|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
25-423 |
3.15e-139 |
|
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: 409.61 E-value: 3.15e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 25 DFNEEQLMMRDSVKEFVDKELWAHKDRFEKKDyAYTQECMKKAGDLGFLSVAVPEAYGGMGMGFVNTVLVCDHISGATGS 104
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREG-EFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 105 FSTAFGAHTGiGTMPITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVlsEDGKTYSITGQKMWISNA 184
Cdd:COG1960 83 LALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV--RDGDGYVLNGQKTFITNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 185 GFCSVFIVFARIGDD---KNITGFIVE-NTPdnGISMNEEEHKLGIRASSTRQVFFNDTKVPAENMLSERGNGFKIAMNA 260
Cdd:COG1960 160 PVADVILVLARTDPAaghRGISLFLVPkDTP--GVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMST 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 261 LNVGRIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYRAAKDIEDritereaags 340
Cdd:COG1960 238 LNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDA---------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 341 shqeaelkgVEEYAIECSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEINRMLSVGMLIK 420
Cdd:COG1960 308 ---------GEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
|
...
gi 500641789 421 KAM 423
Cdd:COG1960 379 RPG 381
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
18-423 |
1.27e-134 |
|
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: 398.77 E-value: 1.27e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 18 EAIFTPEDFNEEQLMMRDSVKEFVDKELWAHKDRFEKKDyaytQECMKKAGDLGFLSVAVPEAYGGMGMGFVNTVLVCDh 97
Cdd:cd01161 20 PSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIP----RKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 98 ISGATGSFSTAFGAHTGIGTMPITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVLSEDGKTYSITGQ 177
Cdd:cd01161 95 IVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKHYVLNGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 178 KMWISNAGFCSVFIVFARI------GDDKN-ITGFIVENTpDNGISMNEEEHKLGIRASSTRQVFFNDTKVPAENMLSER 250
Cdd:cd01161 175 KIWITNGGIADIFTVFAKTevkdatGSVKDkITAFIVERS-FGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 251 GNGFKIAMNALNVGRIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYRAAKDIED 330
Cdd:cd01161 254 GDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 331 RITereaagsshqeaelkgvEEYAIECSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEIN 410
Cdd:cd01161 334 GLK-----------------AEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEIL 396
|
410
....*....|...
gi 500641789 411 RMLSVGMLIKKAM 423
Cdd:cd01161 397 RLFIALTGLQHAG 409
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
28-420 |
9.84e-116 |
|
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: 349.26 E-value: 9.84e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 28 EEQLMMRDSVKEFVDKELWAHKDRFEKKDyAYTQECMKKAGDLGFLSVAVPEAYGGMGMGFVNTVLVCDHISGATGSFST 107
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKG-EFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 108 AFGAHTGIGTMPITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVlsEDGKTYSITGQKMWISNAGFC 187
Cdd:cd01158 80 IVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAK--KDGDDYVLNGSKMWITNGGEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 188 SVFIVFARIGDD---KNITGFIVE-NTPdnGISMNEEEHKLGIRASSTRQVFFNDTKVPAENMLSERGNGFKIAMNALNV 263
Cdd:cd01158 158 DFYIVFAVTDPSkgyRGITAFIVErDTP--GLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 264 GRIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYRAAkdiedritEREAAGsshq 343
Cdd:cd01158 236 GRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAA--------RLKDNG---- 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500641789 344 eaelkgvEEYAIECSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEINRMLSVGMLIK 420
Cdd:cd01158 304 -------EPFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
25-413 |
2.98e-101 |
|
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: 312.04 E-value: 2.98e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 25 DFNEEQLMMRDSVKEFVDKELWAHKDRFEKKDYaYTQECMKKAGDLGFLSVAVPEAYGGMGMGFVNTVLVCDHISGATGS 104
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNE-FPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 105 FSTAFGAHTGIGTMPITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAvlSEDGKTYSITGQKMWISNA 184
Cdd:cd01156 80 VALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--EKKGDRYVLNGSKMWITNG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 185 GFCSVFIVFARIGDDK---NITGFIVEnTPDNGISMNEEEHKLGIRASSTRQVFFNDTKVPAENMLSERGNGFKIAMNAL 261
Cdd:cd01156 158 PDADTLVVYAKTDPSAgahGITAFIVE-KGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 262 NVGRIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYRAAKDI-EDRITEREAAGs 340
Cdd:cd01156 237 DYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACdRGNMDPKDAAG- 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500641789 341 shqeaelkgveeyAIECSilkvavSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEINRML 413
Cdd:cd01156 316 -------------VILYA------AEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMV 369
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
