|
Name |
Accession |
Description |
Interval |
E-value |
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
5-379 |
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: 678.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 5 LTEEQRLLVESARAFARHELAPKAADWDRDHHFPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQLAAGCVATT 84
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 85 AYISIHNMAAWMLASFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARREGDEYVLDGSKCFISGAGSTQV 164
Cdd:cd01162 81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 165 LIVMARTGEDGARGISCFLVPADAPGIRYGRNEDKMGWRAQPTRTITFEGVRIPAGNRIGPEGQGFVYAMKGLDGGRLNI 244
Cdd:cd01162 161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 245 ASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDRGDAEATLYCAMAKRFATD 324
Cdd:cd01162 241 ASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 15595943 325 RCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVARRLLEQ 379
Cdd:cd01162 321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-381 |
1.60e-166 |
|
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: 470.86 E-value: 1.60e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 1 MDFDLTEEQRLLVESARAFARHELAPKAADWDRDHHFPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQLAAGC 80
Cdd:COG1960 1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 81 VATTAYISIHNMAAWMLASFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARREGDEYVLDGSKCFISGAG 160
Cdd:COG1960 81 ASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 161 STQVLIVMARTGED-GARGISCFLVPADAPGIRYGRNEDKMGWRAQPTRTITFEGVRIPAGNRIGPEGQGFVYAMKGLDG 239
Cdd:COG1960 161 VADVILVLARTDPAaGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 240 GRLNIASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDRGDaEATLYCAMAK 319
Cdd:COG1960 241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE-DAALEAAMAK 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595943 320 RFATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVARRLLEQGG 381
Cdd:COG1960 320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
7-378 |
5.64e-144 |
|
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: 413.20 E-value: 5.64e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 7 EEQRLLVESARAFARHELAPKAADWDRDHHFPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQLAAGCVATTAY 86
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 87 ISIHN-MAAWMLASFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARREGDEYVLDGSKCFISGAGSTQVL 165
Cdd:cd01158 81 VSVHNsLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 166 IVMARTGED-GARGISCFLVPADAPGIRYGRNEDKMGWRAQPTRTITFEGVRIPAGNRIGPEGQGFVYAMKGLDGGRLNI 244
Cdd:cd01158 161 IVFAVTDPSkGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 245 ASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDRGDA---EAtlycAMAKRF 321
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPfikEA----AMAKLF 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15595943 322 ATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVARRLLE 378
Cdd:cd01158 317 ASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
7-374 |
8.37e-122 |
|
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: 355.44 E-value: 8.37e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 7 EEQRLLVESARAFARHELAPKAADWDRDHHFPVEVIRAAAEQgylglyiaeedgglglsrlstslifeqlaagcvattay 86
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLL-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 87 isihnMAAWMLASFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARREGDEYVLDGSKCFISGAGSTQVLI 166
Cdd:cd00567 43 -----LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 167 VMARTGEDGA--RGISCFLVPADAPGIRYGRNEDKMGWRAQPTRTITFEGVRIPAGNRIGPEGQGFVYAMKGLDGGRLNI 244
Cdd:cd00567 118 VLARTDEEGPghRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 245 ASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDRGDAEATLYCAMAKRFATD 324
Cdd:cd00567 198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATE 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15595943 325 RCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVAR 374
Cdd:cd00567 278 AAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
4-376 |
1.65e-105 |
|
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: 315.50 E-value: 1.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 4 DLTEEQRLLVESARAFARHELAPKAADWDRDHHFPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQL--AAGCV 81
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEIsrASGSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 82 ATTaYISIHNMAAWMLASFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARREGDEYVLDGSKCFISGAGS 161
