|
Name |
Accession |
Description |
Interval |
E-value |
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
39-412 |
0e+00 |
|
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: 745.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 39 LNEEQKGFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTT 118
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 119 AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDI 198
Cdd:cd01162 81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 199 YVVMCRTGESGAKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINV 278
Cdd:cd01162 161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 279 ASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVALCSMAKLFATE 358
Cdd:cd01162 241 ASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 118403322 359 ECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQ 412
Cdd:cd01162 321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
37-411 |
1.53e-152 |
|
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: 436.58 E-value: 1.53e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 37 LGLNEEQKGFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTS 116
Cdd:COG1960 3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 117 TTAYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGES 196
Cdd:COG1960 83 LALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 197 DIYVVMCRT-GESGAKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGR 275
Cdd:COG1960 163 DVILVLARTdPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 276 INVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEErEDAVALCSMAKLF 355
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAG-EDAALEAAMAKLF 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 118403322 356 ATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLL 411
Cdd:COG1960 322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
41-411 |
4.35e-147 |
|
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: 422.45 E-value: 4.35e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 41 EEQKGFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAY 120
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 121 ISIHN-MCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIY 199
Cdd:cd01158 81 VSVHNsLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 200 VVMCRTGES-GAKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINV 278
Cdd:cd01158 161 IVFAVTDPSkGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 279 ASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAvALQEEREDAVALCSMAKLFATE 358
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAA-RLKDNGEPFIKEAAMAKLFASE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 118403322 359 ECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLL 411
Cdd:cd01158 320 VAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLL 372
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
41-408 |
1.38e-121 |
|
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: 355.82 E-value: 1.38e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 41 EEQKGFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLgfggvyvrtdvggsglsrldtsvifealatgctsttay 120
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLL-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 121 isihnMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYV 200
Cdd:cd00567 43 -----LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 201 VMCRTGESGA--KGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINV 278
Cdd:cd00567 118 VLARTDEEGPghRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 279 ASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVALCSMAKLFATE 358
Cdd:cd00567 198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATE 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 118403322 359 ECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISR 408
Cdd:cd00567 278 AAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
38-412 |
6.05e-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: 304.72 E-value: 6.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 38 GLNEEQKGFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTST 117
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 118 TAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGES 196
Cdd:cd01156 81 ALSYGAHsNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 197 DIYVVMCRTG-ESGAKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGR 275
Cdd:cd01156 161 DTLVVYAKTDpSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 276 INVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVAlCSMAKLF 355
Cdd:cd01156 241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKD-AAGVILY 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 118403322 356 ATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQ 412
Cdd:cd01156 320 AAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
41-411 |
1.34e-99 |
|
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: 301.34 E-value: 1.34e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 41 EEQKGFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALA-TGCTSTTa 119
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELArAGGSGPG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 120 yISIHN-MCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDI 198
Cdd:cd01160 80 -LSLHTdIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 199 YVVMCRTG--ESGAKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRI 276
Cdd:cd01160 159 VIVVARTGgeARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 277 NVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDaVALCSMAKLFA 356
Cdd:cd01160 239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD-VAEASMAKYWA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 118403322 357 TEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLL 411
Cdd:cd01160 318 TELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
39-411 |
1.31e-87 |
|
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: 271.00 E-value: 1.31e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 39 LNEEQKGFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTT 118
