|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
5-380 |
1.47e-160 |
|
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: 455.45 E-value: 1.47e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 5 PETLDALVTTVRRFVRERLVPAESRVEETNRIPDDIIEEMRAMGLFGLSIPEEYGGLGLTMEEEVRVGFELGYTSPAFRS 84
Cdd:COG1960 6 TEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 85 VIGTNNGiGSQGIIADGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGDSYIINGTKRFITNAPVAGV 164
Cdd:COG1960 86 PVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 165 FTLMARMGGS-GPSGISAFLAERDLPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSIIGGvEGRGFKTAMKVLNRGRL 243
Cdd:COG1960 165 ILVLARTDPAaGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGE-EGKGFKIAMSTLNAGRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 244 HISSVCAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDEsNVDIIRKAASCKLFC 323
Cdd:COG1960 244 GLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDA-GEDAALEAAMAKLFA 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490824828 324 SEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIAREMIRE 380
Cdd:COG1960 323 TEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
6-379 |
6.17e-137 |
|
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: 395.10 E-value: 6.17e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 6 ETLDALVTTVRRFVRERLVPAESRVEETNRIPDDIIEEMRAMGLFGLSIPEEYGGLGLTMEEEVRVGFELGYTSPAFRSV 85
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 86 IGTNNGIGSQGIIADGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGDSYIINGTKRFITNAPVAGVF 165
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 166 TLMARMGGS-GPSGISAFLAERDLPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSIIgGVEGRGFKTAMKVLNRGRLH 244
Cdd:cd01158 161 IVFAVTDPSkGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENIL-GEEGEGFKIAMQTLDGGRIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 245 ISSVCAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDESnVDIIRKAASCKLFCS 324
Cdd:cd01158 240 IAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNG-EPFIKEAAMAKLFAS 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 490824828 325 EMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIAREMIR 379
Cdd:cd01158 319 EVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
6-375 |
3.93e-120 |
|
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: 350.82 E-value: 3.93e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 6 ETLDALVTTVRRFVRERLVPAESRVEETNRIPDdiiEEMRAMGLFGlsipeeygglgltmeeevrvgfelgytspafrsv 85
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPW---ELLAELGLLL---------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 86 igtnngiGSQGIIADGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGDSYIINGTKRFITNAPVAGVF 165
Cdd:cd00567 44 -------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 166 TLMARMGGSGPS--GISAFLAERDLPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSIIGGvEGRGFKTAMKVLNRGRL 243
Cdd:cd00567 117 IVLARTDEEGPGhrGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGE-EGGGFELAMKGLNVGRL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 244 HISSVCAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDESNVDIIRKAASCKLFC 323
Cdd:cd00567 196 LLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFA 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 490824828 324 SEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIAR 375
Cdd:cd00567 276 TEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
6-374 |
1.51e-118 |
|
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: 349.84 E-value: 1.51e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 6 ETLDALVTTVRRFVRERLVPAesRVEETNRIPDDIIEEMRAMGLFGLSIPEEYGGLGLTMEEEVRVGFELGYTSpAFRSV 85
Cdd:cd01161 29 EELNMLVGPVEKFFEEVNDPA--KNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDL-GFSVT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 86 IGTNNGIGSQGIIADGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAER--DGDSYIINGTKRFITNAPVAG 163
Cdd:cd01161 106 LGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWITNGGIAD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 164 VFTLMARM-----GGSGPSGISAFLAERDLPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSIIGGVeGRGFKTAMKVL 238
Cdd:cd01161 186 IFTVFAKTevkdaTGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEV-GDGFKVAMNIL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 239 NRGRLHISSVCAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDE-SNVDIIRKAA 317
Cdd:cd01161 265 NNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRgLKAEYQIEAA 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490824828 318 SCKLFCSEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIA 374
Cdd:cd01161 345 ISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIA 401
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
10-380 |
9.88e-105 |
|
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: 313.23 E-value: 9.88e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 10 ALVTTVRRFVRERLVPAESRVEETNRIPDDIIEEMRAMGLFGLSIPEEYGGLGLTMEEEVRVGFELGYTSPAFRSVIGTN 89