Cdd:cd01156 81 ALS-YGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 162 TQVLIVMARTGED-GARGISCFLVPADAPGIRYGRNEDKMGWRAQPTRTITFEGVRIPAGNRIGPEGQGFVYAMKGLDGG 240
Cdd:cd01156 160 ADTLVVYAKTDPSaGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 241 RLNIASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDRGDAEAtLYCAMAKR 320
Cdd:cd01156 240 RLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDP-KDAAGVIL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15595943 321 FATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVARRL 376
Cdd:cd01156 319 YAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGREL 374
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
7-377 |
1.16e-104 |
|
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: 313.28 E-value: 1.16e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 7 EEQRLLVESARAFARHELAPKAADWDRDHHFPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQLA-AGCVATTa 85
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELArAGGSGPG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 86 yISIHN-MAAWMLASFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARREGDEYVLDGSKCFISGAGSTQV 164
Cdd:cd01160 80 -LSLHTdIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 165 LIVMARTGED--GARGISCFLVPADAPGIRYGRNEDKMGWRAQPTRTITFEGVRIPAGNRIGPEGQGFVYAMKGLDGGRL 242
Cdd:cd01160 159 VIVVARTGGEarGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 243 NIASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDRGDAEATLYCaMAKRFA 322
Cdd:cd01160 239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEAS-MAKYWA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 15595943 323 TDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVARRLL 377
Cdd:cd01160 318 TELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
5-379 |
1.57e-94 |
|
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: 287.56 E-value: 1.57e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 5 LTEEQRLLVESARAFARHELAPKAADWDRDHHFPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQLAAGCVATT 84
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 85 AYISIHNMAAWMLASFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARREGDEYVLDGSKCFISGAGSTQV 164
Cdd:cd01157 81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 165 LIVMARTGED----GARGISCFLVPADAPGIRYGRNEDKMGWRAQPTRTITFEGVRIPAGNRIGPEGQGFVYAMKGLDGG 240
Cdd:cd01157 161 YFLLARSDPDpkcpASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 241 RLNIASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDRGdAEATLYCAMAKR 320
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSG-RRNTYYASIAKA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15595943 321 FATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVARRLLEQ 379
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
1-381 |
1.11e-86 |
|
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: 268.57 E-value: 1.11e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 1 MDFDLTEEQRLLVESARAFARHELAPKAADWDRDHhfPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQL--AA 78
Cdd:cd01161 23 LTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKI--PRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVgmDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 79 G-CVATTAYISIHNMAawmLASFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARL--RTRARREGDEYVLDGSKCF 155
Cdd:cd01161 101 GfSVTLGAHQSIGFKG---ILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIrtTAVLSEDGKHYVLNGSKIW 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 156 ISGAGSTQVLIVMART---GEDGAR--GISCFLVPADAPGIRYGRNEDKMGWRAQPTRTITFEGVRIPAGNRIGPEGQGF 230
Cdd:cd01161 178 ITNGGIADIFTVFAKTevkDATGSVkdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 231 VYAMKGLDGGRLNIASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDRG-DA 309
Cdd:cd01161 258 KVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGlKA 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595943 310 EATLYCAMAKRFATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVARRLLEQGG 381
Cdd:cd01161 338 EYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHAG 409
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
5-374 |
2.40e-73 |
|
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: 233.40 E-value: 2.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 5 LTEEQRLLVESARAFARHELAPKAADWDRDHHFPVEVIRAAAEQGYLGLYIaEEDGGLGLSRLSTSLIFEQLAAGCVATT 84
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATI-KGYGCAGLSSVAYGLIAREVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 85 AYISIH-NMAAWMLASFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARREGDEYVLDGSKCFISGAGSTQ 163
