|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
1-518 |
0e+00 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 915.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 1 MRRVFSSAPRRYVRHASYAAGLFNSRVVPEELFPYPSRQLDSDESETVQVLIEQIRSSDKDL-NLAGARIATEYGGLGLG 79
Cdd:PTZ00457 1 MRRRFSSAPRQYVRHASYAAGLFNFKIVPEEMFPYPCRKLDGDEAENLQSLLEQIRSNDKILgNLYGARIATEYGGLGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 80 HTAHALVCEEVGTNGDSKLLQTIQHCGFASYLLSTVGSKEVKGKYLTGMSDGKVMMGWATREGCGNDISMNTAKATLTSD 159
Cdd:PTZ00457 81 HTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWATEEGCGSDISMNTTKASLTDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 160 GRYVLTGCKRCEFAEGATHYLVLAKALTQTATEAGPMEVSRNTFFVLEKSAKGVSVNGGTVSFEDTPAADVVGVVGEGFK 239
Cdd:PTZ00457 161 GSYVLTGQKRCEFAASATHFLVLAKTLTQTAAEEGATEVSRNSFFICAKDAKGVSVNGDSVVFENTPAADVVGVVGEGFK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 240 DRMITLFTEQYVYAATLLGISKRVVQELRDSVPEQWATDTVASCACIMYAMESSLYALTANLDLPTEDSLLEAALVSVFV 319
Cdd:PTZ00457 241 DAMITLFTEQYLYAASLLGIMKRVVQELRGSNAEEGATDTVASFACAMYAMESTLYALTANLDLPTEDSLLECTLVSAFV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 320 QSSTNEWLSILSTATPMSEVLEKCFANARLLLSMMESTDFLYSSAVCCGVEDYGLVFQRTSTLQMVQLRTMRSMGMKDRV 399
Cdd:PTZ00457 321 QSTTNQLLSILETATPPSTTLEKCFANARLFLSMMESRDFLYSSAVCCGVEDYGLFFQRASTLQMMQARTLRSLGVRDRV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 400 PVREL-DCSAIDSAVVAFGNAVEATFVRNGSQVPQQQLIINRLGEAASLLYAASASASRAAMCQSKRLPTAKTERELAST 478
Cdd:PTZ00457 401 PIKNLpDCSLIDEAVVAFGNAVEATFVRSGSQVPYQQLLLNRLGEAASLLYAASAVASRASMCVSKGLPSAKVEGELASA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 157864482 479 FIAMATNRVIQLSEESYNIGMTADDSYKRIAVEMCDEVLR 518
Cdd:PTZ00457 481 FIAMAVSRARQLSEESCNVGKTADDSYKRIALEMCDDALQ 520
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
26-319 |
5.07e-30 |
|
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: 121.10 E-value: 5.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 26 RVVPEELFPYpSRQLDSDEsETVQVLIEQIrssdKDLNLAGARIATEYGGLGLGHTAHALVCEEVGTnGDSKLLQTIQHC 105
Cdd:COG1960 18 EFAEEEIAPE-AREWDREG-EFPRELWRKL----AELGLLGLTIPEEYGGLGLSLVELALVLEELAR-ADASLALPVGVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 106 GFASYLLSTVGSKEVKGKYLTGMSDGKVMMGWATRE-GCGNDISMNTAKATLTSDGrYVLTGCKR-CEFAEGATHYLVLA 183
Cdd:COG1960 91 NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEpGAGSDAAALRTTAVRDGDG-YVLNGQKTfITNAPVADVILVLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 184 KaltqTATEAGPMEVSrntFFVLEKSAKGVSVNG------------GTVSFEDT--PAADVVGVVGEGFKDRMITLFTEQ 249
Cdd:COG1960 170 R----TDPAAGHRGIS---LFLVPKDTPGVTVGRiedkmglrgsdtGELFFDDVrvPAENLLGEEGKGFKIAMSTLNAGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 250 YVYAATLLGISKRVVQELRDSVPE-----------QWATDTVASCACIMYAMESSLYALTANLDLpTEDSLLEAALVSVF 318
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREreqfgrpiadfQAVQHRLADMAAELEAARALVYRAAWLLDA-GEDAALEAAMAKLF 321
|
.
