|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
8-377 |
5.25e-74 |
|
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: 234.73 E-value: 5.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 8 TDIQKKWIRKFKKI-ESEFKARAAENDIQSRFPYENIEWLIKEGYTKLTLPVEFGGEGATIEDMVILQSYLGTIDGATAL 86
Cdd:COG1960 6 TEEQRALRDEVREFaEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 87 SIGWHLSVIGQLY-----EQHmwslsmlDSFAKEVVHGALI-NRAVSEAETGSPTrgGRPSTHAVKAENGYVINGVKTFT 160
Cdd:COG1960 86 PVGVHNGAAEALLrfgteEQK-------ERYLPRLASGEWIgAFALTEPGAGSDA--AALRTTAVRDGDGYVLNGQKTFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 161 SMSKALTHYIVGAYVEE---TKSMGFFLIPQSTKGVSIADNWDMVGMRATESHDLILDDVYVPNENFV--ESKR----ES 231
Cdd:COG1960 157 TNAPVADVILVLARTDPaagHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLgeEGKGfkiaMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 232 RPNGWLLHIPSCYLGIAQAARDYAVDFAKNYRPNSitGTIDSLPTVQQNLGKMESLLLSARHFLWSTARGYQSYTEDAQi 311
Cdd:COG1960 237 TLNAGRLGLAAQALGIAEAALELAVAYAREREQFG--RPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAAL- 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487750527 312 wnETSASKVVVMNQGIEIVDLAMRIVGAKSLEMSRPLQRYYRDIRAGLHNPPMEDMAYTNIAKSIT 377
Cdd:COG1960 314 --EAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
119-357 |
6.69e-55 |
|
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: 183.64 E-value: 6.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 119 GALINRAVSEAETGSptRGGRPSTHAVKAENGYVINGVKTFTSMSKALTHYIVGAYVEE----TKSMGFFLIPQSTKGVS 194
Cdd:cd00567 68 EAIAAFALTEPGAGS--DLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEegpgHRGISAFLVPADTPGVT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 195 IADNWDMVGMRATESHDLILDDVYVPNENFVE------SKRESRPNGWLLHIPSCYLGIAQAARDYAVDFAKNYRPnsIT 268
Cdd:cd00567 146 VGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGeegggfELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQ--FG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 269 GTIDSLPTVQQNLGKMESLLLSARHFLWSTARGYQSYTEDAQIWneTSASKVVVMNQGIEIVDLAMRIVGAKSLEMSRPL 348
Cdd:cd00567 224 KPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLE--AAMAKLFATEAAREVADLAMQIHGGRGYSREYPV 301
|
....*....
gi 487750527 349 QRYYRDIRA 357
Cdd:cd00567 302 ERYLRDARA 310
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
125-215 |
1.62e-15 |
|
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: 71.54 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 125 AVSEAETGSPTRGgrPSTHAVKAENG-YVINGVKTFTSMSKALTHYIVGAYVEETK---SMGFFLIPQSTKGVSIADNWD 200
Cdd:pfam02770 3 ALTEPGAGSDVAS--LKTTAADGDGGgWVLNGTKWWITNAGIADLFLVLARTGGDDrhgGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 487750527 201 MVGMRATESHDLILD 215
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
16-301 |
1.42e-12 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 68.36 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 16 RKFKKIESEFKAR-----AAENDIQSRFPYENIEW-LIKE-GYTKLTLPVEFGGEGATIEDMVILQSYLGTIDGATALSI 88
