRDMLGANGISDEYHVIRHVINLESVNTYEGTHDIHALILGRAITGLAAF 417
Cdd:PLN02526 331 TPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIASF 402
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
43-409 |
6.43e-83 |
|
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: 257.21 E-value: 6.43e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 43 EEEVAIRDAFRGYCQAELQPRVKMANRLETFDKKIMEEIGSLGVlgctikgygcagvssvayglltrevervdsayrsav 122
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLG------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 123 svqsslaMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKYDSKSktYILNGSKTWITSAPIADV 202
Cdd:cd00567 45 -------AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG--YVLNGRKIFISNGGDADL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 203 IVVWAKCEDGKVRG-----FLVDRKIsgKGLETPKIEGKFSLRASPTGMILMDEVRVPEEQLLPNV-AGFSGPFSCLNNA 276
Cdd:cd00567 116 FIVLARTDEEGPGHrgisaFLVPADT--PGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEgGGFELAMKGLNVG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 277 RYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLADAITEIALGLQACLHVGRLKDQ-KLHTPDMISLLKR 355
Cdd:cd00567 194 RLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQgPDEARLEAAMAKL 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 19920834 356 NNTGKSLDIARQMRDMLGANGISDEYHVIRHVINLESVNTYEGTHDIHALILGR 409
Cdd:cd00567 274 FATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
43-411 |
1.73e-82 |
|
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: 257.58 E-value: 1.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 43 EEEVAIRDAFRGYCQAELQPRVKMANRLETFDKKIMEEIGSLGVLGCTI-KGYGCAGVSSVAYGLLTREVERVDSAYRSA 121
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIpEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 122 VSVQSSLAMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKYDSKSktYILNGSKTWITSAPIAD 201
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDD--YVLNGSKMWITNGGEAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 202 VIVVWAKCEDGK----VRGFLVDRkiSGKGLETPKIEGKFSLRASPTGMILMDEVRVPEEQLLPNVA-GFSGPFSCLNNA 276
Cdd:cd01158 159 FYIVFAVTDPSKgyrgITAFIVER--DTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGeGFKIAMQTLDGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 277 RYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLADAITEI----ALGLQAclhvGRLKDQKLHTPDMISL 352
Cdd:cd01158 237 RIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIeaarLLTYKA----ARLKDNGEPFIKEAAM 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 19920834 353 LKRNNTGKSLDIARQMRDMLGANGISDEYHVIRHVINLESVNTYEGTHDIHALILGRAI 411
Cdd:cd01158 313 AKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
41-411 |
9.89e-63 |
|
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: 206.49 E-value: 9.89e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 41 LTEEEVAIRDAFRGYCQAELQPRVKMANRLETFDKKIMEEIGSLGVLGCTI-KGYGCAGVSSVAYGLLTREVERVDSAYR 119
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITApEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 120 SAVSVQSSLAMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAkyDSKSKTYILNGSKTWITSAPI 199
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--EKKGDRYVLNGSKMWITNGPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 200 ADVIVVWAKCE-DGKVRG---FLVDRkiSGKGLETPKIEGKFSLRASPTGMILMDEVRVPEEQLLPNVAG-----FSGpf 270
Cdd:cd01156 160 ADTLVVYAKTDpSAGAHGitaFIVEK--GMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKgvyvlMSG-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 271 scLNNARYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLADAITEialgLQAC----LHVGRLKDQKLHT 346
Cdd:cd01156 236 --LDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTR----LNASrsylYTVAKACDRGNMD 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19920834 347 PDMISLLKRNNTGKSLDIARQMRDMLGANGISDEYHVIRHvinLESVNTYE---GTHDIHALILGRAI 411
Cdd:cd01156 310 PKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRL---LRDAKLYEigaGTSEIRRMVIGREL 374
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
33-414 |
4.82e-62 |
|
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: 205.78 E-value: 4.82e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 33 DPLNLESQLTEEEVAIRDAFRGYCQAELQPRVKmaNRLETFDKKIMEEIGSLGVLGCTI-KGYGCAGVSSVAYGLLTrEV 111
Cdd:cd01161 19 YPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKN--DQLEKIPRKTLTQLKELGLFGLQVpEEYGGLGLNNTQYARLA-EI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 112 ERVDSAYRSAVSVQSSLAMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKYDSKSKTYILNGSK 191