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 119 AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDI 198
Cdd:cd01157 81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 199 YVVMCRTGES----GAKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGG 274
Cdd:cd01157 161 YFLLARSDPDpkcpASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 275 RINVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVaLCSMAKL 354
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTY-YASIAKA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 118403322 355 FATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLL 411
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
37-413 |
1.84e-87 |
|
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: 271.65 E-value: 1.84e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 37 LGLNEEQKGFQKVAFD----FAAREMAPnmAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALAT 112
Cdd:cd01161 21 SVLTEEQTEELNMLVGpvekFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 113 GCTSTTAYiSIHNMCAWM-IDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAK--QQGDHYILNGSKAF 189
Cdd:cd01161 99 DLGFSVTL-GAHQSIGFKgILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVlsEDGKHYVLNGSKIW 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 190 ISGGGESDIYVVMCRTGESGAKG-----ISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGF 264
Cdd:cd01161 178 ITNGGIADIFTVFAKTEVKDATGsvkdkITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 265 LIAMKGLNGGRINVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMI-RTAAVALQEERE 343
Cdd:cd01161 258 KVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAyMTSGNMDRGLKA 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 344 DAVALCSMAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQD 413
Cdd:cd01161 338 EYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQH 407
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
35-413 |
3.85e-62 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 205.88 E-value: 3.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 35 PSLGLNEEQKGFQKVAFDFAAREMAPNMAEWDQKELFP--VDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALAT 112
Cdd:PLN02519 22 SSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 113 GCTSTTAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFIS 191
Cdd:PLN02519 102 ASGSVGLSYGAHsNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 192 GGGESDIYVVMCRTG-ESGAKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKG 270
Cdd:PLN02519 182 NGPVAQTLVVYAKTDvAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 271 LNGGRINVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVAlCS 350
Cdd:PLN02519 262 LDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKD-CA 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118403322 351 MAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQD 413
Cdd:PLN02519 341 GVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
39-408 |
3.13e-60 |
|
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: 200.28 E-value: 3.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 39 LNEEQKGFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRtDVGGSGLSRLDTSVI---FEALATGCT 115
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIareVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 116 STtayISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGG 194
Cdd:cd01151 92 SF---MSVQsSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 195 ESDIYVVMCRTGESGakGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIgTEGQGFLIAMKGLNGG 274
Cdd:cd01151 169 IADVFVVWARNDETG--KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 275 RINVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLM-IRTAavALQEEREDAVALCSMAK 353
Cdd:cd01151 246 RYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLAcLRVG--RLKDQGKATPEQISLLK 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 118403322 354 LFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISR 408
Cdd:cd01151 324 RNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGR 378
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
62-413 |
7.33e-52 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 178.00 E-value: 7.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 62 MAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTstTAYISIHNMCAWMIDSFGNEEQRH 141
Cdd:PRK12341 29 FRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGA--PAFLITNGQCIHSMRRFGSAEQLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 142 KfcpplcTMEKFA-----SYCL--TEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYVVMCRTGESGA--KG 212
Cdd:PRK12341 107 K------TAESTLetgdpAYALalTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLARDPQPKDpkKA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 213 ISCIVVEKGTPGLSFGKKEKkVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASVIL 292
Cdd:PRK12341 181 FTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFED 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 293 TQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAValqeEREDAVAL---CSMAKLFATEECFAICNQALQ 369
Cdd:PRK12341 260 AARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAW----QADNGQSLrtsAALAKLYCARTAMEVIDDAIQ 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 118403322 370 MHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQD 413
Cdd:PRK12341 336 IMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKD 379
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
261-410 |
1.07e-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: 165.12 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 261 GQGFLIAMKGLNGGRINVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQE 340
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 341 EREDAVAlCSMAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNL 410
Cdd:pfam00441 81 GGPDGAE-ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
52-399 |
6.56e-49 |
|