Cdd:PLN02519 31 LQFKESVQQFAQEniaphAAAIDATNSFPKDVNLWkLMGDfNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 89 GWHLSV-IGQLY-----EQHMWSLSMLDSfaKEVVhGALinrAVSEAETGSPTRGGRpsTHAVKAENGYVINGVKTFTSM 162
Cdd:PLN02519 111 GAHSNLcINQLVrngtpAQKEKYLPKLIS--GEHV-GAL---AMSEPNSGSDVVSMK--CKAERVDGGYVLNGNKMWCTN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 163 SKALTHYIVGAYVEET---KSMGFFLIPQSTKGVSIADNWDMVGMRATESHDLILDDVYVPNENFVESKRE------SRP 233
Cdd:PLN02519 183 GPVAQTLVVYAKTDVAagsKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKgvyvmmSGL 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487750527 234 NGWLLHIPSCYLGIAQAARDYAVDFAKNY----RPnsitgtIDSLPTVQQNLGKMESLLLSARHFLWSTARG 301
Cdd:PLN02519 263 DLERLVLAAGPLGLMQACLDVVLPYVRQReqfgRP------IGEFQFIQGKLADMYTSLQSSRSYVYSVARD 328
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
8-377 |
5.25e-74 |
|
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: 234.73 E-value: 5.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 8 TDIQKKWIRKFKKI-ESEFKARAAENDIQSRFPYENIEWLIKEGYTKLTLPVEFGGEGATIEDMVILQSYLGTIDGATAL 86
Cdd:COG1960 6 TEEQRALRDEVREFaEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 87 SIGWHLSVIGQLY-----EQHmwslsmlDSFAKEVVHGALI-NRAVSEAETGSPTrgGRPSTHAVKAENGYVINGVKTFT 160
Cdd:COG1960 86 PVGVHNGAAEALLrfgteEQK-------ERYLPRLASGEWIgAFALTEPGAGSDA--AALRTTAVRDGDGYVLNGQKTFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 161 SMSKALTHYIVGAYVEE---TKSMGFFLIPQSTKGVSIADNWDMVGMRATESHDLILDDVYVPNENFV--ESKR----ES 231
Cdd:COG1960 157 TNAPVADVILVLARTDPaagHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLgeEGKGfkiaMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 232 RPNGWLLHIPSCYLGIAQAARDYAVDFAKNYRPNSitGTIDSLPTVQQNLGKMESLLLSARHFLWSTARGYQSYTEDAQi 311
Cdd:COG1960 237 TLNAGRLGLAAQALGIAEAALELAVAYAREREQFG--RPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAAL- 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487750527 312 wnETSASKVVVMNQGIEIVDLAMRIVGAKSLEMSRPLQRYYRDIRAGLHNPPMEDMAYTNIAKSIT 377
Cdd:COG1960 314 --EAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
119-357 |
6.69e-55 |
|
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: 183.64 E-value: 6.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 119 GALINRAVSEAETGSptRGGRPSTHAVKAENGYVINGVKTFTSMSKALTHYIVGAYVEE----TKSMGFFLIPQSTKGVS 194
Cdd:cd00567 68 EAIAAFALTEPGAGS--DLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEegpgHRGISAFLVPADTPGVT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 195 IADNWDMVGMRATESHDLILDDVYVPNENFVE------SKRESRPNGWLLHIPSCYLGIAQAARDYAVDFAKNYRPnsIT 268
Cdd:cd00567 146 VGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGeegggfELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQ--FG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 269 GTIDSLPTVQQNLGKMESLLLSARHFLWSTARGYQSYTEDAQIWneTSASKVVVMNQGIEIVDLAMRIVGAKSLEMSRPL 348
Cdd:cd00567 224 KPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLE--AAMAKLFATEAAREVADLAMQIHGGRGYSREYPV 301
|
....*....