Cdd:cd01161 96 VGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKHYVLNGSK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 192 TWITSAPIADVIVVWAKCE----DG----KVRGFLVDRkiSGKGLETPKIEGKFSLRASPTGMILMDEVRVPEEQLLPNV 263
Cdd:cd01161 176 IWITNGGIADIFTVFAKTEvkdaTGsvkdKITAFIVER--SFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 264 A-GFSGPFSCLNNARYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLADAITEIALGLQACLHVGRLKDQ 342
Cdd:cd01161 254 GdGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDR 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19920834 343 KLhTPD------MISLLKRNNTGKSLDIARQmrdMLGANGISDEYHVIRHVINLESVNTYEGTHDIHALILgrAITGL 414
Cdd:cd01161 334 GL-KAEyqieaaISKVFASEAAWLVVDEAIQ---IHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI--ALTGL 405
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
43-411 |
6.16e-55 |
|
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: 186.17 E-value: 6.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 43 EEEVAIRDAFRGYCQAELQPRVKMANRLETFDKKIMEEIGSLGVLGCTI-KGYGCAGVSSVAYGLLTREVERVdSAYRSA 121
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFpEEYGGIGGDLLSAAVLWEELARA-GGSGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 122 VSVQSSLAMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKYDSKSktYILNGSKTWITSAPIAD 201
Cdd:cd01160 80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDH--YVLNGSKTFITNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 202 VIVVWAKcEDGKVRG------FLVDRKIsgKGLETPKIEGKFSLRASPTGMILMDEVRVPEEQLLPNV-AGFSGPFSCLN 274
Cdd:cd01160 158 VVIVVAR-TGGEARGaggislFLVERGT--PGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEEnKGFYYLMQNLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 275 NARYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLADAITEIALGLQACLHVGRLKDQKLHTPDMISLLK 354
Cdd:cd01160 235 QERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAK 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 19920834 355 RNNTGKSLDIARQMRDMLGANGISDEYHVIRHVINLESVNTYEGTHDIHALILGRAI 411
Cdd:cd01160 315 YWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
41-413 |
2.24e-53 |
|
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: 182.26 E-value: 2.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 41 LTEEEVAIRDAFRGYCQAELQPRVKMANRLETFDKKIMEEIGSLGVLGCTIKG-YGCAGVSSVAYGLLTREVERVDSAYR 119
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDdVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 120 SAVSVQSsLAMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKYDSKSktYILNGSKTWITSAPI 199
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDH--YVLNGSKAFISGAGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 200 ADVIVVWAKCEDGKVRG---FLVDRkiSGKGLETPKIEGKFSLRASPTGMILMDEVRVP-EEQLLPNVAGFSGPFSCLNN 275
Cdd:cd01162 158 SDVYVVMARTGGEGPKGiscFVVEK--GTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPvENRLGGEGQGFGIAMAGLNG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 276 ARYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLADAITEialgLQACLHVGRLKDQKLH--TPDMISLL 353
Cdd:cd01162 236 GRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATE----LVASRLMVRRAASALDrgDPDAVKLC 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19920834 354 ---KRNNTGKSLDIARQMRDMLGANGISDEYHVIRHVINLESVNTYEGTHDIHALILGRAITG 413
Cdd:cd01162 312 amaKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
12-330 |
1.78e-49 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 172.81 E-value: 1.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 12 PCARRLASTSSKAAAPKFNWQDPlnlesqlTEEEVAIRDAFRGYCQAELQPRVKMANRLETFDKKIMEEIGSLGVLGCTI 91
Cdd:PTZ00461 15 TCGWTAAATMTSASRAFMDLYNP-------TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 92 -KGYGCAGVSSVAYGLLTREVERVDSAYRSAVSVQSSLAMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPA 170
Cdd:PTZ00461 88 pEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 171 GMETRAKYDSKSKtYILNGSKTWITSAPIADVIVVWAKCeDGKVRGFLVDRKISGKGlETPKIEgKFSLRASPTGMILMD 250
Cdd:PTZ00461 168 GMRTTAKKDSNGN-YVLNGSKIWITNGTVADVFLIYAKV-DGKITAFVVERGTKGFT-QGPKID-KCGMRASHMCQLFFE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 251 EVRVPEEQLLPNVA-GFSGPFSCLNNARYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLAD--AITEIA 327
Cdd:PTZ00461 244 DVVVPAENLLGEEGkGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEgyADTEAA 323
|
...