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: 171.03 E-value: 6.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 52 DFAAREMAPNMAEWDQKEL--------FP---VDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTsTTAY 120
Cdd:cd01153 7 RLAENVLAPLNADGDREGPvfddgrvvVPppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDA-PLMY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 121 ISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGD-HYILNGSKAFISGG----GE 195
Cdd:cd01153 86 ASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGehdmSE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 196 SDIYVVMCRTGE--SGAKGISCIVVEK----GTP-GLSFGKKEKKVGWNSQPTRAVIFEDCAVPVanrIGTEGQGFLIAM 268
Cdd:cd01153 166 NIVHLVLARSEGapPGVKGLSLFLVPKflddGERnGVTVARIEEKMGLHGSPTCELVFDNAKGEL---IGEEGMGLAQMF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 269 KGLNGGRINVASCSLGAAHASVILTQEHLKVRKQFGAPL--------ARSQYLQFQLADMATKLVASRLMIRTAAVALQE 340
Cdd:cd01153 243 AMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIkaapavtiIHHPDVRRSLMTQKAYAEGSRALDLYTATVQDL 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118403322 341 EREDAV-------------ALCSMAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSN 399
Cdd:cd01153 323 AERKATegedrkalsaladLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTT 394
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
5-412 |
3.95e-44 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 158.56 E-value: 3.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 5 RSGYRRFGCLRAALKSLAQTHHRSITFCIDPSlglnEEQKGFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGF 84
Cdd:PTZ00461 7 SSLGRRSATCGWTAAATMTSASRAFMDLYNPT----PEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 85 GGVYVRTDVGGSGLSRLDTSVIFEALATG----CTsttAYISiHNMCawMIDSFGNE---EQRHKFCPPLCTMEKFASYC 157
Cdd:PTZ00461 83 MGVTVPEADGGAGMDAVAAVIIHHELSKYdpgfCL---AYLA-HSML--FVNNFYYSaspAQRARWLPKVLTGEHVGAMG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 158 LTEPGSGSDAASLLTSAKQQGD-HYILNGSKAFISGGGESDIYVVMCRTGESgakgISCIVVEKGTPGLSFGKKEKKVGW 236
Cdd:PTZ00461 157 MSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVADVFLIYAKVDGK----ITAFVVERGTKGFTQGPKIDKCGM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 237 NSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQ 316
Cdd:PTZ00461 233 RASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 317 LADMATKLVASRLMIRTAAVALQEEREDAVAlCSMAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILE 396
Cdd:PTZ00461 313 IAEGYADTEAAKALVYSVSHNVHPGNKNRLG-SDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGG 391
|
410
....*....|....*.
gi 118403322 397 GSNEVMRMLISRNLLQ 412
Cdd:PTZ00461 392 GTIEAHHKNITKDLLK 407
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
39-413 |
8.71e-42 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 151.52 E-value: 8.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 39 LNEEQKGFQKVAFDFAAREMAPN-MAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALatGCTST 117
Cdd:PRK03354 5 LNDEQELFVAGIRELMASENWEAyFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL--GRLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 118 TAYISIHNMCAW-MIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGES 196
Cdd:PRK03354 83 PTYVLYQLPGGFnTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 197 DIYVVMCRTGESGAKGI-SCIVVEKGTPGLSFGKKEkKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGR 275
Cdd:PRK03354 163 PYIVVMARDGASPDKPVyTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 276 INVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVAlQEEREDAVALCSMAKLF 355
Cdd:PRK03354 242 FLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWK-ADNGTITSGDAAMCKYF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 118403322 356 ATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQD 413
Cdd:PRK03354 321 CANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
39-410 |
5.32e-39 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 144.61 E-value: 5.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 39 LNEEQKGFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRtDVGGSGLSRLDTSVIFEALATGCTSTT 118
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK-GYGCPGLSITASAIATAEVARVDASCS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 119 AYISIHN-MCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESD 197
Cdd:PLN02526 108 TFILVHSsLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 198 IYVVMCRTGESgaKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIgTEGQGFLIAMKGLNGGRIN 277
Cdd:PLN02526 188 VLVIFARNTTT--NQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL-PGVNSFQDTNKVLAVSRVM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 278 VASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADM-----ATKLVASRLmirtaaVALQEEREDAVALCSMA 352
Cdd:PLN02526 265 VAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMlgniqAMFLVGWRL------CKLYESGKMTPGHASLG 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 118403322 353 KLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNL 410
Cdd:PLN02526 339 KAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
77-412 |
8.97e-39 |
|
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: 143.26 E-value: 8.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 77 RKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASY 156
Cdd:cd01152 42 RALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 157 CLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYVVMCRTGESGAK--GISCIVVEKGTPGLSFGKKEKKV 234
Cdd:cd01152 122 GFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEAPKhrGISILLVDMDSPGVTVRPIRSIN 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 235 GwnSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGR---INVASCSLGAAHASVILTQEHlkvrkqfGAPLARSQ 311
Cdd:cd01152 202 G--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERvsiGGSAATFFELLLARLLLLTRD-------GRPLIDDP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 312 YLQFQLADMATKLVASRLMIRTAAVALQEEReDAVALCSMAKLFATEECFAICNQALQMHGGYGYLKDYA--------VQ 383
Cdd:cd01152 273 LVRQRLARLEAEAEALRLLVFRLASALAAGK-PPGAEASIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWE 351
|
330 340
....*....|....*....|....*....