Cdd:cd01151 92 SFMSVQsSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 164 VLIVMARTGEDGarGISCFLVPADAPGIRYGRNEDKMGWRAQPTRTITFEGVRIPAGNRIgPEGQGFVYAMKGLDGGRLN 243
Cdd:cd01151 172 VFVVWARNDETG--KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNARYG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 244 IASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQM-VRLGahRL-DRGDAeATLYCAMAKRF 321
Cdd:cd01151 249 IAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLAcLRVG--RLkDQGKA-TPEQISLLKRN 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15595943 322 ATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVAR 374
Cdd:cd01151 326 NCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGR 378
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
1-379 |
6.04e-73 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 232.31 E-value: 6.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 1 MDFDLTEEQRLLVESARAFARHElAPKA--ADWDRDHHFPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQLAA 78
Cdd:PRK12341 1 MDFSLTEEQELLLASIRELITRN-FPEEyfRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 79 GCVatTAYI-----SIHNMAawmlaSFGDA-ALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARREGDEYVLDGS 152
Cdd:PRK12341 80 CGA--PAFLitngqCIHSMR-----RFGSAeQLRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 153 KCFISGAGSTQVLIVMARTGE--DGARGISCFLVPADAPGIRYGRNEdKMGWRAQPTRTITFEGVRIPAGNRIGPEGQGF 230
Cdd:PRK12341 153 KTFITGAKEYPYMLVLARDPQpkDPKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 231 VYAMKGLDGGRLNIASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDRG--- 307
Cdd:PRK12341 232 LNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGqsl 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595943 308 ---DAEATLYCAMAkrfatdrCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVARRLLEQ 379
Cdd:PRK12341 312 rtsAALAKLYCART-------AMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKD 379
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
3-380 |
1.31e-72 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 232.07 E-value: 1.31e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 3 FDLTEEQrlLVESARAFARHELAPKAADWDRDHHFPVEV--IRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQL--AA 78
Cdd:PLN02519 26 FDDTQLQ--FKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEIsrAS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 79 GCVATTaYISIHNMAAWMLASFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARREGDEYVLDGSKCFISG 158
Cdd:PLN02519 104 GSVGLS-YGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 159 AGSTQVLIVMARTG-EDGARGISCFLVPADAPGIRYGRNEDKMGWRAQPTRTITFEGVRIPAGNRIGPEGQGFVYAMKGL 237
Cdd:PLN02519 183 GPVAQTLVVYAKTDvAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 238 DGGRLNIASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDRGDAEATlYCAM 317
Cdd:PLN02519 263 DLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DCAG 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595943 318 AKRFATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVARRLLEQG 380
Cdd:PLN02519 342 VILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKEE 404
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
14-377 |
1.55e-63 |
|
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: 208.78 E-value: 1.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 14 ESARAFARHELAPKAADWDRD--------HHFPVEV---IRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQLAAGCvA 82
Cdd:cd01153 3 EEVARLAENVLAPLNADGDREgpvfddgrVVVPPPFkeaLDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGD-A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 83 TTAYISIHNMAAWMLASFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARREGD-EYVLDGSKCFISGA-- 159
Cdd:cd01153 82 PLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGeh 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 160 --GSTQVLIVMARTGE--DGARGISCFLVP-----ADAPGIRYGRNEDKMGWRAQPTRTITFEGVRipaGNRIGPEGQGF 230
Cdd:cd01153 162 dmSENIVHLVLARSEGapPGVKGLSLFLVPkflddGERNGVTVARIEEKMGLHGSPTCELVFDNAK---GELIGEEGMGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 231 VYAMKGLDGGRLNIASCSLGAAQAALEQSMRYVEEREQFGKPLATFQAL----------QFKLADMLTE---------LT 291
Cdd:cd01153 239 AQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVtiihhpdvrrSLMTQKAYAEgsraldlytAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 292 ASRQMVRLGAHRLDRGDAEA--TLYCAMAKRFATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMR 369
Cdd:cd01153 319 VQDLAERKATEGEDRKALSAlaDLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQA 398
|
....*...