28-412 |
1.13e-96 |
|
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: 298.43 E-value: 1.13e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 28 EEQLMMRDSVKEFVDKELWAHkDRFEKKDYAYTQECMKKAGDLGflsvavpeayggmgmgfvntvlvcdhisgatgsfst 107
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPY-ARERRETPEEPWELLAELGLLL------------------------------------ 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 108 afgahtgiGTMPITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVLSEDGktYSITGQKMWISNAGFC 187
Cdd:cd00567 44 --------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG--YVLNGRKIFISNGGDA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 188 SVFIVFARIGDD----KNITGFIVE-NTPdnGISMNEEEHKLGIRASSTRQVFFNDTKVPAENMLSERGNGFKIAMNALN 262
Cdd:cd00567 114 DLFIVLARTDEEgpghRGISAFLVPaDTP--GVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLN 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 263 VGRIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYRAAKDIEDritereaagssh 342
Cdd:cd00567 192 VGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ------------ 259
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 343 qeaelkGVEEYAIECSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEINRM 412
Cdd:cd00567 260 ------GPDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRL 323
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
27-413 |
9.37e-84 |
|
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: 266.62 E-value: 9.37e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 27 NEEQLMMRDSVKEFVDKELWAHKDRFEKKDYaYTQECMKKAGDLGFLSVAVPEAYGGMGMGFVNTVLVCDHISGATGSFS 106
Cdd:cd01162 2 NEEQRAIQEVARAFAAKEMAPHAADWDQKKH-FPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 107 TAFGAHTGIGTMpITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVLseDGKTYSITGQKMWISNAGF 186
Cdd:cd01162 81 AYISIHNMCAWM-IDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVR--EGDHYVLNGSKAFISGAGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 187 CSVFIVFARIGDD--KNITGFIVE-NTPdnGISMNEEEHKLGIRASSTRQVFFNDTKVPAENMLSERGNGFKIAMNALNV 263
Cdd:cd01162 158 SDVYVVMARTGGEgpKGISCFVVEkGTP--GLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 264 GRIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYRAAKDIEDritereaagsshq 343
Cdd:cd01162 236 GRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDR------------- 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 344 eaelkGVEEYAIECSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEINRML 413
Cdd:cd01162 303 -----GDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLI 367
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
28-409 |
2.83e-79 |
|
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: 254.73 E-value: 2.83e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 28 EEQLMMRDSVKEFVDKELWAHKDRFEKKDYaYTQECMKKAGDLGFLSVAVPEAYGGMGMGFVNTVLVCDHIsGATGSFST 107
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGE-VPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEEL-ARAGGSGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 108 AFGAHTGIGTMPITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAvlSEDGKTYSITGQKMWISNAGFC 187
Cdd:cd01160 79 GLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTA--RKDGDHYVLNGSKTFITNGMLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 188 SVFIVFARIGDDKN----ITGFIVENTPDnGISMNEEEHKLGIRASSTRQVFFNDTKVPAENMLSERGNGFKIAMNALNV 263
Cdd:cd01160 157 DVVIVVARTGGEARgaggISLFLVERGTP-GFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 264 GRIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYRAAkdiedritEREAAGSSHq 343
Cdd:cd01160 236 ERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCA--------WRHEQGRLD- 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500641789 344 eaelkgveeyAIECSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEI 409
Cdd:cd01160 307 ----------VAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEI 362
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
26-421 |
3.23e-75 |
|
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: 244.42 E-value: 3.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 26 FNEEQLMMRDSVKEFVDKELWAHKDRFEKKDyAYTQECMKKAGDLGFLSVAVPEAYGGMGMGFVNTVLVCDHIS-GATGs 104
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSG-EYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAyGCTG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 105 FSTAFGAhTGIGTMPITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVlsEDGKTYSITGQKMWISNA 184
Cdd:cd01157 79 VQTAIEA-NSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAE--KKGDEYIINGQKMWITNG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 185 GFCSVFIVFARIGDD------KNITGFIVE-NTPdnGISMNEEEHKLGIRASSTRQVFFNDTKVPAENMLSERGNGFKIA 257
Cdd:cd01157 156 GKANWYFLLARSDPDpkcpasKAFTGFIVEaDTP--GIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 258 MNALNVGRIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYRAAKDIEDRITEREA 337
Cdd:cd01157 234 MGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 338 AgsshqeaelkgveeyaiecSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEINRMLSVGM 417
Cdd:cd01157 314 A-------------------SIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISRE 374
|
....