gi 487750527 349 QRYYRDIRA 357
Cdd:cd00567 302 ERYLRDARA 310
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
16-362 |
2.00e-42 |
|
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: 152.09 E-value: 2.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 16 RKFKKIESEFKARAAENDIQSRFPYENIEWLIKEGYTKLTLPVEFGGEGATIEDMVILQSYLGTIDGATALSIGWHLSVI 95
Cdd:cd01163 1 ARARPLAARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 96 GQLYEqhmWSLSML-DSFAKEVVHGALINRAVSEAETGSPtrgGRPSTHAVKAENGYVINGVKTFTSMSkALTHYIVGAY 174
Cdd:cd01163 81 EALLL---AGPEQFrKRWFGRVLNGWIFGNAVSERGSVRP---GTFLTATVRDGGGYVLNGKKFYSTGA-LFSDWVTVSA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 175 VEETKSMGFFLIPQSTKGVSIADNWDMVGMRATESHDLILDDVYVPNENFVES-KRESRPN-GWL---LHIPSCYLGIAQ 249
Cdd:cd01163 154 LDEEGKLVFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRpNAPDRGTlLTAiyqLVLAAVLAGIAR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 250 AARDYAVDFAKNY-RP--NSITGTIDSLPTVQQNLGKMESLLLSARHFLWSTARGY-QSYTEDAQIWNE--------TSA 317
Cdd:cd01163 234 AALDDAVAYVRSRtRPwiHSGAESARDDPYVQQVVGDLAARLHAAEALVLQAARALdAAAAAGTALTAEargeaalaVAA 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 487750527 318 SKVVVMNQGIEIVDLAMRIVGAKSLEMSRPLQRYYRDIRA-GLHNP 362
Cdd:cd01163 314 AKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNARThTLHNP 359
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
24-376 |
4.99e-37 |
|
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: 137.48 E-value: 4.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 24 EFKARAAENDIQSRFPYENIEWLIKEGYTKLTLPVEFGGEGATIEDMVILQSYLGTIDGatalSIGWHLSVIGQlyeqHM 103
Cdd:cd01159 9 LIRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACG----SAAWVASIVAT----HS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 104 WSLSMLDSFAKEVVHGALINRAVSeaetGSPTRGGRpsthAVKAENGYVINGVKTFTSMSKALTHYIVGAYVEET---KS 180
Cdd:cd01159 81 RMLAAFPPEAQEEVWGDGPDTLLA----GSYAPGGR----AERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDdggPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 181 MGFFLIPQStkGVSIADNWDMVGMRATESHDLILDDVYVPNENFVESKRESRPNG-----------WLLHIPSCY----L 245
Cdd:cd01159 153 PRAFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMMAGDGpggstpvyrmpLRQVFPLSFaavsL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 246 GIAQAARDYAVDFAKN-YRPNSITGTIDSLPTVQQNLGKMESLLLSARHFL-------WSTARGYQSYTEDAQIWNETSA 317
Cdd:cd01159 231 GAAEGALAEFLELAGKrVRQYGAAVKMAEAPITQLRLAEAAAELDAARAFLeratrdlWAHALAGGPIDVEERARIRRDA 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 318 SKVVvmNQGIEIVDLAMRIVGAKSLEMSRPLQRYYRDIRA-GLHNPPMEDMAYTNIAKSI 376
Cdd:cd01159 311 AYAA--KLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHAaAQHAALNPETAAEAYGRAL 368
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
7-356 |
2.69e-30 |
|
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: 119.29 E-value: 2.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 7 HTDIqKKWIRKFkkIESEFKARAAENDIQSRFPYENIEWLIKEGYTKLTLPVEFGGEGATIEDMVILQSYLGTIDGATAL 86
Cdd:cd01158 3 HQMI-RKTVRDF--AEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 87 SIGWHLSVIGQL-------YEQHMWslsmLDSFAKEVVHGALinrAVSEAETGSPTrgGRPSTHAVKAENGYVINGVKTF 159
Cdd:cd01158 80 IVSVHNSLGANPiikfgteEQKKKY----LPPLATGEKIGAF---ALSEPGAGSDA--AALKTTAKKDGDDYVLNGSKMW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 160 TSMSKALTHYIVGAYVEET---KSMGFFLIPQSTKGVSIADNWDMVGMRATESHDLILDDVYVPNENFV----------- 225
Cdd:cd01158 151 ITNGGEADFYIVFAVTDPSkgyRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILgeegegfkiam 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 226 ESKRESRPNgwllhIPSCYLGIAQAARDYAVDFAKNYRpnSITGTIDSLPTVQQNLGKMESLLLSARHFLWSTARGYQ-- 303