gi 15595943 370 VIVARRLL 377
Cdd:cd01153 399 LDLIGRKI 406
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
1-379 |
8.56e-58 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 192.74 E-value: 8.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 1 MDFDLTEEQRLLVESARAFARHELAPKA-ADWDRDHHFPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQLaaG 79
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELMASENWEAYfAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 80 CVATTAYISIHNMAAW-MLASFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARREGDEYVLDGSKCFISG 158
Cdd:PRK03354 79 RLGAPTYVLYQLPGGFnTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 159 AGSTQVLIVMARTGEDGARGI-SCFLVPADAPGIRYGRNEdKMGWRAQPTRTITFEGVRIPAGNRIGPEGQGFVYAMKGL 237
Cdd:PRK03354 159 SAYTPYIVVMARDGASPDKPVyTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 238 DGGRLNIASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDRGDAEATlYCAM 317
Cdd:PRK03354 238 DHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSG-DAAM 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595943 318 AKRFATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVARRLLEQ 379
Cdd:PRK03354 317 CKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
22-377 |
1.10e-54 |
|
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: 185.29 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 22 HELAPKAADWDRDHHFPVEVIRAAA-EQGYLGLYIAEEDGGLGLSRLSTSLIFEQLAAGCVATTAYisihNMAA------ 94
Cdd:cd01155 26 LEYYAEGGDRWWTPPPIIEKLKAKAkAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRSFFAPEVF----NCQApdtgnm 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 95 WMLASFGDAALKEAWLPGLIGGESLASYCLTEPD-AGSDAARLRTRARREGDEYVLDGSKCFISGAGS--TQVLIVMART 171
Cdd:cd01155 102 EVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGDprCKIAIVMGRT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 172 GEDGA---RGISCFLVPADAPGIRYGRNEDKMGWRAQPT--RTITFEGVRIPAGNRIGPEGQGFVYAMKGLDGGRLNIAS 246
Cdd:cd01155 182 DPDGAprhRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 247 CSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDR-GDAEATLYCAMAKRFATDR 325
Cdd:cd01155 262 RLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTvGNKAARKEIAMIKVAAPRM 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15595943 326 CFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVARRLL 377
Cdd:cd01155 342 ALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMEL 393
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
3-378 |
3.99e-52 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 178.98 E-value: 3.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 3 FDLTEEQRLLVESARAFARHELAPKAADWDRDHHFPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQLA----A 78
Cdd:PTZ00461 35 YNPTPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSkydpG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 79 GCVATTAYISIHNMAAWMLASfgdAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARREGDE-YVLDGSKCFIS 157
Cdd:PTZ00461 115 FCLAYLAHSMLFVNNFYYSAS---PAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGnYVLNGSKIWIT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 158 GAGSTQVLIVMARTgeDGArgISCFLVPADAPGIRYGRNEDKMGWRAQPTRTITFEGVRIPAGNRIGPEGQGFVYAMKGL 237
Cdd:PTZ00461 192 NGTVADVFLIYAKV--DGK--ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 238 DGGRLNIASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDRGDAEaTLYCAM 317
Cdd:PTZ00461 268 ELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKN-RLGSDA 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595943 318 AKRFATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVARRLLE 378
Cdd:PTZ00461 347 AKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLK 407
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
227-376 |
3.55e-50 |
|
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: 165.51 E-value: 3.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 227 GQGFVYAMKGLDGGRLNIASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDR 306
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 307 GDaEATLYCAMAKRFATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVARRL 376
Cdd:pfam00441 81 GG-PDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
6-117 |
1.30e-41 |
|
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: 141.83 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 6 TEEQRLLVESARAFARHELAPKAADWDRDHHFPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQLAAGCVATTA 85
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 15595943 86 YISIHN-MAAWMLASFGDAALKEAWLPGLIGGE 117
Cdd:pfam02771 81 ALSVHSsLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
6-377 |
5.73e-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: 5.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 6 TEEQRLLVESARAFARH----ELAPKAADWDRDHHFPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQLAAGCV 81
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHlppeLREESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 82 ATTAYISIHNMAAWMLASFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARREGDEYVLDGSKCFISGAGS 161
Cdd:cd01152 81 PVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 162 TQVLIVMARTGEDGA--RGISCFLVPADAPGIRygrnedkmgWRaqPTRTIT---------FEGVRIPAGNRIGPEGQGF 230
Cdd:cd01152 161 ADWAWLLVRTDPEAPkhRGISILLVDMDSPGVT---------VR--PIRSINggeffnevfLDDVRVPDANRVGEVNDGW 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 231 VYAMKGLDGGRLNIAscslGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDRG--- 307