gi 500641789 418 LIKK 421
Cdd:cd01157 375 HLGK 378
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
28-410 |
3.61e-69 |
|
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: 228.78 E-value: 3.61e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 28 EEQLMMRDSVKEFVDKELWAH-KDRFEKKDYAYtqECMKKAGDLGFLSvAVPEAYGGMGMGFVNTVLVCDHISGATGSFS 106
Cdd:cd01151 15 EEERAIRDTAREFCQEELAPRvLEAYREEKFDR--KIIEEMGELGLLG-ATIKGYGCAGLSSVAYGLIAREVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 107 TAFGAHTGIGTMPITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAvlSEDGKTYSITGQKMWISNAGF 186
Cdd:cd01151 92 SFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRA--RKDGGGYKLNGSKTWITNSPI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 187 CSVFIVFARIGDDKNITGFIVENTPDnGISMNEEEHKLGIRASSTRQVFFNDTKVPAENMLSErGNGFKIAMNALNVGRI 266
Cdd:cd01151 170 ADVFVVWARNDETGKIRGFILERGMK-GLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPG-AEGLRGPFKCLNNARY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 267 KLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYRAA--KDiEDRITEREAagsshqe 344
Cdd:cd01151 248 GIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGrlKD-QGKATPEQI------- 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500641789 345 aelkgveeyaiecSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEIN 410
Cdd:cd01151 320 -------------SLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIH 372
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
26-413 |
3.63e-63 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 213.58 E-value: 3.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 26 FNEEQLMMRDSVKEFVDKELWAHKDRFEKKDYAYTQ-ECMKKAGDLGFLSVAVPEAYGGMGMGFVNTVLVCDHISGATGS 104
Cdd:PLN02519 26 FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDvNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 105 FSTAFGAHTGIGTMPITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVLSEDGktYSITGQKMWISNA 184
Cdd:PLN02519 106 VGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 185 GFCSVFIVFARI---GDDKNITGFIVENTPDnGISMNEEEHKLGIRASSTRQVFFNDTKVPAENMLSERGNGFKIAMNAL 261
Cdd:PLN02519 184 PVAQTLVVYAKTdvaAGSKGITAFIIEKGMP-GFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 262 NVGRIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYRAAKDIEDRITEREaagss 341
Cdd:PLN02519 263 DLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK----- 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500641789 342 hqeaelkgveeyaiECSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEINRML 413
Cdd:PLN02519 338 --------------DCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRML 395
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
29-408 |
8.90e-58 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 199.39 E-value: 8.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 29 EQLMMRDSVKEFVDKELWAHKdRFEKKDYAYTQECMKKAGDLGFLSVAVPEAYGGMGMGFVNTVLVCDHISGATGSFSTA 108
Cdd:PTZ00461 40 EHAALRETVAKFSREVVDKHA-REDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 109 FGAHTGIGTMPITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVLSEDGKtYSITGQKMWISNAGFCS 188
Cdd:PTZ00461 119 YLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGN-YVLNGSKIWITNGTVAD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 189 VFIVFARIgdDKNITGFIVENTPdNGISMNEEEHKLGIRASSTRQVFFNDTKVPAENMLSERGNGFKIAMNALNVGRIKL 268
Cdd:PTZ00461 198 VFLIYAKV--DGKITAFVVERGT-KGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 269 AAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYRAAKDIEDRITEREAAGSShqeaelk 348
Cdd:PTZ00461 275 AAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAA------- 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 349 gveeyaiecsilKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNE 408
Cdd:PTZ00461 348 ------------KLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIE 395
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
60-409 |
4.42e-55 |
|
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: 191.83 E-value: 4.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 60 TQECMKKAGDLGFLSVAVPEAYGGMGMGFVNTVLVCDHISGATGSFSTAFGAHTGIGTmpITLYGTEEQKQKYVPKLASG 139
Cdd:cd01153 38 FKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQGAAAT--LLAHGTEAQREKWIPRLAEG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 140 EWFGAYCLTEPGAGSDANSGKTKAVLSEDGkTYSITGQKMWISNA-GFCS---VFIVFARIGDD----KNITGFIVENTP 211
Cdd:cd01153 116 EWTGTMCLTEPDAGSDLGALRTKAVYQADG-SWRINGVKRFISAGeHDMSeniVHLVLARSEGAppgvKGLSLFLVPKFL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 212 D----NGISMNEEEHKLGIRASSTRQVFFNDTKVPaenMLSERGNGFKIAMNALNVGRIKLAAACLDAQRRVITQAVNYS 287
Cdd:cd01153 195 DdgerNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 288 NERIQFNTAISQFGA--------IRSKLAEMATSCYAGESAT-YRAAKDIEDR--ITEREAAGSSHQEAELKgveeyaie 356
Cdd:cd01153 272 KERKQGGDLIKAAPAvtiihhpdVRRSLMTQKAYAEGSRALDlYTATVQDLAErkATEGEDRKALSALADLL-------- 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 500641789 357 CSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEI 409
Cdd:cd01153 344 TPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
25-409 |
9.36e-47 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 168.75 E-value: 9.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 25 DF--NEEQLMMRDSVKEFVDKElwAHKDRFEKKD--YAYTQECMKKAGDLGFLSVAVPEAYGGMGMGFVNTVLVCDHISG 100
Cdd:PRK12341 2 DFslTEEQELLLASIRELITRN--FPEEYFRTCDenGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 101 ATGS---FSTAFGAHTgigtmpITLYGTEEQKQKYVPK-LASGEwfGAYCL--TEPGAGSDANSGKTKAVlSEDGKTYsI 174
Cdd:PRK12341 80 CGAPaflITNGQCIHS------MRRFGSAEQLRKTAEStLETGD--PAYALalTEPGAGSDNNSATTTYT-RKNGKVY-L 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 175 TGQKMWISNAGFCSVFIVFARIGDDKN----ITGFIVE-NTPdnGISMnEEEHKLGIRASSTRQVFFNDTKVPAENMLSE 249
Cdd:PRK12341 150 NGQKTFITGAKEYPYMLVLARDPQPKDpkkaFTLWWVDsSKP--GIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 250 RGNGFKIAMNALNVGRIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYRAAKDIE 329
Cdd:PRK12341 227 EGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQAD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 330 DRITEReaagsshqeaelkgveeyaIECSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEI 409
Cdd:PRK12341 307 NGQSLR-------------------TSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEI 367
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
27-140 |
4.58e-39 |
|
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: 138.75 E-value: 4.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 27 NEEQLMMRDSVKEFVDKELWAHKDRFEKKDYaYTQECMKKAGDLGFLSVAVPEAYGGMGMGFVNTVLVCDHISGATGSFS 106
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGE-FPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVA 79
|
90 100 110
....*....|....*....|....*....|....