Cdd:cd01162 7 AIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAYISIH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 90 NGIGSQgIIADGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGDSYIINGTKRFITNAPVAGVFTLMA 169
Cdd:cd01162 87 NMCAWM-IDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVYVVMA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 170 RMGGSGPSGISAFLAERDLPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSIIGGvEGRGFKTAMKVLNRGRLHISSVC 249
Cdd:cd01162 166 RTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGG-EGQGFGIAMAGLNGGRLNIASCS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 250 AGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDESNVDIIRKAASCKLFCSEMVGR 329
Cdd:cd01162 245 LGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFD 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 490824828 330 VADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIAREMIRE 380
Cdd:cd01162 325 VANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
6-379 |
8.06e-98 |
|
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: 295.86 E-value: 8.06e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 6 ETLDALVTTVRRFVRERLVPAESRVEETNRIPDDIIEEMRAMGLFGLSIPEEYGGLGLTMEEEVRVGFELGYTSPAFRSV 85
Cdd:cd01156 4 DEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 86 IGTNNGIGSQGIIADGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGDSYIINGTKRFITNAPVAGVF 165
Cdd:cd01156 84 YGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDADTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 166 TLMARMGGS-GPSGISAFLAERDLPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSIIGGvEGRGFKTAMKVLNRGRLH 244
Cdd:cd01156 164 VVYAKTDPSaGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGG-ENKGVYVLMSGLDYERLV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 245 ISSVCAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDESNVDiiRK-AASCKLFC 323
Cdd:cd01156 243 LAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMD--PKdAAGVILYA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490824828 324 SEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIAREMIR 379
Cdd:cd01156 321 AEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
9-378 |
2.03e-94 |
|
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: 286.70 E-value: 2.03e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 9 DALVTTVRRFVRERLVPAESRVEETNRIPDDIIEEMRAMGLFGLSIPEEYGGLGLTMEEEVRVGFELGYtSPAFRSVIGT 88
Cdd:cd01160 4 DAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELAR-AGGSGPGLSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 89 NNGIGSQGIIADGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGDSYIINGTKRFITNAPVAGVFTLM 168
Cdd:cd01160 83 HTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 169 ARMGG--SGPSGISAFLAERDLPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSIIGGvEGRGFKTAMKVLNRGRLHIS 246
Cdd:cd01160 163 ARTGGeaRGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGE-ENKGFYYLMQNLPQERLLIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 247 SVCAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDESNVDIIrKAASCKLFCSEM 326
Cdd:cd01160 242 AGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVA-EASMAKYWATEL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 490824828 327 VGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIAREMI 378
Cdd:cd01160 321 QNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
6-378 |
1.13e-88 |
|
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: 272.54 E-value: 1.13e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 6 ETLDALVTTVRRFVRERLVPAESRVEETNRIPDDIIEEMRAMGLFGLSIPEEYGGLGLTMEEEVRVGFELGYTSPAFRSV 85
Cdd:cd01157 3 EQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 86 IgTNNGIGSQGIIADGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGDSYIINGTKRFITNAPVAGVF 165
Cdd:cd01157 83 I-EANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 166 TLMARMGGS--GPSG--ISAFLAERDLPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSIIGGvEGRGFKTAMKVLNRG 241
Cdd:cd01157 162 FLLARSDPDpkCPASkaFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIG-EGAGFKIAMGAFDKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 242 RLHISSVCAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDeSNVDIIRKAASCKL 321
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVD-SGRRNTYYASIAKA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490824828 322 FCSEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIAREMI 378
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
4-376 |
1.06e-77 |
|
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: 244.58 E-value: 1.06e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 4 DPETLDALVT--------TVRRFVRERLVPaesRVEETNR---IPDDIIEEMRAMGLFGlSIPEEYGGLGLTMEEEVRVG 72
Cdd:cd01151 5 DPLNLDDLLTeeerairdTAREFCQEELAP---RVLEAYReekFDRKIIEEMGELGLLG-ATIKGYGCAGLSSVAYGLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 73 FELGYTSPAFRSVIGTNNGIGSQGIIADGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGDSYIINGT 152