Cdd:cd01158 231 QTLDGGRIG-----IAAQALGIAQAALDAAVDYAKERK--QFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDng 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 487750527 304 -SYTEDAqiwnetSASKVVVMNQGIEIVDLAMRIVGAKSLEMSRPLQRYYRDIR 356
Cdd:cd01158 304 ePFIKEA------AMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAK 351
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
16-356 |
3.01e-26 |
|
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: 108.30 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 16 RKFKKIESEFKAR-----AAENDIQSRFPYENIEWLIKEGYTKLTLPVEFGGEGATIEDMVILQSYLGTIDGATA--LSI 88
Cdd:cd01162 6 RAIQEVARAFAAKemaphAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAayISI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 89 gwhlsvigqlyeqHMWSLSMLDSFAKEVVHGALINRAVSE--------AETGSPTRGGRPSTHAVKAENGYVINGVKTFT 160
Cdd:cd01162 86 -------------HNMCAWMIDSFGNDEQRERFLPDLCTMeklasyclTEPGSGSDAAALRTRAVREGDHYVLNGSKAFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 161 SMSKALTHYIVGAYVEETKSMGF--FLIPQSTKGVSIADNWDMVGMRATESHDLILDDVYVPNENFVESKRE------SR 232
Cdd:cd01162 153 SGAGDSDVYVVMARTGGEGPKGIscFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQgfgiamAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 233 PNGWLLHIPSCYLGIAQAARDYAVDFAKnYRpNSITGTIDSLPTVQQNLGKMESLLLSARHFLWSTARGYQSYTEDAQIW 312
Cdd:cd01162 233 LNGGRLNIASCSLGAAQAALDLARAYLE-ER-KQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKL 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 487750527 313 neTSASKVVVMNQGIEIVDLAMRIVGAKSLEMSRPLQRYYRDIR 356
Cdd:cd01162 311 --CAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLR 352
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
15-304 |
8.96e-21 |
|
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: 92.47 E-value: 8.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 15 IRKFkkIESEFKARAAENDIQSRFPYENIEWLIKEGYTKLTLPVEFGGEGATIEDMVILQSYLGTIDGATALSIGWHLSV 94
Cdd:cd01156 13 VREF--AQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHSNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 95 -IGQLY-----EQHMWSLSMLDSfaKEVVhGALinrAVSEAETGSPTRGgrPSTHAVKAENGYVINGVKTF-TSMSKALT 167
Cdd:cd01156 91 cINQIYrngsaAQKEKYLPKLIS--GEHI-GAL---AMSEPNAGSDVVS--MKLRAEKKGDRYVLNGSKMWiTNGPDADT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 168 hYIVGAYVE---ETKSMGFFLIPQSTKGVSIADNWDMVGMRATESHDLILDDVYVPNENFVESKRE------SRPNGWLL 238
Cdd:cd01156 163 -LVVYAKTDpsaGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKgvyvlmSGLDYERL 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487750527 239 HIPSCYLGIAQAARDYAVDFAKNYRpnSITGTIDSLPTVQQNLGKMESLLLSARHFLWSTARGYQS 304
Cdd:cd01156 242 VLAGGPIGIMQAALDVAIPYAHQRK--QFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDR 305
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
9-356 |
2.17e-16 |
|
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: 79.85 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 9 DIQKKWIRKFkkIESEFKARAAENDIQSRFPYENIEWLIKEGYTKLTLPVEFGGEGATIEDMVILQSYLGTIdGATALSI 88
Cdd:cd01160 4 DAFRDVVRRF--FAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARA-GGSGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 89 GWHlSVIGQLYEQHMWSLSMLDSFAKEVVHGALINR-AVSEAETGSPTRGGRpsTHAVKAENGYVINGVKTFTSMSKALT 167
Cdd:cd01160 81 SLH-TDIVSPYITRAGSPEQKERVLPQMVAGKKIGAiAMTEPGAGSDLQGIR--TTARKDGDHYVLNGSKTFITNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 168 HYIVGAYV--EETKSMG--FFLIPQSTKGVSIADNWDMVGMRATESHDLILDDVYVPNENFVesKRESRPNGWLL-HIPS 242
Cdd:cd01160 158 VVIVVARTggEARGAGGisLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLL--GEENKGFYYLMqNLPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 243 CYLGIAQ---AARDYAVDFAKNY--RPNSITGTIDSLPTVQQNLGKMESLLLSARHFLWSTArgyqsyTEDAQiwNETSA 317