gi 157864482 319 V 319
Cdd:COG1960 322 A 322
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
17-327 |
8.41e-30 |
|
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: 121.04 E-value: 8.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 17 SYAAGLFNSRVVPEELFPYPsRQLDSDESETVQVLIEQI----------RSSD-------------KDLNLAGARIATEY 73
Cdd:cd01161 1 SFALNMFLGDIVTKQVFPYP-SVLTEEQTEELNMLVGPVekffeevndpAKNDqlekiprktltqlKELGLFGLQVPEEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 74 GGLGLGHTAHALVCEEVGTNGD-SKLLQTIQHCGFASYLLstVGSKEVKGKYLTGMSDGKVMMGWA-TREGCGNDISMNT 151
Cdd:cd01161 80 GGLGLNNTQYARLAEIVGMDLGfSVTLGAHQSIGFKGILL--FGTEAQKEKYLPKLASGEWIAAFAlTEPSSGSDAASIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 152 AKATLTSDGR-YVLTGCKRCEFAEG-ATHYLVLAKalTQTATEAGPMEvSRNTFFVLEKSAKGVSV------------NG 217
Cdd:cd01161 158 TTAVLSEDGKhYVLNGSKIWITNGGiADIFTVFAK--TEVKDATGSVK-DKITAFIVERSFGGVTNgppekkmgikgsNT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 218 GTVSFEDT--PAADVVGVVGEGFKDRMITLFTEQYVYAATLLGISKRVVQELRDsvpeqWATDTV--------------- 280
Cdd:cd01161 235 AEVYFEDVkiPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVD-----YANNRKqfgkkihefgliqek 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 157864482 281 -ASCACIMYAMESSLYALTANLDLP-TEDSLLEAALVSVFvqSSTNEWL 327
Cdd:cd01161 310 lANMAILQYATESMAYMTSGNMDRGlKAEYQIEAAISKVF--ASEAAWL 356
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
60-132 |
3.13e-10 |
|
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: 57.47 E-value: 3.13e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157864482 60 KDLNLAGARIATEYGGLGLGHTAHALVCEEVGTnGDSKLLQTIQ-HCGFASYLLSTVGSKEVKGKYLTGMSDGK 132
Cdd:pfam02771 41 GELGLLGITIPEEYGGAGLDYLAYALVAEELAR-ADASVALALSvHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
1-518 |
0e+00 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 915.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 1 MRRVFSSAPRRYVRHASYAAGLFNSRVVPEELFPYPSRQLDSDESETVQVLIEQIRSSDKDL-NLAGARIATEYGGLGLG 79
Cdd:PTZ00457 1 MRRRFSSAPRQYVRHASYAAGLFNFKIVPEEMFPYPCRKLDGDEAENLQSLLEQIRSNDKILgNLYGARIATEYGGLGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 80 HTAHALVCEEVGTNGDSKLLQTIQHCGFASYLLSTVGSKEVKGKYLTGMSDGKVMMGWATREGCGNDISMNTAKATLTSD 159
Cdd:PTZ00457 81 HTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWATEEGCGSDISMNTTKASLTDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 160 GRYVLTGCKRCEFAEGATHYLVLAKALTQTATEAGPMEVSRNTFFVLEKSAKGVSVNGGTVSFEDTPAADVVGVVGEGFK 239
Cdd:PTZ00457 161 GSYVLTGQKRCEFAASATHFLVLAKTLTQTAAEEGATEVSRNSFFICAKDAKGVSVNGDSVVFENTPAADVVGVVGEGFK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 240 DRMITLFTEQYVYAATLLGISKRVVQELRDSVPEQWATDTVASCACIMYAMESSLYALTANLDLPTEDSLLEAALVSVFV 319
Cdd:PTZ00457 241 DAMITLFTEQYLYAASLLGIMKRVVQELRGSNAEEGATDTVASFACAMYAMESTLYALTANLDLPTEDSLLECTLVSAFV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 320 QSSTNEWLSILSTATPMSEVLEKCFANARLLLSMMESTDFLYSSAVCCGVEDYGLVFQRTSTLQMVQLRTMRSMGMKDRV 399