Cdd:cd01151 81 REVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 153 KRFITNAPVAGVFTLMARMGGSGpsGISAFLAERDLPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSIIGGVegRGFK 232
Cdd:cd01151 161 KTWITNSPIADVFVVWARNDETG--KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA--EGLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 233 TAMKVLNRGRLHISSVCAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDESnvdi 312
Cdd:cd01151 237 GPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQG---- 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490824828 313 irKAAS-----CKLFCSEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIARE 376
Cdd:cd01151 313 --KATPeqislLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRA 379
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
6-380 |
5.49e-73 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 232.84 E-value: 5.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 6 ETLDALVTTVRRFVRERLVPAESRVEETNRIPDDI--IEEMRAMGLFGLSIPEEYGGLGLTMEEEVRVGFELGYTSPAFR 83
Cdd:PLN02519 28 DTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 84 SVIGTNNGIGSQGIIADGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGDSYIINGTKRFITNAPVAG 163
Cdd:PLN02519 108 LSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 164 VFTLMARMG-GSGPSGISAFLAERDLPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSIIGGvEGRGFKTAMKVLNRGR 242
Cdd:PLN02519 188 TLVVYAKTDvAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQ-EGKGVYVMMSGLDLER 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 243 LHISSVCAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDESNVDiiRK-AASCKL 321
Cdd:PLN02519 267 LVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVD--RKdCAGVIL 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 490824828 322 FCSEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIAREMIRE 380
Cdd:PLN02519 345 CAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
29-369 |
8.69e-68 |
|
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: 219.57 E-value: 8.69e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 29 RVEETNRIPDDIIEEMRAM---GLFGLSIPEEYGGLGLTMEEEVrVGFELGYtspafRSVIGTNNGIGSQG----IIADG 101
Cdd:cd01153 27 FDDGRVVVPPPFKEALDAFaeaGWMALGVPEEYGGQGLPITVYS-ALAEIFS-----RGDAPLMYASGTQGaaatLLAHG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 102 TDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGD-SYIINGTKRFITNAPVAG----VFTLMARMGGSGP 176
Cdd:cd01153 101 TEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGEHDMseniVHLVLARSEGAPP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 177 S--GISAFL-------AERDlpGLTVGTPDHKMGQRGTQTCDVYLENvrvpATSIIGGVEGRGFKTAMKVLNRGRLHISS 247
Cdd:cd01153 181 GvkGLSLFLvpkflddGERN--GVTVARIEEKMGLHGSPTCELVFDN----AKGELIGEEGMGLAQMFAMMNGARLGVGT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 248 VCAGTAERPIEESVGFAGSRVQFGK--------RIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDESNV----DIIRK 315
Cdd:cd01153 255 QGTGLAEAAYLNALAYAKERKQGGDlikaapavTIIHHPDVRRSLMTQKAYAEGSRALDLYTATVQDLAERkateGEDRK 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490824828 316 AAS---------CKLFCSEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQ 369
Cdd:cd01153 335 ALSaladlltpvVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQ 397
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
10-380 |
6.42e-65 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 212.10 E-value: 6.42e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 10 ALVTTVRRFVRERLVPAESRVEETNRIPDDIIEEMRAMGLFGLSIPEEYGGLGLTMEEEVRVGFELGYTSPAF------R 83
Cdd:PTZ00461 43 ALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFclaylaH 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 84 SVIGTNNGIGSqgiiadGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGD-SYIINGTKRFITNAPVA 162
Cdd:PTZ00461 123 SMLFVNNFYYS------ASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 163 GVFTLMARMGGSgpsgISAFLAERDLPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSIIGGvEGRGFKTAMKVLNRGR 242
Cdd:PTZ00461 197 DVFLIYAKVDGK----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGE-EGKGMVGMMRNLELER 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 243 LHISSVCAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDESNVDIIRKAAScKLF 322
Cdd:PTZ00461 272 VTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAA-KLF 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 490824828 323 CSEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIAREMIRE 380
Cdd:PTZ00461 351 ATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKG 408
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
10-375 |
1.08e-60 |
|
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: 200.69 E-value: 1.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 10 ALVTTVRRFVRERLVPAESRVEE-------TNRIPDDIIEEMRAM----GLFGLSIPEEYGGLGLTMEEEVRVGFELGyt 78