Cdd:cd01152 230 KVAMTTLNFERVSIG----GSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGkpp 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595943 308 DAEAtlycAMAKRFATDRCFDVCNEALQLHGGYGYLNDYPLE-----RWVRD---TRVHQILEGTNEIMRVIVARRLL 377
Cdd:cd01152 306 GAEA----SIAKLFGSELAQELAELALELLGTAALLRDPAPGaelagRWEADylrSRATTIYGGTSEIQRNIIAERLL 379
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
87-376 |
1.22e-38 |
|
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: 143.28 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 87 ISIHNMAAWMLASFGDAALKEaWLPGLIGGES----LASYCLTEPDAGSD-AARLRTRARREGDEYVLDGSKCFISGAGS 161
Cdd:cd01154 113 LTMTDAAVYALRKYGPEELKQ-YLPGLLSDRYktglLGGTWMTEKQGGSDlGANETTAERSGGGVYRLNGHKWFASAPLA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 162 tQVLIVMART--GEDGARGISCFLVPADAP-----GIRYGRNEDKMGWRAQPTRTITFEGVripAGNRIGPEGQGFVYAM 234
Cdd:cd01154 192 -DAALVLARPegAPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYIL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 235 KGLDGGRLNIASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDRGDAE---- 310
Cdd:cd01154 268 EMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADkpve 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595943 311 ---ATLYCAMAKRFATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVARRL 376
Cdd:cd01154 348 ahmARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVL 416
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
5-376 |
1.42e-35 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 134.59 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 5 LTEEQRLLVESARAFARHELAPKAADWDRDHHFPVEVIRAAAEQGYLGLYIaEEDGGLGLSRLSTSLIFEQLAAGCVATT 84
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVARVDASCS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 85 AYISIHN-MAAWMLASFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARREGDEYVLDGSKCFISGAGSTQ 163
Cdd:PLN02526 108 TFILVHSsLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 164 VLIVMARTGEdgARGISCFLVPADAPGIRYGRNEDKMGWRAQPTRTITFEGVRIPAGNRIgPEGQGFVYAMKGLDGGRLN 243
Cdd:PLN02526 188 VLVIFARNTT--TNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL-PGVNSFQDTNKVLAVSRVM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 244 IASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTAsrqMVRLGaHRLDRGDAEATL---YCAMAKR 320
Cdd:PLN02526 265 VAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQA---MFLVG-WRLCKLYESGKMtpgHASLGKA 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15595943 321 FATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRVIVARRL 376
Cdd:PLN02526 341 WITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
91-367 |
1.53e-27 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 114.51 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 91 NMAawMLASFGDAALKEAWLPGLIGGESLASYCLTEPD-AGSDAARLRTRARREGDEYVLDGSKCFISGA--GSTQVLIV 167
Cdd:PLN02876 525 NME--VLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIV 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 168 MARTGEDGA--RGISCFLVPADAPGIRYGRNEDKMGWRAQPT--RTITFEGVRIPAGNRIGPEGQGFVYAMKGLDGGRLN 243
Cdd:PLN02876 603 MGKTDFNAPkhKQQSMILVDIQTPGVQIKRPLLVFGFDDAPHghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLH 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 244 IASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDR-GDAEATLYCAMAKRFA 322
Cdd:PLN02876 683 HCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRlGNKKARGIIAMAKVAA 762
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15595943 323 TDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEI 367
Cdd:PLN02876 763 PNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
121-213 |
3.19e-25 |
|
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: 98.12 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 121 SYCLTEPDAGSDAARLR-TRARREGDEYVLDGSKCFISGAGSTQVLIVMARTG-EDGARGISCFLVPADAPGIRYGRNED 198
Cdd:pfam02770 1 AFALTEPGAGSDVASLKtTAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGgDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 15595943 199 KMGWRAQPTRTITFE 213
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
30-341 |
1.84e-24 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 105.42 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 30 DWD---RDHHFPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQLAAGCVATTAYISIHNM--AAWMLASFGDAA 104
Cdd:PRK13026 99 DWDivqNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSlgPGELLTHYGTQE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 105 LKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTR-----ARREGDEYV---LDGSKCFISGAGSTQVLIVMART----- 171
Cdd:PRK13026 179 QKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTgivcrGEFEGEEVLglrLTWDKRYITLAPVATVLGLAFKLrdpdg 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 172 --GEDGARGISCFLVPADAPGIRYGRNEDKMGWRAQ--PTRTitfEGVRIPAGNRI-GPE--GQGFVYAMKGLDGGRlNI 244
Cdd:PRK13026 259 llGDKKELGITCALIPTDHPGVEIGRRHNPLGMAFMngTTRG---KDVFIPLDWIIgGPDyaGRGWRMLVECLSAGR-GI 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 245 ASCSLGAAQAALEQSMR--YVEEREQFGKPLATFQALQFKLADM--LT-ELTASRQMVRLGahrLDRGdAEATLYCAMAK 319
Cdd:PRK13026 335 SLPALGTASGHMATRTTgaYAYVRRQFGMPIGQFEGVQEALARIagNTyLLEAARRLTTTG---LDLG-VKPSVVTAIAK 410
|
330 340
....*....|....*....|..