Cdd:PTZ00457 321 QSTTNQLLSILETATPPSTTLEKCFANARLFLSMMESRDFLYSSAVCCGVEDYGLFFQRASTLQMMQARTLRSLGVRDRV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 400 PVREL-DCSAIDSAVVAFGNAVEATFVRNGSQVPQQQLIINRLGEAASLLYAASASASRAAMCQSKRLPTAKTERELAST 478
Cdd:PTZ00457 401 PIKNLpDCSLIDEAVVAFGNAVEATFVRSGSQVPYQQLLLNRLGEAASLLYAASAVASRASMCVSKGLPSAKVEGELASA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 157864482 479 FIAMATNRVIQLSEESYNIGMTADDSYKRIAVEMCDEVLR 518
Cdd:PTZ00457 481 FIAMAVSRARQLSEESCNVGKTADDSYKRIALEMCDDALQ 520
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
26-319 |
5.07e-30 |
|
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: 121.10 E-value: 5.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 26 RVVPEELFPYpSRQLDSDEsETVQVLIEQIrssdKDLNLAGARIATEYGGLGLGHTAHALVCEEVGTnGDSKLLQTIQHC 105
Cdd:COG1960 18 EFAEEEIAPE-AREWDREG-EFPRELWRKL----AELGLLGLTIPEEYGGLGLSLVELALVLEELAR-ADASLALPVGVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 106 GFASYLLSTVGSKEVKGKYLTGMSDGKVMMGWATRE-GCGNDISMNTAKATLTSDGrYVLTGCKR-CEFAEGATHYLVLA 183
Cdd:COG1960 91 NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEpGAGSDAAALRTTAVRDGDG-YVLNGQKTfITNAPVADVILVLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 184 KaltqTATEAGPMEVSrntFFVLEKSAKGVSVNG------------GTVSFEDT--PAADVVGVVGEGFKDRMITLFTEQ 249
Cdd:COG1960 170 R----TDPAAGHRGIS---LFLVPKDTPGVTVGRiedkmglrgsdtGELFFDDVrvPAENLLGEEGKGFKIAMSTLNAGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 250 YVYAATLLGISKRVVQELRDSVPE-----------QWATDTVASCACIMYAMESSLYALTANLDLpTEDSLLEAALVSVF 318
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREreqfgrpiadfQAVQHRLADMAAELEAARALVYRAAWLLDA-GEDAALEAAMAKLF 321
|
.
gi 157864482 319 V 319
Cdd:COG1960 322 A 322
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
17-327 |
8.41e-30 |
|
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: 121.04 E-value: 8.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 17 SYAAGLFNSRVVPEELFPYPsRQLDSDESETVQVLIEQI----------RSSD-------------KDLNLAGARIATEY 73
Cdd:cd01161 1 SFALNMFLGDIVTKQVFPYP-SVLTEEQTEELNMLVGPVekffeevndpAKNDqlekiprktltqlKELGLFGLQVPEEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 74 GGLGLGHTAHALVCEEVGTNGD-SKLLQTIQHCGFASYLLstVGSKEVKGKYLTGMSDGKVMMGWA-TREGCGNDISMNT 151
Cdd:cd01161 80 GGLGLNNTQYARLAEIVGMDLGfSVTLGAHQSIGFKGILL--FGTEAQKEKYLPKLASGEWIAAFAlTEPSSGSDAASIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 152 AKATLTSDGR-YVLTGCKRCEFAEG-ATHYLVLAKalTQTATEAGPMEvSRNTFFVLEKSAKGVSV------------NG 217
Cdd:cd01161 158 TTAVLSEDGKhYVLNGSKIWITNGGiADIFTVFAK--TEVKDATGSVK-DKITAFIVERSFGGVTNgppekkmgikgsNT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 218 GTVSFEDT--PAADVVGVVGEGFKDRMITLFTEQYVYAATLLGISKRVVQELRDsvpeqWATDTV--------------- 280