Cdd:cd01155 5 ELRARVKAFMEEHVYPAEQEFLEyyaeggdRWWTPPPIIEKLKAKakaeGLWNLFLPEVSGLSGLTNLEYAYLAEETG-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 79 spafRSVIG---TNNGIGSQG----IIADGTDDQKKYWLPRLASGGIIASFALTEPDVGS-DAGAVRTTAERDGDSYIIN 150
Cdd:cd01155 83 ----RSFFApevFNCQAPDTGnmevLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASsDATNIECSIERDGDDYVIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 151 GTKRFITNA--PVAGVFTLMARMGGSGPSGI---SAFLAERDLPGLTV-------GTPDHKMGQrgtqtCDVYLENVRVP 218
Cdd:cd01155 159 GRKWWSSGAgdPRCKIAIVMGRTDPDGAPRHrqqSMILVPMDTPGVTIirplsvfGYDDAPHGH-----AEITFDNVRVP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 219 ATSIIGGvEGRGFKTAMKVLNRGRLHISSVCAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMV 298
Cdd:cd01155 234 ASNLILG-EGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLV 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490824828 299 LDAARAFDESNVDIIRKA-ASCKLFCSEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIAR 375
Cdd:cd01155 313 LKAAHMIDTVGNKAARKEiAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
17-380 |
6.29e-57 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 190.32 E-value: 6.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 17 RFVRERLVPAE--SRVEETNRIPDDIIEEMRAMGLFGLSIPEEYGG-------LGLTMEEEVRVGfelgytSPAFrsVIG 87
Cdd:PRK12341 17 RELITRNFPEEyfRTCDENGTYPREFMRALADNGISMLGVPEEFGGtpadyvtQMLVLEEVSKCG------APAF--LIT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 88 tnNGIGSQGIIADGTDDQ-KKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGDSYIINGTKRFITNAPVAGVFT 166
Cdd:PRK12341 89 --NGQCIHSMRRFGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYML 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 167 LMARMGGSG--PSGISAFLAERDLPGLTVgTPDHKMGQRGTQTCDVYLENVRVPATSIIGgVEGRGFKTAMKVLNRGRLH 244
Cdd:PRK12341 167 VLARDPQPKdpKKAFTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVG-EEGMGFLNVMYNFEMERLI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 245 ISSVCAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDeSNVDIIRKAASCKLFCS 324
Cdd:PRK12341 245 NAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQAD-NGQSLRTSAALAKLYCA 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490824828 325 EMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIAREMIRE 380
Cdd:PRK12341 324 RTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKD 379
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
31-380 |
1.13e-53 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 181.95 E-value: 1.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 31 EETNRIPDDIIEEMRAMGLFGLSIPEEYGGLGLTMEEEVRVGFELG-YTSPAFrsVIGTNNGiGSQGIIADGTDDQKKYW 109
Cdd:PRK03354 33 DRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGrLGAPTY--VLYQLPG-GFNTFLREGTQEQIDKI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 110 LPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGDSYIINGTKRFITNAPVAGVFTLMARMGGSGPSGI-SAFLAERDL 188
Cdd:PRK03354 110 MAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVyTEWFVDMSK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 189 PGLTVgTPDHKMGQRGTQTCDVYLENVRVPATSIIgGVEGRGFKTAMKVLNRGRLHISSVCAGTAERPIEESVGFAGSRV 268
Cdd:PRK03354 190 PGIKV-TKLEKLGLRMDSCCEITFDDVELDEKDMF-GREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 269 QFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDESNVDiIRKAASCKLFCSEMVGRVADNAVQIHGGSGYMQNYP 348
Cdd:PRK03354 268 QFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT-SGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHR 346
|
330 340 350
....*....|....*....|....*....|..
gi 490824828 349 VEHFYRDVRLFRLYEGTSQIQRIIIAREMIRE 380
Cdd:PRK03354 347 ISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
10-377 |
2.54e-52 |
|
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: 178.31 E-value: 2.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 10 ALVTTVRRFVRErLVPAESRVE---ETNRIPDDIIEEMRAM---GLFGLSIPEEYGGLGLTMEEEVRVGFELGYtspAFR 83
Cdd:cd01152 5 AFRAEVRAWLAA-HLPPELREEsalGYREGREDRRRWQRALaaaGWAAPGWPKEYGGRGASLMEQLIFREEMAA---AGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 84 SVIGTNNGIGSQG--IIADGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGDSYIINGTKRFITNAPV 161
Cdd:cd01152 81 PVPFNQIGIDLAGptILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 162 AGVFTLMARMGGSGP--SGISAFLAERDLPGLTVGTPDHKMGqrGTQTCDVYLENVRVPATSIIGGVeGRGFKTAMKVLN 239
Cdd:cd01152 161 ADWAWLLVRTDPEAPkhRGISILLVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEV-NDGWKVAMTTLN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 240 RGRLHIssvcAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDESNvDIIRKAASC 319
Cdd:cd01152 238 FERVSI----GGSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGK-PPGAEASIA 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490824828 320 KLFCSEMVGRVADNAVQIHGGSGYMQNYP--------VEHFYRDVRLFRLYEGTSQIQRIIIAREM 377
Cdd:cd01152 313 KLFGSELAQELAELALELLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIAERL 378
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
228-377 |