gi 500641789 107 TAFGAHTGIGTMPITLYGTEEQKQKYVPKLASGE 140
Cdd:pfam02771 80 LALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
26-409 |
2.55e-38 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 145.36 E-value: 2.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 26 FNEEQLMMRDSVKEFVDKELWAHKDRFEKKDYAYTQECMKKAGDLGFLSVAVPEAYGGMGMGFVNTVLVCDHISGATGSF 105
Cdd:PRK03354 5 LNDEQELFVAGIRELMASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 106 STAFGAHTGIGTmpITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTkAVLSEDGKTYsITGQKMWISNAG 185
Cdd:PRK03354 85 YVLYQLPGGFNT--FLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKT-TYTRRNGKVY-LNGSKCFITSSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 186 FCSVFIVFARIGDDKNI---TGFIVENTPDnGISMnEEEHKLGIRASSTRQVFFNDTKVPAENMLSERGNGFKIAMNALN 262
Cdd:PRK03354 161 YTPYIVVMARDGASPDKpvyTEWFVDMSKP-GIKV-TKLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 263 VGRIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYraakdiedriterEAAGSSH 342
Cdd:PRK03354 239 HERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLY-------------EAAWKAD 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500641789 343 QEAELKGveeyaiECSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEI 409
Cdd:PRK03354 306 NGTITSG------DAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEM 366
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
251-413 |
1.22e-36 |
|
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: 133.53 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 251 GNGFKIAMNALNVGRIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYRAAKDIED 330
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 331 RITEReaagsshqeaelkgveeyaIECSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEIN 410
Cdd:pfam00441 81 GGPDG-------------------AEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQ 141
|
...
gi 500641789 411 RML 413
Cdd:pfam00441 142 RNI 144
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
3-410 |
4.70e-36 |
|
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: 139.81 E-value: 4.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 3 DKTRGGQFIVKETKCEAIFTpeDFNEEQLMMRDSVKEFVDkELWAHKdrfekkdyAYTQecMKKAGDLGFLSVAVPEAYG 82
Cdd:cd01154 22 DLSRLGELAGGELYELARLA--DRNPPVLEMWDRWGRRVD-RVWVHP--------AWHA--LMRRLIEEGVINIEDGPAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 83 GMG--MGFVNTVLVCDHISGA----TGSFSTAFGahtgigtmpITLYGTEEQKQKYVPKLASGE---WFGAYCLTEPGAG 153
Cdd:cd01154 89 EGRrhVHFAAGYLLSDAAAGLlcplTMTDAAVYA---------LRKYGPEELKQYLPGLLSDRYktgLLGGTWMTEKQGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 154 SDANSGKTKAVLSEDGkTYSITGQKmWISNAGFCSVFIVFARIGDDKNITG----FIVENT-PD---NGISMNEEEHKLG 225
Cdd:cd01154 160 SDLGANETTAERSGGG-VYRLNGHK-WFASAPLADAALVLARPEGAPAGARglslFLVPRLlEDgtrNGYRIRRLKDKLG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 226 IRASSTRQVFFNDTKvpAEnMLSERGNGFKIAMNALNVGRIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRS 305
Cdd:cd01154 238 TRSVATGEVEFDDAE--AY-LIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 306 KLAEMATSCYAGESATYRAAkdiedRITEREAAGSSHQEAELKgveeyaIECSILKVAVSEDVQACADEGIQIFGGMGFS 385
Cdd:cd01154 315 DLAEMEVDVEAATALTFRAA-----RAFDRAAADKPVEAHMAR------LATPVAKLIACKRAAPVTSEAMEVFGGNGYL 383
|
410 420
....*....|....*....|....*
gi 500641789 386 EDTPMESAWRDARIARIYEGTNEIN 410
Cdd:cd01154 384 EEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
20-414 |
1.67e-35 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 138.06 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 20 IFTPEDFNeeqlmMRDSVKEFVDKELWAHKDRF-EKKDYAYtqECMKKAGDLGFLSVAVpEAYGGMGMGFVNTVLVCDHI 98
Cdd:PLN02526 28 LLTPEEQA-----LRKRVRECMEKEVAPIMTEYwEKAEFPF--HIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 99 SGATGSFSTAFGAHTGIGTMPITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVLSEDGktYSITGQK 178
Cdd:PLN02526 100 ARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG--WILNGQK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 179 MWISNAGFCSVFIVFARIGDDKNITGFIV-ENTPdnGISMNEEEHKLGIRASSTRQVFFNDTKVPAENMLSErGNGFKIA 257
Cdd:PLN02526 178 RWIGNSTFADVLVIFARNTTTNQINGFIVkKGAP--GLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPG-VNSFQDT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 258 MNALNVGRIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYRAAKdiedrITEREA 337
Cdd:PLN02526 255 NKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCK-----LYESGK 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500641789 338 AGSSHqeaelkgveeyaieCSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEINRMLS 414
Cdd:PLN02526 330 MTPGH--------------ASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVT 392
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
34-411 |
7.92e-35 |
|
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: 135.98 E-value: 7.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 34 RDSVKEFVDKELW-----AHKDRFEKKDYAYTQ-----ECMKKAGDLGFLSVAVPEAYGGMGMGFVNTVLVCDhISGATG 103
Cdd:cd01155 7 RARVKAFMEEHVYpaeqeFLEYYAEGGDRWWTPppiieKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAE-ETGRSF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 104 SFSTAFG-AHTGIGTMPI-TLYGTEEQKQKYVPKLASGEWFGAYCLTEPG-AGSDANSGKTKavLSEDGKTYSITGQKMW 180
Cdd:cd01155 86 FAPEVFNcQAPDTGNMEVlHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECS--IERDGDDYVINGRKWW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 181 ISNAGF--CSVFIVFARIGDDKNI-----TGFIVE-NTPdnGISMneeehklgIRASstrQVF-------------FNDT 239
Cdd:cd01155 164 SSGAGDprCKIAIVMGRTDPDGAPrhrqqSMILVPmDTP--GVTI--------IRPL---SVFgyddaphghaeitFDNV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 240 KVPAENMLSERGNGFKIAMNALNVGRIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGES 319
Cdd:cd01155 231 RVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 320 ATYRAAKDIeDRITEREAAGsshqeaelkgveeyaiECSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARI 399
Cdd:cd01155 311 LVLKAAHMI-DTVGNKAARK----------------EIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWART 373
|
410
....*....|..