gi 15595943 320 RFATDRCFDVCNEALQLHGGYG 341
Cdd:PRK13026 411 YHMTELARDVVNDAMDIHAGKG 432
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
40-381 |
8.10e-23 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 100.33 E-value: 8.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 40 EVIRAAAEQGYLGLYIAEEDGGLGLSrLSTSLIF-EQLAAGCVATTAYISIHNMAAWMLASFGDAALKEAWLPGLIGGES 118
Cdd:PTZ00456 103 EAYQALKAGGWTGISEPEEYGGQALP-LSVGFITrELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEW 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 119 LASYCLTEPDAGSDAARLRTRARREGD-EYVLDGSKCFISgAGSTQ-----VLIVMART--GEDGARGISCFLVPADAP- 189
Cdd:PTZ00456 182 SGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFIS-AGDHDlteniVHIVLARLpnSLPTTKGLSLFLVPRHVVk 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 190 ---GIRYGRN------EDKMGWRAQPTRTITFEGvriPAGNRIGPEGQGFVYAMKGLDGGRLNIASCSLGAAQAALEQSM 260
Cdd:PTZ00456 261 pdgSLETAKNvkciglEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNAL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 261 RYVEEREQFGKPLATFQALqfKLADMLTELTASRQMV------------------RLGAHRLDRGDAEAT--------LY 314
Cdd:PTZ00456 338 RYARERRSMRALSGTKEPE--KPADRIICHANVRQNIlfakavaeggrallldvgRLLDIHAAAKDAATRealdheigFY 415
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595943 315 CAMAKRFATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEIMRV-IVARRLLE-QGG 381
Cdd:PTZ00456 416 TPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVLSlKGG 484
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
7-341 |
1.27e-20 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 93.73 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 7 EEQRLL---VEsarafarhELAPKAADWD---RDHHFPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQLAAGC 80
Cdd:PRK09463 82 EEQAFLdgpVE--------ELCRMVNDWQithELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRS 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 81 VATTAYISIHNM--AAWMLASFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTR-----ARREGDEYV---LD 150
Cdd:PRK09463 154 GTLAVTVMVPNSlgPGELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTgvvckGEWQGEEVLgmrLT 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 151 GSKCFISGAGSTQVLIVMART-------GEDGARGISCFLVPADAPGIRYGRNEDKMGWRAQ--PTRTitfEGVRIPAGN 221
Cdd:PRK09463 234 WNKRYITLAPIATVLGLAFKLydpdgllGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQngPTRG---KDVFIPLDY 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 222 RIG-PE--GQGFVYAMKGLDGGR-LNIASCSLGAAQAALEQSMRYVEEREQFGKPLATFQALQFKLADMLTELTASRQMV 297
Cdd:PRK09463 311 IIGgPKmaGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAAR 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15595943 298 RLGAHRLDRGDAEATLyCAMAKRFATDRCFDVCNEALQLHGGYG 341