gi 118403322 384 QYMRDSRVHQILEGSNEVMRMLISRNLLQ 412
Cdd:cd01152 352 ADYLRSRATTIYGGTSEIQRNIIAERLLG 380
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
54-412 |
2.87e-38 |
|
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: 142.14 E-value: 2.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 54 AAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEAL--------ATGCTSTtayiSIHN 125
Cdd:cd01155 25 FLEYYAEGGDRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETgrsffapeVFNCQAP----DTGN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 126 McaWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPG-SGSDAASLLTSAKQQGDHYILNGSKAFISGGGESD--IYVVM 202
Cdd:cd01155 101 M--EVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGDPRckIAIVM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 203 CRTGESGA---KGISCIVVEKGTPGLSFGKKEKKVGWNSQPT--RAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRIN 277
Cdd:cd01155 179 GRTDPDGAprhRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIH 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 278 VASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVAL-QEEREDAVALCSMAKLFA 356
Cdd:cd01155 259 HCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIdTVGNKAARKEIAMIKVAA 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 118403322 357 TEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQ 412
Cdd:cd01155 339 PRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
40-151 |
9.53e-38 |
|
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: 132.59 E-value: 9.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 40 NEEQKGFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTA 119
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 118403322 120 YISIHN-MCAWMIDSFGNEEQRHKFCPPLCTME 151
Cdd:pfam02771 81 ALSVHSsLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
121-402 |
5.70e-32 |
|
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: 125.56 E-value: 5.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 121 ISIHNMCAWMIDSFGNEEQRHkFCPPLCTMEK----FASYCLTEPGSGSDAASLLTSA-KQQGDHYILNGSKAFISGGgE 195
Cdd:cd01154 113 LTMTDAAVYALRKYGPEELKQ-YLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAeRSGGGVYRLNGHKWFASAP-L 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 196 SDIYVVMCRT--GESGAKGISCIVV----EKGT-PGLSFGKKEKKVGWNSQPTRAVIFEDCavpVANRIGTEGQGFLIAM 268
Cdd:cd01154 191 ADAALVLARPegAPAGARGLSLFLVprllEDGTrNGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYIL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 269 KGLNGGRINVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQ-------EE 341
Cdd:cd01154 268 EMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDraaadkpVE 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118403322 342 REDAVALCSMAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVM 402
Cdd:cd01154 348 AHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
155-247 |
5.34e-29 |
|
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: 108.52 E-value: 5.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 155 SYCLTEPGSGSDAASLLTSA-KQQGDHYILNGSKAFISGGGESDIYVVMCRTG-ESGAKGISCIVVEKGTPGLSFGKKEK 232
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGgDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 118403322 233 KVGWNSQPTRAVIFE 247
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
134-412 |
8.37e-24 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 104.11 E-value: 8.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 134 FGNEEQRHKFCPPLCTMEKFASYCLTEPG-SGSDAASLLTSAKQQGDHYILNGSKAFISGGGES--DIYVVMCRTGESGA 210
Cdd:PLN02876 532 YGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPrcRVLIVMGKTDFNAP 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 211 --KGISCIVVEKGTPGLSFGKKEKKVGWNSQPT--RAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAA 286
Cdd:PLN02876 612 khKQQSMILVDIQTPGVQIKRPLLVFGFDDAPHghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAA 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 287 HASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEE-REDAVALCSMAKLFATEECFAICN 365
Cdd:PLN02876 692 ERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRLgNKKARGIIAMAKVAAPNMALKVLD 771
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 118403322 366 QALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQ 412