gi 500641789 400 ARIYEGTNEINR 411
Cdd:cd01155 374 LRIADGPDEVHL 385
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
58-426 |
4.26e-33 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 134.23 E-value: 4.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 58 AYTQECMKkagdlGFLSVAVPEAYGGMGM----GFVNTVLVcdhisgATGSFSTAFGAHTGIGTM-PITLYGTEEQKQKY 132
Cdd:PTZ00456 104 AYQALKAG-----GWTGISEPEEYGGQALplsvGFITRELM------ATANWGFSMYPGLSIGAAnTLMAWGSEEQKEQY 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 133 VPKLASGEWFGAYCLTEPGAGSDANSGKTKAVLSEDGkTYSITGQKMWISnAGFCS-----VFIVFARIGDD----KNIT 203
Cdd:PTZ00456 173 LTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADG-SYKITGTKIFIS-AGDHDlteniVHIVLARLPNSlpttKGLS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 204 GFIVEN---TPDNGISMNEE------EHKLGIRASSTRQVFFNDTKvpaENMLSERGNGFKIAMNALNVGRIKLAAACLD 274
Cdd:PTZ00456 251 LFLVPRhvvKPDGSLETAKNvkciglEKKMGIKGSSTCQLSFENSV---GYLIGEPNAGMKQMFTFMNTARVGTALEGVC 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 275 AQRRVITQAVNYSNERiqfntaISQFGAIRSKLAEMATS---CYAGESATYRAAKDIED----------RITEREAAGSS 341
Cdd:PTZ00456 328 HAELAFQNALRYARER------RSMRALSGTKEPEKPADriiCHANVRQNILFAKAVAEggrallldvgRLLDIHAAAKD 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 342 HQEAELKGvEEYAIECSILKVAVSE-DVQAcADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEINrmlSVGMLIK 420
Cdd:PTZ00456 402 AATREALD-HEIGFYTPIAKGCLTEwGVEA-ASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQ---ALDFIGR 476
|
....*.
gi 500641789 421 KAMKGH 426
Cdd:PTZ00456 477 KVLSLK 482
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
34-411 |
3.27e-31 |
|
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: 125.15 E-value: 3.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 34 RDSVKEFVD----KELWAHKDRFEKKDYAYTQECMKKAGDLGFLSVAVPEAYGGMGMGFVNTVLVCDHI--SGATGSFST 107
Cdd:cd01152 7 RAEVRAWLAahlpPELREESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMaaAGAPVPFNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 108 AfgahtGIGTMPITL--YGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVLseDGKTYSITGQKMWISNAG 185
Cdd:cd01152 87 I-----GIDLAGPTIlaYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVR--DGDDWVVNGQKIWTSGAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 186 FCSVFIVFARIGDD----KNITGFIVE-NTPdnGISMNEEEHKLGirASSTRQVFFNDTKVPAENMLSERGNGFKIAMNA 260
Cdd:cd01152 160 YADWAWLLVRTDPEapkhRGISILLVDmDSP--GVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 261 LNVGRIKLA--AACLDAQRRVITQAVNYSNERIQFntaisqFGAIRSKLAEMAtscyagesATYRAAKDIEDRITEREAA 338
Cdd:cd01152 236 LNFERVSIGgsAATFFELLLARLLLLTRDGRPLID------DPLVRQRLARLE--------AEAEALRLLVFRLASALAA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 339 GS-SHQEAelkgveeyaiecSILKVAVSEDVQACADEGIQIFGGMG-FSEDTPM-------ESAWRDARIARIYEGTNEI 409
Cdd:cd01152 302 GKpPGAEA------------SIAKLFGSELAQELAELALELLGTAAlLRDPAPGaelagrwEADYLRSRATTIYGGTSEI 369
|
..