gi 19920834 328 LGL 330
Cdd:PTZ00461 324 KAL 326
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
41-413 |
9.25e-44 |
|
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: 156.98 E-value: 9.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 41 LTEEEVAIRDAFRGYCQAELQPRVKMANRLETFDKKIMEEIGSLGVLGCTI-KGYGCAGVSSVAYGLLTREVERVDSAYR 119
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIpEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 120 SAVSVqSSLAMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAkyDSKSKTYILNGSKTWITSAPI 199
Cdd:cd01157 81 TAIEA-NSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIINGQKMWITNGGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 200 ADVIVVWA------KCEDGKV-RGFLVDRKISGkgLETPKIEGKFSLRASPTGMILMDEVRVPEEQLL-PNVAGFSGPFS 271
Cdd:cd01157 158 ANWYFLLArsdpdpKCPASKAfTGFIVEADTPG--IQPGRKELNMGQRCSDTRGITFEDVRVPKENVLiGEGAGFKIAMG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 272 CLNNARYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLADaiteIALGLQaclhVGRLKDQKlhTPDMIS 351
Cdd:cd01157 236 AFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLAD----MAMKVE----LARLAYQR--AAWEVD 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19920834 352 LLKRNNTGKSL------DIARQMR----DMLGANGISDEYHVIRHVINLESVNTYEGTHDIHALILGRAITG 413
Cdd:cd01157 306 SGRRNTYYASIakafaaDIANQLAtdavQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
1-409 |
3.70e-40 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 147.72 E-value: 3.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 1 MIAQSVISKLRPCARRLASTSSKAAapkfnwqdplnlesqLTEEEVAIRDAFRGYCQAELQPRVKMANRLETFDKKI--M 78
Cdd:PLN02519 1 MLLSAAKARRRGLARRFSSSSSSLL---------------FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlW 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 79 EEIGSLGVLGCTI-KGYGCAGVSSVAYGLLTREVERVDSAYRSAVSVQSSLAMGAIYDFGSEEQKQRYLPSMAEGKLIGA 157
Cdd:PLN02519 66 KLMGDFNLHGITApEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 158 FGLTEPNHGSDPAGMETRAkyDSKSKTYILNGSKTWITSAPIADVIVVWAKCEDGK----VRGFLVDRKIsgKGLETPKI 233
Cdd:PLN02519 146 LAMSEPNSGSDVVSMKCKA--ERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAgskgITAFIIEKGM--PGFSTAQK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 234 EGKFSLRASPTGMILMDEVRVPEEQLLPNVA-GFSGPFSCLNNARYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAAN 312
Cdd:PLN02519 222 LDKLGMRGSDTCELVFENCFVPEENVLGQEGkGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 313 QLIQKKLADAITEIALGLQACLHVGRLKDQKLHTPDMISLLKRNNTGKSLDIARQMRDMLGANGISDEYHVIRHvinLES 392
Cdd:PLN02519 302 QFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRL---LRD 378
|
410 420
....*....|....*....|
gi 19920834 393 VNTYE---GTHDIHALILGR 409
Cdd:PLN02519 379 AKLYEigaGTSEIRRMLIGR 398
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
42-153 |
1.71e-36 |
|
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: 129.12 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 42 TEEEVAIRDAFRGYCQAELQPRVKMANRLETFDKKIMEEIGSLGVLGCTI-KGYGCAGVSSVAYGLLTREVERVDSAYRS 120
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIpEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 19920834 121 AVSVQSSLAMGAIYDFGSEEQKQRYLPSMAEGK 153
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
129-412 |
1.53e-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: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 129 AMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKYDsKSKTYILNGSKTWITSAP--IADVIV-- 204
Cdd:cd01153 92 AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQ-ADGSWRINGVKRFISAGEhdMSENIVhl 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 205 VWAKCEDGK--VRG---FLVDRKISGK---GLETPKIEGKFSLRASPTGMILMDEVRVP---EEQllpnvAGFSGPFSCL 273