Cdd:PLN02876 772 MAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKLELQ 818
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
83-411 |
3.53e-21 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 95.71 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 83 GFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAY--ISIHNMCAWMidSFGNEEQRHKFCPPLCTMEKFASYCLTE 160
Cdd:PTZ00456 112 GWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYpgLSIGAANTLM--AWGSEEQKEQYLTKLVSGEWSGTMCLTE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 161 PGSGSDAASLLTSAKQQGD-HYILNGSKAFISGGG----ESDIYVVMCRTGES--GAKGISCIVVEKGTP---------- 223
Cdd:PTZ00456 190 PQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDhdltENIVHIVLARLPNSlpTTKGLSLFLVPRHVVkpdgsletak 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 224 GLSFGKKEKKVGWNSQPTRAVIFEDcavPVANRIGTEGQGFLIAMKGLNGGRInvaSCSL-GAAHASVILtQEHLKVRKQ 302
Cdd:PTZ00456 270 NVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARV---GTALeGVCHAELAF-QNALRYARE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 303 FGAPLARSQYLQFQLAdmATKLVAS---RLMIRTA-AVA---------------LQEEREDAVA----------LCSMAK 353
Cdd:PTZ00456 343 RRSMRALSGTKEPEKP--ADRIICHanvRQNILFAkAVAeggrallldvgrlldIHAAAKDAATrealdheigfYTPIAK 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 118403322 354 LFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRM-LISRNLL 411
Cdd:PTZ00456 421 GCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVL 479
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
278-400 |
6.67e-19 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 82.39 E-value: 6.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 278 VASCSLGAAHASVILTQEHL--KVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDA-------VAL 348
Cdd:pfam08028 2 IAAAALGAARAALAEFTERArgRVRAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGkpvtpalRAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 118403322 349 CSMAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNE 400
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
74-411 |
2.20e-12 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 68.83 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 74 DVMRKAaqlGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMC--AWMIDSFGNEEQRHKFCPPLCTME 151
Cdd:PRK13026 115 DYLKKE---GFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLgpGELLTHYGTQEQKDYWLPRLADGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 152 KFASYCLTEPGSGSDAASL-----LTSAKQQGDHYI---LNGSKAFIS--------G------------GGESDIyvvmc 203
Cdd:PRK13026 192 EIPCFALTGPEAGSDAGAIpdtgiVCRGEFEGEEVLglrLTWDKRYITlapvatvlGlafklrdpdgllGDKKEL----- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 204 rtgesgakGISCIVVEKGTPGLSFGKKEKKVGWNSQ--PTRAvifEDCAVPVANRIGTE---GQGFLIAMKGLNGGR-IN 277
Cdd:PRK13026 267 --------GITCALIPTDHPGVEIGRRHNPLGMAFMngTTRG---KDVFIPLDWIIGGPdyaGRGWRMLVECLSAGRgIS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 278 VASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATK---LVASRLMIrTAAVALQEEREDAVAlcsMAKL 354
Cdd:PRK13026 336 LPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNtylLEAARRLT-TTGLDLGVKPSVVTA---IAKY 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 355 FATEECFAICNQALQMHGGYGYL---KDYAVQQYMRdSRVHQILEGSNevmrmLISRNLL 411
Cdd:PRK13026 412 HMTELARDVVNDAMDIHAGKGIQlgpKNYLGHAYMA-VPIAITVEGAN-----ILTRNLM 465
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
134-375 |
2.63e-12 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 68.69 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 134 FGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASL-----LTSAKQQGDHYI---LNGSKAFIS--------G----- 192
Cdd:PRK09463 175 YGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIpdtgvVCKGEWQGEEVLgmrLTWNKRYITlapiatvlGlafkl 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 193 -------GGESDIyvvmcrtgesgakGISCIVVEKGTPGLSFGKKEKKVGWNSQ--PTRAvifEDCAVPVANRIGTE--- 260
Cdd:PRK09463 255 ydpdgllGDKEDL-------------GITCALIPTDTPGVEIGRRHFPLNVPFQngPTRG---KDVFIPLDYIIGGPkma 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 261 GQGFLIAMKGLNGGR-INVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATK---LVASRLMIrTAAV 336
Cdd:PRK09463 319 GQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTLT-TAAV 397
|
250 260 270
....*....|....*....|....*....|....*....