gi 500641789 410 NR 411
Cdd:cd01152 370 QR 371
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
144-237 |
1.55e-21 |
|
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: 89.26 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 144 AYCLTEPGAGSDANSGKTKAVlSEDGKTYSITGQKMWISNAGFCSVFIVFARIGDDK---NITGFIVE-NTPdnGISMNE 219
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAA-DGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDrhgGISLFLVPkDAP--GVSVRR 77
|
90
....*....|....*...
gi 500641789 220 EEHKLGIRASSTRQVFFN 237
Cdd:pfam02770 78 IETKLGVRGLPTGELVFD 95
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
116-409 |
1.00e-17 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 87.16 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 116 GTMPITL-YGTEEQKQKYVPKLASGEWFGAYCLTEPG-AGSDANSgkTKAVLSEDGKTYSITGQKMWISNA--GFCSVFI 191
Cdd:PLN02876 524 GNMEVLLrYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATN--IECSIRRQGDSYVINGTKWWTSGAmdPRCRVLI 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 192 VFARI----GDDKNITGFIVE-NTPdnGISMNEEEHKLGIRAS--STRQVFFNDTKVPAENMLSERGNGFKIAMNALNVG 264
Cdd:PLN02876 602 VMGKTdfnaPKHKQQSMILVDiQTP--GVQIKRPLLVFGFDDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPG 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 265 RIKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESATYRAAkDIEDRITEREAAGSshqe 344
Cdd:PLN02876 680 RLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAA-DQLDRLGNKKARGI---- 754
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500641789 345 aelkgveeyaieCSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNEI 409
Cdd:PLN02876 755 ------------IAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
268-408 |
5.91e-15 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 71.99 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 268 LAAACLDAQRRVITQAVNYSNERIQ--FNTAISQFGAIRSKLAEMATSCYAGESATYRAAKDIEDRItereAAGSSHQEA 345
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAA----AAGKPVTPA 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500641789 346 ELKgveeyaiECSILKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEGTNE 408
Cdd:pfam08028 78 LRA-------EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
35-320 |
2.99e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 72.68 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 35 DSVKEFVD--KELWahkdrfekkDYaytqecMKKAGdlgFLSVAVPEAYGGMGMG-FVNTVLVCdHIsgATGSFSTAFGA 111
Cdd:PRK13026 101 DIVQNRKDlpPEVW---------DY------LKKEG---FFALIIPKEYGGKGFSaYANSTIVS-KI--ATRSVSAAVTV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 112 HT----GIGTMpITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVLSE---DGKT---YSITGQKMWI 181
Cdd:PRK13026 160 MVpnslGPGEL-LTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRgefEGEEvlgLRLTWDKRYI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 182 SNAGFCSV----FIVF---ARIGDDKN--IT-GFIVENTPdnGISMNEEEHKLGirasstrQVFFN------DTKVPAEN 245
Cdd:PRK13026 239 TLAPVATVlglaFKLRdpdGLLGDKKElgITcALIPTDHP--GVEIGRRHNPLG-------MAFMNgttrgkDVFIPLDW 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 246 MLSER---GNGFKIAMNALNVGR-IKL---AAACLDAQRRVITQavnYSNERIQFNTAISQFGAIRSKLAEMATSCYAGE 318
Cdd:PRK13026 310 IIGGPdyaGRGWRMLVECLSAGRgISLpalGTASGHMATRTTGA---YAYVRRQFGMPIGQFEGVQEALARIAGNTYLLE 386
|
..
gi 500641789 319 SA 320
Cdd:PRK13026 387 AA 388
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
71-321 |
8.28e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 71.39 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 71 GFLSVAVPEAYGGMGmgfvntvlvcdhisgatgsFSTAfgAHTGI--------GTMPITL--------------YGTEEQ 128
Cdd:PRK09463 122 GFFGMIIPKEYGGLE-------------------FSAY--AHSRVlqklasrsGTLAVTVmvpnslgpgelllhYGTDEQ 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 129 KQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVL---SEDGKT---YSITGQKMWISNAGFCSVFIVFAR------- 195
Cdd:PRK09463 181 KDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVckgEWQGEEvlgMRLTWNKRYITLAPIATVLGLAFKlydpdgl 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 196 IGDDKN--IT-GFIVENTPdnGISMNEEEHKLGirasstrQVFFN------DTKVPAENMLSER---GNGFKIAMNALNV 263
Cdd:PRK09463 261 LGDKEDlgITcALIPTDTP--GVEIGRRHFPLN-------VPFQNgptrgkDVFIPLDYIIGGPkmaGQGWRMLMECLSV 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 500641789 264 GR-IKLAAACLDAQRRVITQAVNYSNERIQFNTAISQFGAIRSKLAEMATSCYAGESAT 321
Cdd:PRK09463 332 GRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAAR 390
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
124-407 |
2.33e-12 |
|
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: 69.67 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 124 GTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVLSEDGKTYSI-----TGQKMWISNAGF-CSVFIVFARI- 196
Cdd:cd01150 117 GTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFVIntpdfTATKWWPGNLGKtATHAVVFAQLi 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 197 --GDDKNITGFIVE------NTPDNGISMNEEEHKLGIRASSTRQVFFNDTKVPAENMLSERGN---------------- 252
Cdd:cd01150 197 tpGKNHGLHAFIVPirdpktHQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDvspdgtyvspfkdpnk 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 253 GFKIAMNALNVGRIKLAAACLDAQRRVITQAVNYSNERIQF-------NTAISQFGAIRSKLAEMATSCYAGESATyraa 325
Cdd:cd01150 277 RYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFgpkpsdpEVQILDYQLQQYRLFPQLAAAYAFHFAA---- 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 326 KDIEDRITEREAAGSSHQEAELKgvEEYAIECSiLKVAVSEDVQACADEGIQIFGGMGFSEDTPMESAWRDARIARIYEG 405
Cdd:cd01150 353 KSLVEMYHEIIKELLQGNSELLA--ELHALSAG-LKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEG 429
|
..