3.65e-49 |
|
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: 162.81 E-value: 3.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 228 GRGFKTAMKVLNRGRLHISSVCAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDE 307
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 308 SNVDIIRkAASCKLFCSEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIAREM 377
Cdd:pfam00441 81 GGPDGAE-ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
103-379 |
8.48e-42 |
|
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: 151.37 E-value: 8.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 103 DDQKKYWLPRLAS-----GGIIASFaLTEPDVGSDAGAVRTTAERD-GDSYIINGTKRFiTNAPVAGVFTLMARMGGS-- 174
Cdd:cd01154 128 PEELKQYLPGLLSdryktGLLGGTW-MTEKQGGSDLGANETTAERSgGGVYRLNGHKWF-ASAPLADAALVLARPEGApa 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 175 GPSGISAFLAERDLP-----GLTVGTPDHKMGQRGTQTCDVYLENvrvpATSIIGGVEGRGFKTAMKVLNRGRLHISSVC 249
Cdd:cd01154 206 GARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDD----AEAYLIGDEGKGIYYILEMLNISRLDNAVAA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 250 AGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDESNVDIIRKAASCKLF------- 322
Cdd:cd01154 282 LGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAHMARLAtpvakli 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 490824828 323 CSEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIAREMIR 379
Cdd:cd01154 362 ACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVLVK 418
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
101-375 |
5.82e-39 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 148.02 E-value: 5.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 101 GTDDQKKYWLPRLASGGIIASFALTEPDVGS-DAGAVRTTAERDGDSYIINGTKRFITNA--PVAGVFTLMARMGGSGP- 176
Cdd:PLN02876 533 GNKEQQLEWLIPLLEGKIRSGFAMTEPQVASsDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTDFNAPk 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 177 -SGISAFLAERDLPGLTVGTP-------DHKMGQrgtqtCDVYLENVRVPATSIIGGvEGRGFKTAMKVLNRGRLHISSV 248
Cdd:PLN02876 613 hKQQSMILVDIQTPGVQIKRPllvfgfdDAPHGH-----AEISFENVRVPAKNILLG-EGRGFEIAQGRLGPGRLHHCMR 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 249 CAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDESNVDIIRKA-ASCKLFCSEMV 327
Cdd:PLN02876 687 LIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRLGNKKARGIiAMAKVAAPNMA 766
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 490824828 328 GRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIAR 375
Cdd:PLN02876 767 LKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAK 814
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
5-116 |
2.06e-37 |
|
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: 131.05 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 5 PETLDALVTTVRRFVRERLVPAESRVEETNRIPDDIIEEMRAMGLFGLSIPEEYGGLGLTMEEEVRVGFELGYTSPAFRS 84
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|..
gi 490824828 85 VIGTNNGIGSQGIIADGTDDQKKYWLPRLASG 116
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASG 112
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
36-365 |
8.54e-36 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 138.80 E-value: 8.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 36 IPDDIIEEMRAMGLFGLSIPEEYGGLGLTMEEEVRVGFELGYTSPAFRSVIGTNNGIGSqgiiAD-----GTDDQKKYWL 110
Cdd:PRK09463 110 LPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLGP----GElllhyGTDEQKDHYL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 111 PRLASGGIIASFALTEPDVGSDAGA-----VRTTAERDGDSYI---INGTKRFITNAPVAGVFTLMARM-------GGSG 175
Cdd:PRK09463 186 PRLARGEEIPCFALTSPEAGSDAGSipdtgVVCKGEWQGEEVLgmrLTWNKRYITLAPIATVLGLAFKLydpdgllGDKE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 176 PSGISAFLAERDLPGLTVGTPDHKMGQRgTQTCDVYLENVRVPATSIIGGVE--GRGFKTAMKVLNRGRlHIS--SVCAG 251
Cdd:PRK09463 266 DLGITCALIPTDTPGVEIGRRHFPLNVP-FQNGPTRGKDVFIPLDYIIGGPKmaGQGWRMLMECLSVGR-GISlpSNSTG 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 252 TAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYagrcmVLDAARAFDESNVDIIRK----AASCKLFCSEMV 327
Cdd:PRK09463 344 GAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAY-----LMDAARTLTTAAVDLGEKpsvlSAIAKYHLTERG 418
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 490824828 328 GRVADNAVQIHGGSGYM---QNYpvehfyrdvrLFRLYEGT 365
Cdd:PRK09463 419 RQVINDAMDIHGGKGIClgpNNF----------LARAYQAA 449
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
10-377 |
2.08e-35 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 134.21 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 10 ALVTTVRRFVRERLVPAESRVEETNRIPDDIIEEMRAMGLFGLSIpEEYGGLGLTMEEEVRVGFELGYTSPAFRSVIGTN 89
Cdd:PLN02526 35 ALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVARVDASCSTFILVH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 90 NGIGSQGIIADGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGDSYIINGTKRFITNAPVAGVFTLMA 169