Cdd:PRK09463 391 TLTTAAVDLGEKPSVL-SAIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
14-357 |
2.12e-19 |
|
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: 88.56 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 14 ESARAFARhELAPKAADWDRDHHFPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQLAAGCVATTAYISIHNMA 93
Cdd:cd01159 1 ARAEDLAP-LIRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 94 AWMLASFGDAALKEAWLPG---LIGGeSLASYCLTEPDAGSdaarlrtrarregdeYVLDGSKCFISGAGSTQVLIVMAR 170
Cdd:cd01159 80 SRMLAAFPPEAQEEVWGDGpdtLLAG-SYAPGGRAERVDGG---------------YRVSGTWPFASGCDHADWILVGAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 171 TGEDGARGISC-FLVPADAPGIRygRNEDKMGWRAQPTRTITFEGVRIPAGNRI---------GPEGQGFVYAMKGLDGG 240
Cdd:cd01159 144 VEDDDGGPLPRaFVVPRAEYEIV--DTWHVVGLRGTGSNTVVVDDVFVPEHRTLtagdmmagdGPGGSTPVYRMPLRQVF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 241 RLNIASCSLGAAQAALEQSMRYVEEREQ---FGKPLATFQALQFKLADMLTELTAS-----RQMVRLGAHRLDRG--DAE 310
Cdd:cd01159 222 PLSFAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAArafleRATRDLWAHALAGGpiDVE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15595943 311 ATLYCAMAKRFATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRV 357
Cdd:cd01159 302 ERARIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHA 348
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
244-366 |
1.90e-16 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 75.07 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 244 IASCSLGAAQAALEQSMRYVEEREQ--FGKPLATFQALQFKLADMLTELTASRQMVRLGAHRLDRGDAEATLYC------ 315
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKPVTpalrae 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15595943 316 -AMAKRFATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNE 366
Cdd:pfam08028 82 aRRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
124-386 |
9.21e-15 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 75.56 E-value: 9.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 124 LTEPDAGSDAAR-LRTRARREGDEYVLDGSKCFISGAGSTQVLIVMARTGedgarGISCFLVPADAP-----GIRYGRNE 197
Cdd:PRK11561 184 MTEKQGGSDVLSnTTRAERLADGSYRLVGHKWFFSVPQSDAHLVLAQAKG-----GLSCFFVPRFLPdgqrnAIRLERLK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 198 DKMGWRAQPTRTITFEGVripAGNRIGPEGQGFVYAMKGLDGGRLNIASCSLGAAQAALEQSMRYVEEREQFGKPLATFQ 277
Cdd:PRK11561 259 DKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQP 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 278 ALQFKLADMLTELTASRQMV-RLGAHRLDRGDAEATLYcamAKRFATDRCFDVCN-------EALQLHGGYGYLNDYPLE 349
Cdd:PRK11561 336 LMRQVLSRMALQLEGQTALLfRLARAWDRRADAKEALW---ARLFTPAAKFVICKrgipfvaEAMEVLGGIGYCEESELP 412
|
250 260 270
....*....|....*....|....*....|....*..