gi 500641789 406 TN 407
Cdd:cd01150 430 DN 431
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
81-322 |
3.98e-10 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 62.59 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 81 YGGMGMGFVNTVLVCDHI--SGATGSFSTAfgAHTGIGTMPITLYGTEEQKQKYVPKLASGEWFGAYClTEPGAGSDANS 158
Cdd:PTZ00457 74 YGGLGLGHTAHALIYEEVgtNCDSKLLSTI--QHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISM 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 159 GKTKAVLSEDGKtYSITGQKMWIsNAGFCSVFIVFArigddKNITGFIVENTPdngisMNEEEHKLGIRASSTRQVFFND 238
Cdd:PTZ00457 151 NTTKASLTDDGS-YVLTGQKRCE-FAASATHFLVLA-----KTLTQTAAEEGA-----TEVSRNSFFICAKDAKGVSVNG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 239 TKV-----PAENMLSERGNGFKIAMNALNVGRIKLAAACLDAQRRVItQAVNYSNERiQFNTAIsqfgairskLAEMATS 313
Cdd:PTZ00457 219 DSVvfentPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVV-QELRGSNAE-EGATDT---------VASFACA 287
|
....*....
gi 500641789 314 CYAGESATY 322
Cdd:PTZ00457 288 MYAMESTLY 296
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
69-398 |
6.10e-10 |
|
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: 61.18 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 69 DLGFLSVAVPEAYGGMGMGFVNTVLVCDHISGATGSFSTAFGAHTGIgTMPITLYGTEEQKQKYVPKLASGEWFGayclt 148
Cdd:cd01163 33 QSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGF-VEALLLAGPEQFRKRWFGRVLNGWIFG----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 149 epGAGSDANSGKTKAVLSE---DGKTYSITGQKMWISNAGFCSVFIVFARIGDDKNItgFIVENTPDNGISMNEEEHKLG 225
Cdd:cd01163 107 --NAVSERGSVRPGTFLTAtvrDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGKLV--FAAVPTDRPGITVVDDWDGFG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 226 IR--ASSTrqVFFNDTKVPAENmLSERGNGFKIAMNALNVGRIKLAAACLDAQRRVITQAVNYSNERIQ------FNTAI 297
Cdd:cd01163 183 QRltASGT--VTFDNVRVEPDE-VLPRPNAPDRGTLLTAIYQLVLAAVLAGIARAALDDAVAYVRSRTRpwihsgAESAR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 298 SQFGAIRSkLAEMATSCYAGESATYRAAKDIeDRITEREAAGSSHQEAELkgveeyAIECSILKVAVSEDVQACADEGIQ 377
Cdd:cd01163 260 DDPYVQQV-VGDLAARLHAAEALVLQAARAL-DAAAAAGTALTAEARGEA------ALAVAAAKVVVTRLALDATSRLFE 331
|
330 340
....*....|....*....|.