Cdd:cd01161 235 AEVYFEDVkiPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVD-----YANNRKqfgkkihefgliqek 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 157864482 281 -ASCACIMYAMESSLYALTANLDLP-TEDSLLEAALVSVFvqSSTNEWL 327
Cdd:cd01161 310 lANMAILQYATESMAYMTSGNMDRGlKAEYQIEAAISKVF--ASEAAWL 356
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
107-319 |
3.75e-21 |
|
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: 94.27 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 107 FASYLLSTVGSKEVKGKYLTGMSDGKVMMGWA-TREGCGNDISMNTAKATLtSDGRYVLTGCKR-CEFAEGATHYLVLAK 184
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFAlTEPGAGSDLAGIRTTARK-DGDGYVLNGRKIfISNGGDADLFIVLAR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 185 altqtaTEAGPMEVSRNTFFVLEKSAKGVSVNG------------GTVSFED--TPAADVVGVVGEGFKDRMITLFTEQY 250
Cdd:cd00567 122 ------TDEEGPGHRGISAFLVPADTPGVTVGRiwdkmgmrgsgtGELVFDDvrVPEDNLLGEEGGGFELAMKGLNVGRL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 251 VYAATLLGISKRVVQELRDSVPE-----------QWATDTVASCACIMYAMESSLYALTANLDLPTEDSLLEAALVSVFV 319
Cdd:cd00567 196 LLAAVALGAARAALDEAVEYAKQrkqfgkplaefQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFA 275
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
61-266 |
3.10e-15 |
|
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: 77.45 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 61 DLNLAGARIATEYGGLGLGHTAHALVCEEVGTNGDSKLLQTIQHCGFASYLLSTVGSKEVKGKYLTGMSDGKVMMGWATR 140
Cdd:cd01156 44 KLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 141 E-GCGND-ISMNTaKATlTSDGRYVLTGCKR-CEFAEGATHYLVLAKaltqtateAGPMEVSRN-TFFVLEKSAKGVSV- 215
Cdd:cd01156 124 EpNAGSDvVSMKL-RAE-KKGDRYVLNGSKMwITNGPDADTLVVYAK--------TDPSAGAHGiTAFIVEKGMPGFSRa 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157864482 216 -----------NGGTVSFED--TPAADVVGVVGEGFKDRMITLFTEQYVYAATLLGISKRVVQE 266
Cdd:cd01156 194 qkldklgmrgsNTCELVFEDceVPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDV 257
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
30-259 |
1.29e-13 |
|
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: 72.30 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 30 EELFPYpSRQLDsDESETVQVLIEQIrssdKDLNLAGARIATEYGGLGLGHTAHALVCEEVGTNGDSKLLQTIQHCGFAS 109
Cdd:cd01158 16 KEIAPL-AAEMD-EKGEFPREVIKEM----AELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSLGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 110 YLLSTVGSKEVKGKYLTGMSDGKVMMGWATRE-GCGNDI-SMNTaKATLTSDgRYVLTGCKrCEFAEG--ATHYLVLAKa 185
Cdd:cd01158 90 NPIIKFGTEEQKKKYLPPLATGEKIGAFALSEpGAGSDAaALKT-TAKKDGD-DYVLNGSK-MWITNGgeADFYIVFAV- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 186 ltqTATEAGPMEVsrnTFFVLEKSAKGVSVNG------------GTVSFED--TPAADVVGVVGEGFKDRMITLFTEQYV 251
Cdd:cd01158 166 ---TDPSKGYRGI---TAFIVERDTPGLSVGKkedklgirgsstTELIFEDvrVPKENILGEEGEGFKIAMQTLDGGRIG 239
|
....*...