Cdd:cd01153 171 VLARSEGAPpgVKGlslFLVPKFLDDGernGVTVARIEEKMGLHGSPTCELVFDNAKGEligEEG-----MGLAQMFAMM 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 274 NNARYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQ--------------LIQKKLADA--------ITEIALGLQ 331
Cdd:cd01153 246 NGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPavtiihhpdvrrslMTQKAYAEGsraldlytATVQDLAER 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 332 ACLHVGRLKDQKLHTPDMISLLKRNNTGKSLDIARQMRDMLGANGISDEYHVIRHVINLESVNTYEGTHDIHAL-ILGRA 410
Cdd:cd01153 326 KATEGEDRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALdLIGRK 405
|
..
gi 19920834 411 IT 412
Cdd:cd01153 406 IV 407
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
265-411 |
6.85e-27 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 105.03 E-value: 6.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 265 GFSGPFSCLNNARYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLADAITEIALGLQACLHVGRLKDQKL 344
Cdd:pfam00441 3 GFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGG 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19920834 345 HTPDMISLLKRNNTGKSLDIARQMRDMLGANGISDEYHVIRHVINLESVNTYEGTHDIHALILGRAI 411
Cdd:pfam00441 83 PDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
157-250 |
4.46e-24 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 95.42 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 157 AFGLTEPNHGSDPAGMETRAkYDSKSKTYILNGSKTWITSAPIADVIVVWAKCE----DGKVRGFLVDRkiSGKGLETPK 232
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLNGTKWWITNAGIADLFLVLARTGgddrHGGISLFLVPK--DAPGVSVRR 77
|
90
....*....|....*...
gi 19920834 233 IEGKFSLRASPTGMILMD 250
Cdd:pfam02770 78 IETKLGVRGLPTGELVFD 95
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
137-411 |
7.05e-21 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 93.36 E-value: 7.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 137 GSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETraKYDSKSKTYILNGSKTWITSAPIADVIVVWAKCEDGKVRG 216
Cdd:PRK03354 101 GTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKT--TYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 217 ----FLVDrkISGKGLETPKIEgKFSLRASPTGMILMDEVRVPEEQLLPNVA-GFSGPFSCLNNARYGIAWGALGAAETC 291
Cdd:PRK03354 179 vyteWFVD--MSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGnGFNRVKEEFDHERFLVALTNYGTAMCA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 292 VEIARQYTLDRKQFGRPLAANQLIQKKLADAITEIALGLQACLHVGRLKDQKLHTPDMISLLKRNNTGKSLDIARQMRDM 371
Cdd:PRK03354 256 FEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQV 335
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19920834 372 LGANGISDEYHVIRHVINLESVNTYEGTHDIHALILGRAI 411
Cdd:PRK03354 336 LGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAV 375
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
129-411 |
7.80e-21 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 93.59 E-value: 7.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 129 AMGAIYDFGSEEQKQrYLPSMAEGK----LIGAFGLTEPNHGSDPAGMETRAKYDSKSkTYILNGSKtWITSAPIADVIV 204
Cdd:cd01154 119 AVYALRKYGPEELKQ-YLPGLLSDRyktgLLGGTWMTEKQGGSDLGANETTAERSGGG-VYRLNGHK-WFASAPLADAAL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 205 VWAKCEDGK--VRG---FLVDRKI---SGKGLETPKIEGKFSLRASPTGMILMDEVrvpEEQLL-PNVAGFSGPFSCLNN 275
Cdd:cd01154 196 VLARPEGAPagARGlslFLVPRLLedgTRNGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIgDEGKGIYYILEMLNI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 276 ARYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLADAITEIALGLQACLHVGRLKDQKLHTPDMISLLKR 355
Cdd:cd01154 273 SRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAHMAR 352
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19920834 356 -------NNTGKSLD-IARQMRDMLGANGISDEYHVIRHVINLESVNTYEGTHDIHALILGRAI 411
Cdd:cd01154 353 latpvakLIACKRAApVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVL 416