Cdd:cd01160 236 ERLLIAAgalAAAEFMLEETRNYvkQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCA------WRHEQ--GRLDV 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 487750527 318 SKVVVM-NQGIE----IVDLAMRIVGAKSLEMSRPLQRYYRDIR 356
Cdd:cd01160 308 AEASMAkYWATElqnrVAYECVQLHGGWGYMREYPIARAYRDAR 351
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
125-215 |
1.62e-15 |
|
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: 71.54 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 125 AVSEAETGSPTRGgrPSTHAVKAENG-YVINGVKTFTSMSKALTHYIVGAYVEETK---SMGFFLIPQSTKGVSIADNWD 200
Cdd:pfam02770 3 ALTEPGAGSDVAS--LKTTAADGDGGgWVLNGTKWWITNAGIADLFLVLARTGGDDrhgGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 487750527 201 MVGMRATESHDLILD 215
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
16-301 |
1.42e-12 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 68.36 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 16 RKFKKIESEFKAR-----AAENDIQSRFPYENIEW-LIKE-GYTKLTLPVEFGGEGATIEDMVILQSYLGTIDGATALSI 88
Cdd:PLN02519 31 LQFKESVQQFAQEniaphAAAIDATNSFPKDVNLWkLMGDfNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 89 GWHLSV-IGQLY-----EQHMWSLSMLDSfaKEVVhGALinrAVSEAETGSPTRGGRpsTHAVKAENGYVINGVKTFTSM 162
Cdd:PLN02519 111 GAHSNLcINQLVrngtpAQKEKYLPKLIS--GEHV-GAL---AMSEPNSGSDVVSMK--CKAERVDGGYVLNGNKMWCTN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 163 SKALTHYIVGAYVEET---KSMGFFLIPQSTKGVSIADNWDMVGMRATESHDLILDDVYVPNENFVESKRE------SRP 233
Cdd:PLN02519 183 GPVAQTLVVYAKTDVAagsKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKgvyvmmSGL 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487750527 234 NGWLLHIPSCYLGIAQAARDYAVDFAKNY----RPnsitgtIDSLPTVQQNLGKMESLLLSARHFLWSTARG 301
Cdd:PLN02519 263 DLERLVLAAGPLGLMQACLDVVLPYVRQReqfgRP------IGEFQFIQGKLADMYTSLQSSRSYVYSVARD 328
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
245-358 |
1.15e-11 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 61.59 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 245 LGIAQAARDYAVDFAKNYRPNSITGTIDSLPTVQQNLGKMESLLLSARHFL-------WSTARGYQSYTEDAQiwNETSA 317
Cdd:pfam08028 7 LGAARAALAEFTERARGRVRAYFGVPLAEDPATQLALAEAAARIDAARLLLeraaariEAAAAAGKPVTPALR--AEARR 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 487750527 318 SKVVVMNQGIEIVDLAMRIVGAKSLEMSRPLQRYYRDIRAG 358
Cdd:pfam08028 85 AAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAA 125
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
22-357 |
1.63e-11 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 65.13 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 22 ESEFKaraaENDIQSRFPYENIEWLIKEGYTKLTLPVEFGGegaTIEDMVILQSYLGTI--DGATALSIGWHLSVIGQLY 99
Cdd:PRK12341 26 EEYFR----TCDENGTYPREFMRALADNGISMLGVPEEFGG---TPADYVTQMLVLEEVskCGAPAFLITNGQCIHSMRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 100 ----EQHmwSLSMLDSFAKEVVHGALinrAVSEAETGSPTrgGRPSTHAVKaENGYV-INGVKTFTSMSKALTHYIVGAY 174
Cdd:PRK12341 99 fgsaEQL--RKTAESTLETGDPAYAL---ALTEPGAGSDN--NSATTTYTR-KNGKVyLNGQKTFITGAKEYPYMLVLAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 175 VEE----TKSMGFFLIPQSTKGVSIADnWDMVGMRATESHDLILDDVYVPNENFVESKREsrpnGWL----------LHI 240
Cdd:PRK12341 171 DPQpkdpKKAFTLWWVDSSKPGIKINP-LHKIGWHMLSTCEVYLDNVEVEESDLVGEEGM----GFLnvmynfemerLIN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 241 PSCYLGIAQAARDYAVDFAkNYRPnSITGTIDSLPTVQQNLGKMESLLLSARHFLWSTArgyqsYTEDAQIWNETSAS-- 318
Cdd:PRK12341 246 AARSLGFAECAFEDAARYA-NQRI-QFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVA-----WQADNGQSLRTSAAla 318
|
330 340 350
....*....|....*....|....*....|....*....