gi 500641789 378 IFGGMGFSEDTPMESAWRDAR 398
Cdd:cd01163 332 VGGASATAREHNLDRHWRNAR 352
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
46-316 |
9.85e-09 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 58.32 E-value: 9.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 46 WAHKDRFEKKdYAYTQECMKKagdlgfLSVAVPEAYGGMgmgfvntvlvcdhISGATGSFSTAfgAHTGIGTMPITLYGT 125
Cdd:PTZ00460 54 WSRQDQILLN-AEKTREAHKH------LNLANPNYYTPN-------------LLCPQGTFIST--VHFAMVIPAFQVLGT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 126 EEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVLSEDGK-----TYSITGQKMWISNAGFCSVF-IVFARI--- 196
Cdd:PTZ00460 112 DEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNefvihTPSVEAVKFWPGELGFLCNFaLVYAKLivn 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 197 GDDKNITGFIVE----NT--PDNGISMNEEEHKLGIRASSTRQVFFNDTKVPAENMLS-----------ERGNGFKIAMN 259
Cdd:PTZ00460 192 GKNKGVHPFMVRirdkEThkPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAryikvsedgqvERQGNPKVSYA 271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500641789 260 ALNVGRIKLAAACLDAQRRVITQAVNYSNERIQFN------TAISQFGAIRSKLAEMATSCYA 316
Cdd:PTZ00460 272 SMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTndnkqeNSVLEYQTQQQKLLPLLAEFYA 334
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
69-407 |
1.87e-08 |
|
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: 56.59 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 69 DLGFLSVAVPEAYGGMGMGFVNTVLVCDHISGATGSfsTAFGAhtgigtmpiTLYGTEEQKQKYVPKLASGEWFGayclT 148
Cdd:cd01159 33 EIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGS--AAWVA---------SIVATHSRMLAAFPPEAQEEVWG----D 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 149 EPG---AGSDANSGKTKAVlsEDGktYSITGQKMWISNAGFCSVFIVFARIGDDKNITGFIVENTPDNGISMNEEEHKLG 225
Cdd:cd01159 98 GPDtllAGSYAPGGRAERV--DGG--YRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAFVVPRAEYEIVDTWHVVG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 226 IRASSTRQVFFNDTKVPAENMLSE----RGNG-------FKIAMNALNVgrIKLAAACLDAQRRVITQAVNYSNERIQFN 294
Cdd:cd01159 174 LRGTGSNTVVVDDVFVPEHRTLTAgdmmAGDGpggstpvYRMPLRQVFP--LSFAAVSLGAAEGALAEFLELAGKRVRQY 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 295 TA---ISQFGAIRSKLAEMATSCyagesatyRAAKDIEDRITEREAAGSshQEAELKGVEE---------YAIECSIlkv 362
Cdd:cd01159 252 GAavkMAEAPITQLRLAEAAAEL--------DAARAFLERATRDLWAHA--LAGGPIDVEErarirrdaaYAAKLSA--- 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 500641789 363 avsEDVQACADEGiqifGGMGFSEDTPMESAWRDARIARIYEGTN 407
Cdd:cd01159 319 ---EAVDRLFHAA----GGSALYTASPLQRIWRDIHAAAQHAALN 356
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
98-409 |
7.98e-08 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 55.25 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 98 ISGATGSFSTAFGAHTGI-----GTMPITLyGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVLSEDGKTY 172
Cdd:PLN02636 126 ITEAVGSVDMSLGIKLGVqyslwGGSVINL-GTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEF 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 173 SIT-----GQKMWISNAGFCSVFI-VFARI--------GD-DKNITGFIV------ENTPDNGISMNEEEHKLGIRASST 231
Cdd:PLN02636 205 VINtpndgAIKWWIGNAAVHGKFAtVFARLklpthdskGVsDMGVHAFIVpirdmkTHQVLPGVEIRDCGHKVGLNGVDN 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 232 RQVFFNDTKVPAENMLSERGN----------------GFKIAMNALNVGRIKLAAACLDAQRRVITQAVNYSNERIQF-- 293
Cdd:PLN02636 285 GALRFRSVRIPRDNLLNRFGDvsrdgkytsslptinkRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFgp 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 294 ----NTAISQFGAIRSKLAEMATSCYAGESAT-YRAAKDIEDRIT-EREAAGSSHqeAELKGVEEYAIecSILKVAVSED 367
Cdd:PLN02636 365 pkqpEISILDYQSQQHKLMPMLASTYAFHFATeYLVERYSEMKKThDDQLVADVH--ALSAGLKAYIT--SYTAKALSTC 440
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 500641789 368 VQACadegiqifGGMGFSEDTPMESAWRDARIARIYEGTNEI 409
Cdd:PLN02636 441 REAC--------GGHGYAAVNRFGSLRNDHDIFQTFEGDNTV 474
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
112-316 |
1.27e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 54.84 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 112 HTGIGTMPITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTKAVLSEDGKTYSI-----TGQKMWISNAGF 186
Cdd:PLN02443 102 HWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIhsptlTSSKWWPGGLGK 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 187 CSVF-IVFARI---GDDKNITGFIVE------NTPDNGISMNEEEHKLGIRASSTRQ---VFFNDTKVPAENMLSERGNG 253
Cdd:PLN02443 182 VSTHaVVYARLitnGKDHGIHGFIVQlrslddHSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSKV 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 254 FK------------IAMNALNVGRIKLAAACLDAQRRVITQAVNYSNERIQF-------NTAISQFGAIRSKLAEMATSC 314
Cdd:PLN02443 262 TRegkyvqsdvprqLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFgsqdggpETQVIDYKTQQSRLFPLLASA 341
|
..
gi 500641789 315 YA 316
Cdd:PLN02443 342 YA 343
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
104-296 |
5.12e-03 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 39.76 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 104 SFSTAFGAHTGIGTMPITLYGTEEQKQKYVPKLASGEWFGAYCLTEPGAGSDANSGKTkaVLSEDGKTYSI-------TG 176
Cdd:PLN02312 148 SLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIET--VTTYDPKTEEFvintpceSA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641789 177 QKMWISNAG-FCSVFIVFARI---GDDKNITGFIVENTPDNG-----ISMNEEEHKLGIRASSTRQVFFNDTKVPAENML 247
Cdd:PLN02312 226 QKYWIGGAAnHATHTIVFSQLhinGKNEGVHAFIAQIRDQDGnicpnIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLL 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500641789 248 S-------------------ERGNGFkiaMNALNVGRIKLAAACLDAQRRVITQAVNYSNERIQFNTA 296
Cdd:PLN02312 306 NsvadvspdgkyvsaikdpdQRFGAF---LAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAFSVT 370
|
|
| |