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
107-308 |
3.04e-20 |
|
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: 93.16 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 107 LTREVERVDSAYRSAVSVQSSLAMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKYDSKSKTYI 186
Cdd:cd01150 87 LTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 187 LN-----GSKTWITS-APIADVIVVWAK-CEDGKVRG---FLV---DRK--ISGKGLETPKIEGKFSLRASPTGMILMDE 251
Cdd:cd01150 167 INtpdftATKWWPGNlGKTATHAVVFAQlITPGKNHGlhaFIVpirDPKthQPLPGVTVGDIGPKMGLNGVDNGFLQFRN 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19920834 252 VRVPEEQLL------------------PNVaGFSGPFSCLNNARYGIAWGALGAAETCVEIARQYTLDRKQFGRP 308
Cdd:cd01150 247 VRIPRENLLnrfgdvspdgtyvspfkdPNK-RYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPK 320
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
127-321 |
4.31e-19 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 88.25 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 127 SLAMGAIYDFGSEEQ-KQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETraKYDSKSKTYILNGSKTWITSAPIADVIVV 205
Cdd:PRK12341 90 GQCIHSMRRFGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATT--TYTRKNGKVYLNGQKTFITGAKEYPYMLV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 206 WAK--CEDGKVRGF---LVDrkISGKGLetpKIE--GKFSLRASPTGMILMDEVRVPEEQLLpNVAGfSGPFSCLNN--- 275
Cdd:PRK12341 168 LARdpQPKDPKKAFtlwWVD--SSKPGI---KINplHKIGWHMLSTCEVYLDNVEVEESDLV-GEEG-MGFLNVMYNfem 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 19920834 276 ARYGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLAD 321
Cdd:PRK12341 241 ERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTL 286
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
43-326 |
4.25e-18 |
|
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: 85.09 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 43 EEEVAIRDAFRGYCQAELQPRVKMANRLETFD--------KKIMEEIGSLGVlgCTIKGYGCAGVSSVAYGLLTREVERV 114
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPELREESALGYREgredrrrwQRALAAAGWAAP--GWPKEYGGRGASLMEQLIFREEMAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 115 DSAYRSAVSVQSSLAmGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKYDSKSktYILNGSKTWI 194
Cdd:cd01152 79 GAPVPFNQIGIDLAG-PTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDD--WVVNGQKIWT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 195 TSAPIADVIVVWAKcEDGKV---RG---FLVDrkisgkgLETPKIEGK--FSLRASP-TGMILMDEVRVPEEQLLPNV-A 264
Cdd:cd01152 156 SGAHYADWAWLLVR-TDPEApkhRGisiLLVD-------MDSPGVTVRpiRSINGGEfFNEVFLDDVRVPDANRVGEVnD 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19920834 265 GFSGPFSCLNNARYGIAwgalGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLADAITEI 326
Cdd:cd01152 228 GWKVAMTTLNFERVSIG----GSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEA 285
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
130-381 |
8.18e-18 |
|
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: 84.75 E-value: 8.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 130 MGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPN-HGSDPAGMETRAKYDSKSktYILNGSKTWITSA--PIADVIVVW 206
Cdd:cd01155 101 MEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDD--YVINGRKWWSSGAgdPRCKIAIVM 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 207 AKCE-DGKVRG-----FLVDRKISGKGLETPKieGKFSLRASPTGM--ILMDEVRVPEEQL-LPNVAGFSGPFSCLNNAR 277
Cdd:cd01155 179 GRTDpDGAPRHrqqsmILVPMDTPGVTIIRPL--SVFGYDDAPHGHaeITFDNVRVPASNLiLGEGRGFEIAQGRLGPGR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 278 YGIAWGALGAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLADAITEIALGLQACLHVGRLKDQK-----LHTPDMISL 352
Cdd:cd01155 257 IHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVgnkaaRKEIAMIKV 336
|
250 260
....*....|....*....|....*....