gi 157864482 252 YAATLLGI 259
Cdd:cd01158 240 IAAQALGI 247
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
61-259 |
1.24e-10 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 63.36 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 61 DLNLAGARIATEYGGLGLGHTAHALVCEEVGTNGDSKLLQTIQHCGFASYLLSTVGSKEVKGKYLTGMSDGKVMMGWATR 140
Cdd:PLN02519 70 DFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 141 E-GCGNDISMNTAKATlTSDGRYVLTGCKR-CEFAEGATHYLVLAKaltqTATEAGPMEVsrnTFFVLEKSAKGVSV--- 215
Cdd:PLN02519 150 EpNSGSDVVSMKCKAE-RVDGGYVLNGNKMwCTNGPVAQTLVVYAK----TDVAAGSKGI---TAFIIEKGMPGFSTaqk 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157864482 216 ---------NGGTVSFED--TPAADVVGVVGEGFKDRMITLFTEQYVYAATLLGI 259
Cdd:PLN02519 222 ldklgmrgsDTCELVFENcfVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGL 276
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
60-132 |
3.13e-10 |
|
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: 57.47 E-value: 3.13e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157864482 60 KDLNLAGARIATEYGGLGLGHTAHALVCEEVGTnGDSKLLQTIQ-HCGFASYLLSTVGSKEVKGKYLTGMSDGK 132
Cdd:pfam02771 41 GELGLLGITIPEEYGGAGLDYLAYALVAEELAR-ADASVALALSvHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
61-266 |
1.46e-09 |
|
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: 59.91 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 61 DLNLAGARIATEYGGLGLGHTAHALVCEEVGTnGDSKLLQTIQHCGFASYLLSTVGSKEVKGKYLTGMSDGKVMMGWATR 140
Cdd:cd01157 43 ELGLMNTHIPEDCGGLGLGTFDTCLITEELAY-GCTGVQTAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 141 E-GCGNDISMNTAKATLTSDgRYVLTGCKRCEFAEG-ATHYLVLAKALTQTATEAGpmevSRNTFFVLEKSAKGVS---- 214
Cdd:cd01157 122 EpGAGSDVAGIKTKAEKKGD-EYIINGQKMWITNGGkANWYFLLARSDPDPKCPAS----KAFTGFIVEADTPGIQpgrk 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157864482 215 -VNGGT-------VSFEDT--PAADVVGVVGEGFKDRMITLFTEQYVYAATLLGISKRVVQE 266
Cdd:cd01157 197 eLNMGQrcsdtrgITFEDVrvPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDE 258
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
61-265 |
2.13e-05 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 46.85 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 61 DLNLAGARIATEYGGLGLGHTAHALVCEEVGTNGDSKLLQTIQHCG-FAS--YLLSTVGSKEV-KGKYLTGMSDGKVMMg 136
Cdd:PTZ00461 79 DLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSMlFVNnfYYSASPAQRARwLPKVLTGEHVGAMGM- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 137 waTREGCGNDISMNTAKATLTSDGRYVLTGCKrCEFAEG--ATHYLVLAKAltqtateagpmeVSRNTFFVLEKSAKGVS 214
Cdd:PTZ00461 158 --SEPGAGTDVLGMRTTAKKDSNGNYVLNGSK-IWITNGtvADVFLIYAKV------------DGKITAFVVERGTKGFT 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157864482 215 VN------GGTVS------FEDT--PAADVVGVVGEGFKDRMITLFTEQYVYAATLLGISKRVVQ 265
Cdd:PTZ00461 223 QGpkidkcGMRAShmcqlfFEDVvvPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVE 287
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
70-279 |
3.53e-05 |
|
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: 46.19 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 70 ATEYGGLGLGHTAHALVCEEVGTNG--DSKLLQTIQHCGfasYLLSTVGSKEVKGKYLTGMSDGKVMmgWA---TREGCG 144
Cdd:cd01152 55 PKEYGGRGASLMEQLIFREEMAAAGapVPFNQIGIDLAG---PTILAYGTDEQKRRFLPPILSGEEI--WCqgfSEPGAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 145 NDISMNTAKATLTSDGrYVLTGCKR-CEFAEGATHYLVLAKALTQTATEAGPmevsrnTFFVLEKSAKGVSV------NG 217
Cdd:cd01152 130 SDLAGLRTRAVRDGDD-WVVNGQKIwTSGAHYADWAWLLVRTDPEAPKHRGI------SILLVDMDSPGVTVrpirsiNG 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157864482 218 GT----VSFED--TPAADVVGVVGEGFKDRMITLFTEQyvyaATLLGISKRVVQELRDSVPEQWATDT 279
Cdd:cd01152 203 GEffneVFLDDvrVPDANRVGEVNDGWKVAMTTLNFER----VSIGGSAATFFELLLARLLLLTRDGR 266