gi 118403322 337 ALQEerEDAVaLCSMAKLFATEECFAICNQALQMHGGYG 375
Cdd:PRK09463 398 DLGE--KPSV-LSAIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
54-391 |
3.11e-11 |
|
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: 64.29 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 54 AAREMAP----NMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAW 129
Cdd:cd01159 2 RAEDLAPlireRAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATHSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 130 MIDSFGNEEQRHKFcpplctmekfasycltepgsGSDAASLLTS-------AKQQGDHYILNGSKAFISGGGESDIYVVM 202
Cdd:cd01159 82 MLAAFPPEAQEEVW--------------------GDGPDTLLAGsyapggrAERVDGGYRVSGTWPFASGCDHADWILVG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 203 CRTGESGAKGISCIVVekgtpglsFGKKEKK-------VGWNSQPTRAVIFEDCAVPVANrigtegqgFLIAMKGLNGGR 275
Cdd:cd01159 142 AIVEDDDGGPLPRAFV--------VPRAEYEivdtwhvVGLRGTGSNTVVVDDVFVPEHR--------TLTAGDMMAGDG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 276 -----------------INVASCSLGAAHASVILTQEHLKVRKQ---FGAPLARSQYLQFQLADMATKLVASR-LMIRTA 334
Cdd:cd01159 206 pggstpvyrmplrqvfpLSFAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARaFLERAT 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118403322 335 AV--ALQEERE----DAVALCSMAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRV 391
Cdd:cd01159 286 RDlwAHALAGGpidvEERARIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHA 348
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
158-402 |
4.37e-10 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 61.31 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 158 LTEPGSGSDAASLLTSA-KQQGDHYILNGSKAFISGGgESDIYVVMCRTgesgAKGISCIVVEKGTP-----GLSFGKKE 231
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAeRLADGSYRLVGHKWFFSVP-QSDAHLVLAQA----KGGLSCFFVPRFLPdgqrnAIRLERLK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 232 KKVGWNSQPTRAVIFEDCavpVANRIGTEGQGF--LIAMKGLNggRINvasCSLGAaHA------SVILTQEHLkvRKQF 303
Cdd:PRK11561 259 DKLGNRSNASSEVEFQDA---IGWLLGEEGEGIrlILKMGGMT--RFD---CALGS-HGlmrrafSVAIYHAHQ--RQVF 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 304 GAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVALcsMAKLFATEECFAICNQ-------ALQMHGGYGY 376
Cdd:PRK11561 328 GKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEAL--WARLFTPAAKFVICKRgipfvaeAMEVLGGIGY 405
|
250 260
....*....|....*....|....*.