gi 19920834 353 LKRNNTGKSLDIARQMRdmlGANGISDEY 381
Cdd:cd01155 337 AAPRMALKIIDRAIQVH---GAAGVSQDT 362
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
28-323 |
2.58e-15 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 78.08 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 28 KFNWQDPLNL-ESQLTEEEVAIRDAfrgycqaELQPRVKMANRLETF--DKKIMEE----IGSLGVLGCTI-KGYGCAGV 99
Cdd:PRK13026 64 KPDWQKLHSYpKPTLTAEEQAFIDN-------EVETLLTMLDDWDIVqnRKDLPPEvwdyLKKEGFFALIIpKEYGGKGF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 100 SSVAYgllTREVERVDSAYRSA---VSVQSSLAMGA-IYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGME-- 173
Cdd:PRK13026 137 SAYAN---STIVSKIATRSVSAavtVMVPNSLGPGElLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdt 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 174 ---TRAKYDSKSKTYI-LNGSKTWITSAPIADVIVVWAKCEDGKvrGFLVDRKISG----------KGLETpkieGKfsl 239
Cdd:PRK13026 214 givCRGEFEGEEVLGLrLTWDKRYITLAPVATVLGLAFKLRDPD--GLLGDKKELGitcaliptdhPGVEI----GR--- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 240 RASPTGMILMD------EVRVPEEQLL--PNVAGfSG---PFSCLNNARyGIAWGALGAA--ETCVEIARQYTLDRKQFG 306
Cdd:PRK13026 285 RHNPLGMAFMNgttrgkDVFIPLDWIIggPDYAG-RGwrmLVECLSAGR-GISLPALGTAsgHMATRTTGAYAYVRRQFG 362
|
330
....*....|....*..
gi 19920834 307 RPLAANQLIQKKLADAI 323
Cdd:PRK13026 363 MPIGQFEGVQEALARIA 379
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
105-348 |
8.51e-14 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 72.98 E-value: 8.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 105 GLLTREVERVDSAYRSAVSVQSSLAMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKyDSKSKT 184
Cdd:PTZ00456 132 GFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAE-PSADGS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 185 YILNGSKTWITSAP---IADVI-VVWAKCEDGKVRG-----FLVDRKI--SGKGLETPK------IEGKFSLRASPTGMI 247
Cdd:PTZ00456 211 YKITGTKIFISAGDhdlTENIVhIVLARLPNSLPTTkglslFLVPRHVvkPDGSLETAKnvkcigLEKKMGIKGSSTCQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 248 LMDEVR---VPEEQllpnvAGFSGPFSCLNNARYGIAWGALGAAETCVEIARQYTLDRKQFgRPLAANQLIQKKlADAIT 324
Cdd:PTZ00456 291 SFENSVgylIGEPN-----AGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSM-RALSGTKEPEKP-ADRII 363
|
250 260 270
....*....|....*....|....*....|....*...