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
69-258 |
6.90e-05 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 45.10 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 69 IATEYGGLGLGHTAHALVCEEVGTNGDSKLLQTiqhCGFASYLLSTVGSKEVKGK-YLTGMSDGKVMMGWA-TREGCGND 146
Cdd:PRK12341 56 VPEEFGGTPADYVTQMLVLEEVSKCGAPAFLIT---NGQCIHSMRRFGSAEQLRKtAESTLETGDPAYALAlTEPGAGSD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 147 ISMNTAKATlTSDGRYVLTGCKrcEFAEGATHY---LVLAKALTQTATEagpmevSRNTFFVLEKSAKGVSVN-----GG 218
Cdd:PRK12341 133 NNSATTTYT-RKNGKVYLNGQK--TFITGAKEYpymLVLARDPQPKDPK------KAFTLWWVDSSKPGIKINplhkiGW 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 157864482 219 T------VSFEDTPA--ADVVGVVGEGFKDRMITLFTEQYVYAATLLG 258
Cdd:PRK12341 204 HmlstceVYLDNVEVeeSDLVGEEGMGFLNVMYNFEMERLINAARSLG 251
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
137-215 |
4.65e-04 |
|
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: 39.57 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 137 WATREGCGNDISMNTAKATLTSDGRYVLTGCKRC-EFAEGATHYLVLAKaltqTATEAGPMEVSrntFFVLEKSAKGVSV 215
Cdd:pfam02770 3 ALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWiTNAGIADLFLVLAR----TGGDDRHGGIS---LFLVPKDAPGVSV 75
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
72-248 |
1.35e-03 |
|
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: 41.22 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 72 EYGGLGLGHTAHALVCEEVGTNGDSklLQTIQHCGFASYLLSTVGSKEVKGKYLTGMSDGKVMMGWA-TREGCGNDISMN 150
Cdd:cd01153 58 EYGGQGLPITVYSALAEIFSRGDAP--LMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMClTEPDAGSDLGAL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 151 TAKATLTSDGRYVLTGCKR-----CEFAEGATHYLVLAKaltqtaTEAGPMEVSRNTFFVLEKSAKGVSVNGGTVS---- 221
Cdd:cd01153 136 RTKAVYQADGSWRINGVKRfisagEHDMSENIVHLVLAR------SEGAPPGVKGLSLFLVPKFLDDGERNGVTVAriee 209
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 157864482 222 -------------FEDTPAAdVVGVVGEGFKdRMITLFTE 248
Cdd:cd01153 210 kmglhgsptcelvFDNAKGE-LIGEEGMGLA-QMFAMMNG 247
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
66-259 |
2.09e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 40.62 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 66 GARIATEYGGLGLGHTAHALVCEEVGTNGDSKLLQTIQHCGFASYLLsTVGSKEVKGKYLTGMSDGKvmmgWA-----TR 140
Cdd:PTZ00456 115 GISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLM-AWGSEEQKEQYLTKLVSGE----WSgtmclTE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 141 EGCGNDISMNTAKATLTSDGRYVLTGCKRceFAEGATH-------YLVLAKALTQTAT---------------EAGPMEV 198
Cdd:PTZ00456 190 PQCGTDLGQVKTKAEPSADGSYKITGTKI--FISAGDHdltenivHIVLARLPNSLPTtkglslflvprhvvkPDGSLET 267
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157864482 199 SRNTFFV-LEKSA--KGVSVngGTVSFEDTpAADVVGVVGEGFKdRMITlFTEQYVYAATLLGI 259
Cdd:PTZ00456 268 AKNVKCIgLEKKMgiKGSST--CQLSFENS-VGYLIGEPNAGMK-QMFT-FMNTARVGTALEGV 326
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
60-271 |
2.33e-03 |
|
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: 40.38 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 60 KDLNLAGARIATEYGGLGLG-HTAHALVcEEVGTnGDSKLLQTIQ-HCGFASYLLsTVGSKEVKGKYLTGMSDGKVMMGW 137
Cdd:cd01163 32 RQSGLGTLRVPKEYGGLGASlPDLYEVV-RELAA-ADSNIAQALRaHFGFVEALL-LAGPEQFRKRWFGRVLNGWIFGNA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864482 138 ATREGCGNDISMNTakATLTSDGRYVLTGCKRceFAEGAthylvlakALTQTATEAGPMEVSRNTFFVLEKSAKGVSVN- 216
Cdd:cd01163 109 VSERGSVRPGTFLT--ATVRDGGGYVLNGKKF--YSTGA--------LFSDWVTVSALDEEGKLVFAAVPTDRPGITVVd 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157864482 217 -----------GGTVSFEDTP--AADVVGVVGEGFKDRMITLFTeQYVYAATLLGISKRVVQELRDSV 271
Cdd:cd01163 177 dwdgfgqrltaSGTVTFDNVRvePDEVLPRPNAPDRGTLLTAIY-QLVLAAVLAGIARAALDDAVAYV 243
|
|
| |