Cdd:PLN02526 114 SSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 170 RmgGSGPSGISAFLAERDLPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSIIGGVEgrGFKTAMKVLNRGRLHIssvc 249
Cdd:PLN02526 194 R--NTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVN--SFQDTNKVLAVSRVMV---- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 250 agtAERPIEESVG-------FAGSRVQFGKRIAEHQMIQAMLADMSTEAYAgrcMVLDAAR--AFDESNVDIIRKAASCK 320
Cdd:PLN02526 266 ---AWQPIGISMGvydmchrYLKERKQFGAPLAAFQINQEKLVRMLGNIQA---MFLVGWRlcKLYESGKMTPGHASLGK 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490824828 321 LFCSEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQRIIIAREM 377
Cdd:PLN02526 340 AWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
30-356 |
5.39e-33 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 130.46 E-value: 5.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 30 VEETNRIPDDIIEEMRAMGLFGLSIPEEYGGLGLTMEEEVRVGFELgytspAFRSV-----IGTNNGIGSQGIIAD-GTD 103
Cdd:PRK13026 103 VQNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKI-----ATRSVsaavtVMVPNSLGPGELLTHyGTQ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 104 DQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTA-----ERDGDSYI---INGTKRFITNAPVAGVFTLMARM---- 171
Cdd:PRK13026 178 EQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGivcrgEFEGEEVLglrLTWDKRYITLAPVATVLGLAFKLrdpd 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 172 ---GGSGPSGISAFLAERDLPGLTVGTPDHKMGQR---GTqtcdVYLENVRVPATSIIGGVE--GRGFKTAMKVLNRGRl 243
Cdd:PRK13026 258 gllGDKKELGITCALIPTDHPGVEIGRRHNPLGMAfmnGT----TRGKDVFIPLDWIIGGPDyaGRGWRMLVECLSAGR- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 244 HIS--SVCAGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAgrcmvLDAARAFDESNVDIIRK----AA 317
Cdd:PRK13026 333 GISlpALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYL-----LEAARRLTTTGLDLGVKpsvvTA 407
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 490824828 318 SCKLFCSEMVGRVADNAVQIHGGSGYM---QNYpVEHFYRDV 356
Cdd:PRK13026 408 IAKYHMTELARDVVNDAMDIHAGKGIQlgpKNY-LGHAYMAV 448
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
121-213 |
1.43e-30 |
|
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: 112.37 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 121 SFALTEPDVGSDAGAVRTTA-ERDGDSYIINGTKRFITNAPVAGVFTLMARMGG-SGPSGISAFLAERDLPGLTVGTPDH 198
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGdDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 490824828 199 KMGQRGTQTCDVYLE 213
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
42-369 |
2.43e-30 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 122.28 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 42 EEMRAMGLFGLSIPEEYGGLGLTMEeevrVGF---ELGYTS-PAFRSVIGTNNGiGSQGIIADGTDDQKKYWLPRLASGG 117
Cdd:PTZ00456 106 QALKAGGWTGISEPEEYGGQALPLS----VGFitrELMATAnWGFSMYPGLSIG-AANTLMAWGSEEQKEQYLTKLVSGE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 118 IIASFALTEPDVGSDAGAVRTTAERDGD-SYIINGTKRFITnapvAG--------VFTLMARMGGSGPS--GISAFLAER 186
Cdd:PTZ00456 181 WSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFIS----AGdhdlteniVHIVLARLPNSLPTtkGLSLFLVPR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 187 DLP----------GLTVGTPDHKMGQRGTQTCDVYLENvrvpATSIIGGVEGRGFKTAMKVLNRGRL--HISSVCAG--- 251
Cdd:PTZ00456 257 HVVkpdgsletakNVKCIGLEKKMGIKGSSTCQLSFEN----SVGYLIGEPNAGMKQMFTFMNTARVgtALEGVCHAela 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 252 -------TAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFD---ESNVDIIRKAAS--- 318
Cdd:PTZ00456 333 fqnalryARERRSMRALSGTKEPEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDihaAAKDAATREALDhei 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490824828 319 ------CKLFCSEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQIQ 369
Cdd:PTZ00456 413 gfytpiAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQ 469
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
21-357 |
7.32e-20 |
|
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: 90.07 E-value: 7.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 21 ERLVPAESRVEETNRIPDDIIEEMRAMGLFGLSIPEEYGGLGLTMEEEVRVGFELGYTSPAFRSVIGTNNGIgSQGIIAD 100
Cdd:cd01163 8 ARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGF-VEALLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 101 GTDDQKKYWLPRLASGGIIASfALTEPDvGSDAGAVRTTAERDGDSYIINGTKRFITNAPVAGvftlMARMGGSGPSG-I 179
Cdd:cd01163 87 GPEQFRKRWFGRVLNGWIFGN-AVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSD----WVTVSALDEEGkL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 180 SAFLAERDLPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSIIGGVEgrGFKTAMKVLNRGRLHISSVCAGTAERPIEE 259
Cdd:cd01163 161 VFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPN--APDRGTLLTAIYQLVLAAVLAGIARAALDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 260 SVGFAGSRvqfgKRIAEHQ---------MIQAMLADMSTEAYAGRCMVLDAARAFDESNVDIIRKA-----------ASC 319
Cdd:cd01163 239 AVAYVRSR----TRPWIHSgaesarddpYVQQVVGDLAARLHAAEALVLQAARALDAAAAAGTALTaeargeaalavAAA 314
|
330 340 350
....*....|....*....|....*....|....*...