gi 19920834 325 -------------EIALGLQACLH-VGRLKDQKLHTPD 348
Cdd:PTZ00456 364 chanvrqnilfakAVAEGGRALLLdVGRLLDIHAAAKD 401
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
104-308 |
1.15e-12 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 69.89 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 104 YGLLTREVERVDSAYRSAVSVQSSLAMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKYDSKSK 183
Cdd:PLN02636 123 YFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 184 TYILN-----GSKTWITSAPI-ADVIVVWAK----CEDGK------VRGFLVDRKISGKGLETPKIE-----GKFSLRAS 242
Cdd:PLN02636 203 EFVINtpndgAIKWWIGNAAVhGKFATVFARlklpTHDSKgvsdmgVHAFIVPIRDMKTHQVLPGVEirdcgHKVGLNGV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 243 PTGMILMDEVRVPEEQL----------------LPNV-AGFSGPFSCLNNARYGIAWGALGAAETCVEIARQYTLDRKQF 305
Cdd:PLN02636 283 DNGALRFRSVRIPRDNLlnrfgdvsrdgkytssLPTInKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQF 362
|
...
gi 19920834 306 GRP 308
Cdd:PLN02636 363 GPP 365
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
132-306 |
1.17e-12 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 69.48 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 132 AIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKYDSKSKTYILN-----GSKTWITS-APIADVIVV 205
Cdd:PLN02443 109 AIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHsptltSSKWWPGGlGKVSTHAVV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 206 WAKC----EDGKVRGFLV-----DRKISGKGLETPKIEGKFSLRASPT---GMILMDEVRVPEEQLLPNVAGFSGPFSCL 273
Cdd:PLN02443 189 YARLitngKDHGIHGFIVqlrslDDHSPLPGVTVGDIGMKFGNGAYNTmdnGFLRFDHVRIPRDQMLMRLSKVTREGKYV 268
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 19920834 274 NN-------------ARYGIAWGALGAAETCVEIARQYTLDRKQFG 306
Cdd:PLN02443 269 QSdvprqlvygtmvyVRQTIVADASTALSRAVCIATRYSAVRRQFG 314
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
30-203 |
1.24e-12 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 69.85 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 30 NWQDPLNL-ESQLTEEEVAIRDafrGYCQaELqprVKMANrletfDKKIMEEIGSL-----------GVLGCTI-KGYGC 96
Cdd:PRK09463 67 DWKKLLNYpKPTLTAEEQAFLD---GPVE-EL---CRMVN-----DWQITHELADLppevwqfikehGFFGMIIpKEYGG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 97 AGVSSVAYGLLTREVERVDSAYRSAVSVQSSLAMGAIY-DFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGME-- 173
Cdd:PRK09463 135 LEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLGPGELLlHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPdt 214
|
170 180 190
....*....|....*....|....*....|....
gi 19920834 174 ---TRAKYDSKSKTYI-LNGSKTWITSAPIADVI 203
Cdd:PRK09463 215 gvvCKGEWQGEEVLGMrLTWNKRYITLAPIATVL 248
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
131-313 |
3.42e-11 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 65.18 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 131 GAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKYDSKSKTYILN-----GSKTWITSAPI-ADVIV 204
Cdd:PLN02312 162 GAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINtpcesAQKYWIGGAANhATHTI 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 205 VWAKCE-DGK---VRGFLVD-RKISGKGLETPKIEG---KFSLRASPTGMILMDEVRVPEEQLLPNVAG----------- 265
Cdd:PLN02312 242 VFSQLHiNGKnegVHAFIAQiRDQDGNICPNIRIADcghKIGLNGVDNGRIWFDNLRIPRENLLNSVADvspdgkyvsai 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 19920834 266 ------FSGPFSCLNNARYGIAWGALGAAETCVEIARQYTLDRKQFGrpLAANQ 313
Cdd:PLN02312 322 kdpdqrFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAFS--VTPNG 373