gi 118403322 377 LKDYAVQQYMRDSRVHQILEGSNEVM 402
Cdd:PRK11561 406 CEESELPRLYREMPVNSIWEGSGNIM 431
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
50-392 |
1.11e-09 |
|
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: 59.64 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 50 AFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAW 129
Cdd:cd01163 2 RARPLAARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 130 MIDSFGNEEQRhKFCPPLCTMEKFASYCLTEPGSgSDAASLLTSAKQQGDHYILNGSKAFISGGGESDiYVVMCRTGESG 209
Cdd:cd01163 82 ALLLAGPEQFR-KRWFGRVLNGWIFGNAVSERGS-VRPGTFLTATVRDGGGYVLNGKKFYSTGALFSD-WVTVSALDEEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 210 AKGIscIVVEKGTPGLS-------FGKKEKKVGwNSQPTRAVIFEDCAVPVANR------IGTEGQGFLIAmkglnggri 276
Cdd:cd01163 159 KLVF--AAVPTDRPGITvvddwdgFGQRLTASG-TVTFDNVRVEPDEVLPRPNApdrgtlLTAIYQLVLAA--------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 277 NVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQ-YLQFQLADMATKLVASRLMIRTAAVALQ-----------EERED 344
Cdd:cd01163 227 VLAGIARAALDDAVAYVRSRTRPWIHSGAESARDDpYVQQVVGDLAARLHAAEALVLQAARALDaaaaagtaltaEARGE 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 118403322 345 AVALCSMAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVH 392
Cdd:cd01163 307 AALAVAAAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNARTH 354
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
74-411 |
1.53e-08 |
|
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: 56.57 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 74 DVMRKAAQLGF-GGVYVRTDVggsglsrLDTSVIFEALATGCTSTTAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTME 151
Cdd:cd01150 61 ELKRKAKTDVErMGELMADDP-------EKMLALTNSLGGYDLSLGAKLGLHlGLFGNAIKNLGTDEHQDYWLQGANNLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 152 KFASYCLTEPGSGSDAASLLTSAK--QQGDHYILN-----GSKAFISGGGESDIYVV----MCRTGES-GAKG----ISC 215
Cdd:cd01150 134 IIGCFAQTELGHGSNLQGLETTATydPLTQEFVINtpdftATKWWPGNLGKTATHAVvfaqLITPGKNhGLHAfivpIRD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 216 IVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVP---VANRIG-------------TEGQGFLIAMKGLNGGRINVA 279
Cdd:cd01150 214 PKTHQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPrenLLNRFGdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 280 SCSLGAAHASVILTQEHLKVRKQFGAPLARS----------QYLQF-QLA-----DMATKLVASRL--MIRTAAVALQEE 341
Cdd:cd01150 294 YDAAMSLKKAATIAIRYSAVRRQFGPKPSDPevqildyqlqQYRLFpQLAaayafHFAAKSLVEMYheIIKELLQGNSEL 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 342 REDAVALCSMAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLL 411
Cdd:cd01150 374 LAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLL 443
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
86-268 |
2.19e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 43.33 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 86 GVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYClTEPGSG 164
Cdd:PTZ00457 67 GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHsGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEEGCG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118403322 165 SDAASLLTSAKQQGD-HYILNGSKAFISGGGESDiYVVMCRT-----GESGAKGI---SCIVVEKGTPGLSfgkkekkVG 235
Cdd:PTZ00457 146 SDISMNTTKASLTDDgSYVLTGQKRCEFAASATH-FLVLAKTltqtaAEEGATEVsrnSFFICAKDAKGVS-------VN 217
|
170 180 190
....*....|....*....|....*....|...
gi 118403322 236 WNSqptraVIFEDcaVPVANRIGTEGQGFLIAM 268
Cdd:PTZ00457 218 GDS-----VVFEN--TPAADVVGVVGEGFKDAM 243
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
114-183 |
4.35e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 42.52 E-value: 4.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118403322 114 CTSTTAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSA--KQQGDHYIL 183
Cdd:PTZ00460 88 CPQGTFISTVHfAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVI 160
|
|
| |