gi 490824828 320 KLFCSEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVR 357
Cdd:cd01163 315 KVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
245-367 |
1.31e-16 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 75.46 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 245 ISSVCAGTAERPIEESVGFAGSRVQ--FGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAF-------DESNVDIIRK 315
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIeaaaaagKPVTPALRAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 490824828 316 AASCKLFCSEMVGRVADNAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQ 367
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
97-345 |
1.42e-15 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 78.14 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 97 IIADGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERD--GDSYIIN-----GTKRFITNAPVAGVF-TLM 168
Cdd:cd01150 113 IKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDplTQEFVINtpdftATKWWPGNLGKTATHaVVF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 169 ARMGGSGPS-GISAFLAE-RD------LPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSII---GGV--EG------- 228
Cdd:cd01150 193 AQLITPGKNhGLHAFIVPiRDpkthqpLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLnrfGDVspDGtyvspfk 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 229 ---RGFKTAMKVLNRGRLHISSVCAGTAERPIEESVGFAGSRVQFGKR-------IAEHQMIQAMLADMSTEAYA----G 294
Cdd:cd01150 273 dpnKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKpsdpevqILDYQLQQYRLFPQLAAAYAfhfaA 352
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 490824828 295 RCMVLDAARAFDESNVDIIRK-------AASCKLFCSEMVGRVADNAVQIHGGSGYMQ 345
Cdd:cd01150 353 KSLVEMYHEIIKELLQGNSELlaelhalSAGLKAVATWTAAQGIQECREACGGHGYLA 410
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
29-368 |
1.84e-15 |
|
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: 77.00 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 29 RVEETNRIPDDIIEEMRAMGLFGLSIPEEYGGLGLTMEEEVRVGFELGYTSPAFRSVIGTNNGIGSQGiIADGTDDQKKY 108
Cdd:cd01159 16 EAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATHSRML-AAFPPEAQEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 109 WlprlASGGiiasfaltePDVGSDAGAVRTTAERDGDSYIINGTKRFIT---NAPVAGVFTLMARMGGSGPSGISAFLAE 185
Cdd:cd01159 95 W----GDGP---------DTLLAGSYAPGGRAERVDGGYRVSGTWPFASgcdHADWILVGAIVEDDDGGPLPRAFVVPRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 186 rdlpGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSII---GGVEG--RGFKTAMKVLNRGRLHISSVCA---GTAERPI 257
Cdd:cd01159 162 ----EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtagDMMAGdgPGGSTPVYRMPLRQVFPLSFAAvslGAAEGAL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 258 EESVGFAGSRVQ---FGKRIAEHQMIQAMLADMSTEayagrcmvLDAARAFDESNV-DIIRKAASCKLF----------- 322
Cdd:cd01159 238 AEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAE--------LDAARAFLERATrDLWAHALAGGPIdveerarirrd 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 490824828 323 CSEMVGRVADNAVQIH---GGSGYMQNYPVEHFYRDVR-----LFRLYEGTSQI 368
Cdd:cd01159 310 AAYAAKLSAEAVDRLFhaaGGSALYTASPLQRIWRDIHaaaqhAALNPETAAEA 363
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
109-368 |
8.97e-10 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 60.15 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 109 WLPRLASG-------------GIIASFALTEPDVGSDAGAVRTTAER-DGDSYIINGTKRFITnAPVAGVFTLMARMGGs 174
Cdd:PRK11561 156 WLTPLLSDrydshllpggqkrGLLIGMGMTEKQGGSDVLSNTTRAERlADGSYRLVGHKWFFS-VPQSDAHLVLAQAKG- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 175 gpsGISAFLAERDLP-----GLTVGTPDHKMGQRGTQTCDVYLENvrvpATSIIGGVEGRGFKTAMKVLNRGRLHISSVC 249
Cdd:PRK11561 234 ---GLSCFFVPRFLPdgqrnAIRLERLKDKLGNRSNASSEVEFQD----AIGWLLGEEGEGIRLILKMGGMTRFDCALGS 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 250 AGTAERPIEESVGFAGSRVQFGKRIAEHQMIQAMLADMSTEAYAGRCMVLDAARAFDESnvDIIRKAASCKLF------- 322
Cdd:PRK11561 307 HGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRR--ADAKEALWARLFtpaakfv 384
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490824828 323 -CSEMVGRVADnAVQIHGGSGYMQNYPVEHFYRDVRLFRLYEGTSQI 368