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
130-387 |
8.83e-10 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 60.58 E-value: 8.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 130 MGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPN-HGSDPAGMETRAKYDSKSktYILNGSKTWITSA--PIADVIVVW 206
Cdd:PLN02876 526 MEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDS--YVINGTKWWTSGAmdPRCRVLIVM 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 207 AKCEDGKVRG-----FLVDRKISGKGLETPKIegKFSLRASPTGM--ILMDEVRVPEEQLLpnvagfsgpfscLNNAR-Y 278
Cdd:PLN02876 604 GKTDFNAPKHkqqsmILVDIQTPGVQIKRPLL--VFGFDDAPHGHaeISFENVRVPAKNIL------------LGEGRgF 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 279 GIAWGAL------------GAAETCVEIARQYTLDRKQFGRPLAANQLIQKKLADAITEIA----LGLQACLHVGRLKDQ 342
Cdd:PLN02876 670 EIAQGRLgpgrlhhcmrliGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEqtrlLVLEAADQLDRLGNK 749
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 19920834 343 KLH-TPDMISLLKRNNTGKSLDIARQMRdmlGANGISDEYhVIRHV 387
Cdd:PLN02876 750 KARgIIAMAKVAAPNMALKVLDMAMQVH---GAAGVSSDT-VLAHL 791
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
123-305 |
9.08e-07 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 51.00 E-value: 9.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 123 SVQSSLAMGAIYDFGSEEQKQRYLPSMAEGKLIGAFGLTEPNHGSDPAGMETRAKYDSKSKTYILN-----GSKTWitsa 197
Cdd:PTZ00460 96 TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFW---- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 198 P-----IADVIVVWAKCE-DGKVRG---FLVdrKISGK-------GLETPKIEGKFSLRASPTGMILMDEVRVPEEQLLP 261
Cdd:PTZ00460 172 PgelgfLCNFALVYAKLIvNGKNKGvhpFMV--RIRDKethkplqGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLA 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19920834 262 NVAGFS--GPFSCLNNARygIAWGAL------------GAAETCVEIARQYTLDRKQF 305
Cdd:PTZ00460 250 RYIKVSedGQVERQGNPK--VSYASMmymrnliidqypRFAAQALTVAIRYSIYRQQF 305
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
279-399 |
1.57e-05 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 44.26 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 279 GIAWGALGAAETCVEIARQYTLDRKQ--FGRPLAANQLIQKKLADAITEI----ALGLQAC-LHVGRLKDQKLHTPDMIS 351
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIdaarLLLERAAaRIEAAAAAGKPVTPALRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 19920834 352 LLKRNN---TGKSLDIARQMRDMLGANGISDEYHVIRHVINLESVNTYEGT 399
Cdd:pfam08028 81 EARRAAafaTELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAV 131
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
185-413 |
3.35e-05 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 45.80 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 185 YILNGSKTWITSAPIADVIVVWAKCED----GKVRGFLVDRkisgkglETPKIEGKFS---LRASPTGMILMDEVRVPEE 257
Cdd:cd01159 120 YRVSGTWPFASGCDHADWILVGAIVEDddggPLPRAFVVPR-------AEYEIVDTWHvvgLRGTGSNTVVVDDVFVPEH 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 258 QLLPNVAGFSGPFSCLNNARYGIAWG----------ALGAAETCVEIARQYTLDRKQ---FGRPLAANQLIQKKLADAIT 324
Cdd:cd01159 193 RTLTAGDMMAGDGPGGSTPVYRMPLRqvfplsfaavSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920834 325 EIAlglQACLHVGRL--------KDQKLHTPDMISLLKRNNT---GKSLDIARQMRDMLGANGISDEYHVIR-----HVI 388
Cdd:cd01159 273 ELD---AARAFLERAtrdlwahaLAGGPIDVEERARIRRDAAyaaKLSAEAVDRLFHAAGGSALYTASPLQRiwrdiHAA 349
|
250 260
....*....|....*....|....*
gi 19920834 389 NLESVNTYEGThdihALILGRAITG 413
Cdd:cd01159 350 AQHAALNPETA----AEAYGRALLG 370
|
|
| |