gi 487750527 319 KVVVMNQGIEIVDLAMRIVGAKSLEMSRPLQRYYRDIRA 357
Cdd:PRK12341 319 KLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRC 357
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
15-225 |
1.05e-09 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 59.57 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 15 IRKFKKIESEFKARaaENDIQSRFPYENIEWLIKEGYTKLTLPVEFGGEGATIEDMVILQSYLGTIDGATALSIGWH-LS 93
Cdd:PTZ00461 48 VAKFSREVVDKHAR--EDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHsML 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 94 VIGQLYeqHMWSLSMLDSFAKEVVHGALINrAVSEAETGSPTRGGRPSTHAVKAENG-YVINGVKTFTSMSKALTHYIVG 172
Cdd:PTZ00461 126 FVNNFY--YSASPAQRARWLPKVLTGEHVG-AMGMSEPGAGTDVLGMRTTAKKDSNGnYVLNGSKIWITNGTVADVFLIY 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487750527 173 AYVEetKSMGFFLIPQSTKGVSIADNWDMVGMRATESHDLILDDVYVPNENFV 225
Cdd:PTZ00461 203 AKVD--GKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLL 253
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
245-357 |
8.41e-09 |
|
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: 53.80 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 245 LGIAQAARDYAVDFAKnyRPNSITGTIDSLPTVQQNLGKMESLLLSARHFLWSTARGYQsytEDAQIWNETSASKVVVMN 324
Cdd:pfam00441 23 LGLARRALDEALAYAR--RRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALD---AGGPDGAEASMAKLYASE 97
|
90 100 110
....*....|....*....|....*....|...
gi 487750527 325 QGIEIVDLAMRIVGAKSLEMSRPLQRYYRDIRA 357
Cdd:pfam00441 98 AAVEVADLAMQLHGGYGYLREYPVERLYRDARV 130
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
8-356 |
4.23e-08 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 54.45 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 8 TDIQKKWIRKFKKI-ESE-FKARAAENDIQSRFPYENIEWLIKEGYTKLTLPVEFGGEGATIEDMVILQSYLGTIDGAT- 84
Cdd:PRK03354 6 NDEQELFVAGIRELmASEnWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 85 ---ALSIGWHlSVIGQLYEQHMWSLSMLDSFAKEvvhgaLINRAVSEAETGSPTrGGRPSTHavKAENGYV-INGVKTFT 160
Cdd:PRK03354 86 vlyQLPGGFN-TFLREGTQEQIDKIMAFRGTGKQ-----MWNSAITEPGAGSDV-GSLKTTY--TRRNGKVyLNGSKCFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 161 SMSKALTHYIVGAYVEETKSMGFF---LIPQSTKGVSIaDNWDMVGMRATESHDLILDDVYVPNEN--------FVESKR 229
Cdd:PRK03354 157 TSSAYTPYIVVMARDGASPDKPVYtewFVDMSKPGIKV-TKLEKLGLRMDSCCEITFDDVELDEKDmfgregngFNRVKE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 230 ESRPNGWLlhIPSCYLGIAQAARDYAVDFAkNYRpnsITG--TIDSLPTVQQNLGKMESLLLSARHFLWSTARGYQSYTE 307
Cdd:PRK03354 236 EFDHERFL--VALTNYGTAMCAFEDAARYA-NQR---VQFgeAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTI 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 487750527 308 DAqiwNETSASKVVVMNQGIEIVDLAMRIVGAKSLEMSRPLQRYYRDIR 356
Cdd:PRK03354 310 TS---GDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLR 355
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
16-259 |
7.18e-07 |
|
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: 50.66 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 16 RKFKKieSEFKARAAENDIQSRFPYENIEWLIKEGYTKLTLPVEFGGEGATIEDMVILQSYL-----GTIDGATALSIGW 90
Cdd:cd01157 13 RKFAR--EEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELaygctGVQTAIEANSLGQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 91 HLSVIGQLYEQHMwslSMLDSFAKEVVHGALinrAVSEAETGSPTRGGRpsTHAVKAENGYVINGVKTFTSMSKALTHYI 170
Cdd:cd01157 91 MPVIISGNDEQKK---KYLGRMTEEPLMCAY---CVTEPGAGSDVAGIK--TKAEKKGDEYIINGQKMWITNGGKANWYF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 171 VGAYVE------ETKSMGFFLIPQSTKGVSIADNWDMVGMRATESHDLILDDVYVPNENFV-----------ESKRESRP 233
Cdd:cd01157 163 LLARSDpdpkcpASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLigegagfkiamGAFDKTRP 242
|
250 260
....*....|....*....|....*.