Cdd:PRK11561 385 iCKRGIPFVAE-AMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNI 430
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
17-259 |
1.39e-07 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 53.35 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 17 RFVRERLVPAESRVEETNRIPD--DIIEEMRAMG-----LFGLSIPEEYGGLGLTMEEEVRVGFELGYTSPA-FRSVIGt 88
Cdd:PTZ00457 26 KIVPEEMFPYPCRKLDGDEAENlqSLLEQIRSNDkilgnLYGARIATEYGGLGLGHTAHALIYEEVGTNCDSkLLSTIQ- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 89 NNGIGSQGIIADGTDDQKKYWLPRLASGGIIASFAlTEPDVGSDAGAVRTTAE-RDGDSYIINGTKRfITNAPVAGVF-- 165
Cdd:PTZ00457 105 HSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISMNTTKASlTDDGSYVLTGQKR-CEFAASATHFlv 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 166 ---TLMARMGGSGP---SGISAFLAERDLPGLTVgtpdhkmgqrgtQTCDVYLENvrVPATSIIgGVEGRGFKTAMKVLN 239
Cdd:PTZ00457 183 lakTLTQTAAEEGAtevSRNSFFICAKDAKGVSV------------NGDSVVFEN--TPAADVV-GVVGEGFKDAMITLF 247
|
250 260
....*....|....*....|
gi 490824828 240 RGRLHISSVCAGTAERPIEE 259
Cdd:PTZ00457 248 TEQYLYAASLLGIMKRVVQE 267
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
97-218 |
9.00e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 50.99 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 97 IIADGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERD--GDSYIIN------------GTKRFITNAPVa 162
Cdd:PLN02443 110 IKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDpkTDEFVIHsptltsskwwpgGLGKVSTHAVV- 188
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490824828 163 gvftlMARMGGSGPS-GISAFLAE-------RDLPGLTVGTPDHKMGQRGTQTCD---VYLENVRVP 218
Cdd:PLN02443 189 -----YARLITNGKDhGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIP 250
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
97-293 |
1.97e-06 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 49.86 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 97 IIADGTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERD--GDSYIIN-----GTKRFITNAPVAGVF-TLM 168
Cdd:PLN02636 152 VINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTDEFVINtpndgAIKWWIGNAAVHGKFaTVF 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 169 ARM-------GGSGPSGISAFLAE-RD------LPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSII---GGVEGRG- 230
Cdd:PLN02636 232 ARLklpthdsKGVSDMGVHAFIVPiRDmkthqvLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLnrfGDVSRDGk 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 231 FKTAMKVLNR-----------GRLHISSVCAGTAERPIEESVGFAGSRVQFGK------RIAEHQMIQAMLADMSTEAYA 293
Cdd:PLN02636 312 YTSSLPTINKrfaatlgelvgGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPpkqpeiSILDYQSQQHKLMPMLASTYA 391
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
46-223 |
3.07e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 42.91 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 46 AMGLFGLSIPEEYGGLGLTMEEEVRVGFELGYTSPAFRSVigtnngigsqgiiadGTDDQKKYWLPRLASGGIIASFALT 125
Cdd:PTZ00460 70 AHKHLNLANPNYYTPNLLCPQGTFISTVHFAMVIPAFQVL---------------GTDEQINLWMPSLLNFEIVGCYAQT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 126 EPDVGSDAGAVRTTAERD--GDSYIIN-----GTK-----------------RFITNAPVAGVFTLMARmggsgpsgISA 181
Cdd:PTZ00460 135 ELGHGSDVQNLETTATYDkqTNEFVIHtpsveAVKfwpgelgflcnfalvyaKLIVNGKNKGVHPFMVR--------IRD 206
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490824828 182 FLAERDLPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSII 223
Cdd:PTZ00460 207 KETHKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLL 248
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
101-226 |
2.67e-03 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 39.76 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490824828 101 GTDDQKKYWLPRLASGGIIASFALTEPDVGSDAGAVRTTAERDGDsyiingTKRFITNAP--------VAG--------- 163
Cdd:PLN02312 168 GTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPK------TEEFVINTPcesaqkywIGGaanhathti 241
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490824828 164 VFTLMARMGGSgpSGISAFLAE-RD-----LPGLTVGTPDHKMGQRGTQTCDVYLENVRVPATSIIGGV 226
Cdd:PLN02312 242 VFSQLHINGKN--EGVHAFIAQiRDqdgniCPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSV 308
|
|
| |