gi 487750527 234 NgwllhIPSCYLGIAQAARDYAVDFA 259
Cdd:cd01157 243 P-----VAAGAVGLAQRALDEATKYA 263
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
50-342 |
7.85e-07 |
|
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: 50.42 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 50 GYTKLTLPVEFGGEGATIEDMVILQ---SYLGTIDGATALSIGWHLSVIGQL--YEQHMWSLSMLDSFAKEVVHGalinr 124
Cdd:cd01152 48 GWAAPGWPKEYGGRGASLMEQLIFReemAAAGAPVPFNQIGIDLAGPTILAYgtDEQKRRFLPPILSGEEIWCQG----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 125 aVSEAETGSPTRGGRpsTHAVKAENGYVINGVKTFTSmSKALTHYIVGAY-----VEETKSMGFFLIPQSTKGVSIADNW 199
Cdd:cd01152 123 -FSEPGAGSDLAGLR--TRAVRDGDDWVVNGQKIWTS-GAHYADWAWLLVrtdpeAPKHRGISILLVDMDSPGVTVRPIR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 200 DMVGmrATESHDLILDDVYVPNENFVeskreSRPN-GWllHIPSCYLGI------AQAARDY--AVDFAKNYRPNSITGT 270
Cdd:cd01152 199 SING--GEFFNEVFLDDVRVPDANRV-----GEVNdGW--KVAMTTLNFervsigGSAATFFelLLARLLLLTRDGRPLI 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487750527 271 IDslPTVQQNLGKMESLLLSARHFLWSTArgyQSYTEDAQIWNETSASKVVVMNQGIEIVDLAMRIVGAKSL 342
Cdd:cd01152 270 DD--PLVRQRLARLEAEAEALRLLVFRLA---SALAAGKPPGAEASIAKLFGSELAQELAELALELLGTAAL 336
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
12-96 |
2.11e-06 |
|
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: 45.92 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 12 KKWIRKFkkIESEFKARAAENDIQSRFPYENIEWLIKEGYTKLTLPVEFGGEGATIEDMVILQSYLGTIDGATALSIGWH 91
Cdd:pfam02771 8 RDTVREF--AEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVALALSVH 85
|
....*
gi 487750527 92 LSVIG 96
Cdd:pfam02771 86 SSLGA 90
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
125-223 |
1.83e-05 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 46.38 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750527 125 AVSEAETGSPTRGGRpsTHAVKAENGYVINGVKTFTSMSKALTHYIVGAYVEETKSMGFFLIPQSTKGVSIADNWDMVGM 204
Cdd:PLN02526 147 ALTEPDYGSDASSLN--TTATKVEGGWILNGQKRWIGNSTFADVLVIFARNTTTNQINGFIVKKGAPGLKATKIENKIGL 224
|
90
....*....|....*....
gi 487750527 205 RATESHDLILDDVYVPNEN 223
Cdd:PLN02526 225 RMVQNGDIVLKDVFVPDED 243
|
|
| |