gi 15595943 350 RWVRDTRVHQILEGTNEIMRVIVARRLLEQGGMLDRL 386
Cdd:PRK11561 413 RLYREMPVNSIWEGSGNIMCLDVLRVLNKQPGVYDLL 449
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
16-358 |
4.77e-12 |
|
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: 66.58 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 16 ARAFARhELAPKAADWDRDHHFPVEVIRAAAEQGYLGLYIAEEDGGLGLSRLSTSLIFEQLAAGCVATTAYISIHNMAAW 95
Cdd:cd01163 3 ARPLAA-RIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 96 MLASFGDAALKEAWLPGLIGGEsLASYCLTEPDaGSDAARLRTRARREGDEYVLDGSKCFISGAGSTQVLIVMARTGEDG 175
Cdd:cd01163 82 ALLLAGPEQFRKRWFGRVLNGW-IFGNAVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 176 ARGiscFLVPADAPGIRYGRNEDKMGWRAQPTRTITFEGVRIPAGNrIGPEGQGFVYAMKGLDGGRLNIASCSLGAAQAA 255
Cdd:cd01163 160 LVF---AAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDE-VLPRPNAPDRGTLLTAIYQLVLAAVLAGIARAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 256 LEQSMRYVEEREQ-FGKPLAT-----FQALQfKLADMLTELTASRQMVRLGAHRLDRGDA-----------EATLYCAMA 318
Cdd:cd01163 236 LDDAVAYVRSRTRpWIHSGAEsarddPYVQQ-VVGDLAARLHAAEALVLQAARALDAAAAagtaltaeargEAALAVAAA 314
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15595943 319 KRFATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVH 358
Cdd:cd01163 315 KVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNARTH 354
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
52-292 |
5.18e-11 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 64.13 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 52 GLYIAEEDGGLGLSRLSTSLIFEQLAAGCVATTAYISIH-NMAAWMLASFGDAALKEAWLPGLIGGESLASYClTEPDAG 130
Cdd:PTZ00457 67 GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHsGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEEGCG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 131 SDAARLRTRARREGD-EYVLDGSKCFISGAGSTQVLI----VMARTGEDGARGI---SCFLVPADAPGIRYGRNedkmgw 202
Cdd:PTZ00457 146 SDISMNTTKASLTDDgSYVLTGQKRCEFAASATHFLVlaktLTQTAAEEGATEVsrnSFFICAKDAKGVSVNGD------ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 203 raqptrTITFEGVriPAGNRIGPEGQGFVYAMKGLDGGRLNIASCSLGAAQAALeQSMRYVEEREQFGKPLATFQALQFK 282
Cdd:PTZ00457 220 ------SVVFENT--PAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVV-QELRGSNAEEGATDTVASFACAMYA 290
|
250
....*....|
gi 15595943 283 LADMLTELTA 292
Cdd:PTZ00457 291 MESTLYALTA 300
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
99-379 |
3.31e-10 |
|
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: 61.58 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 99 SFGDAALKEAWLPGLIGGESLASYCLTEPDAGSDAARLRTRARRE--GDEYVLD-----GSKCFISGAGST-QVLIVMAR 170
Cdd:cd01150 115 NLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDplTQEFVINtpdftATKWWPGNLGKTaTHAVVFAQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 171 TGEDGAR-GISCFLVPA-DA------PGIRYGRNEDKMGWRAQPTRTITFEGVRIPAGN------RIGPEG--------- 227
Cdd:cd01150 195 LITPGKNhGLHAFIVPIrDPkthqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENllnrfgDVSPDGtyvspfkdp 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 228 -QGFVYAMKGLDGGRLNIASCSLGAAQAALEQSMRYVEEREQFGKPLAT-------FQALQFKLADMLTEL----TASRQ 295
Cdd:cd01150 275 nKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKPSDpevqildYQLQQYRLFPQLAAAyafhFAAKS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 296 MVRL---GAHRLDRGDAEA-----TLYCAMaKRFATDRCFDVCNEALQLHGGYGYLNDYPLERWVRDTRVHQILEGTNEI 367
Cdd:cd01150 355 LVEMyheIIKELLQGNSELlaelhALSAGL-KAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTV 433
|
330
....*....|..
gi 15595943 368 MRVIVARRLLEQ 379
Cdd:cd01150 434 LLQQTANYLLKK 445
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
178-379 |
1.57e-06 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 50.24 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 178 GISCFLVPADA-------PGIRYGRNEDKMGWRAQPTRTITFEGVRIPAGN---RIG---PEG----------QGFVYAM 234
Cdd:PLN02636 248 GVHAFIVPIRDmkthqvlPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNllnRFGdvsRDGkytsslptinKRFAATL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 235 KGLDGGRLNIASCSLGAAQAALEQSMRYVEEREQFGKP------LATFQALQFKLADMLT-------------------E 289
Cdd:PLN02636 328 GELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQHKLMPMLAstyafhfateylverysemK 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595943 290 LTASRQMVRlGAHRLDRG-DAEATLYCAMAkrfatdrcFDVCNEALQLHgGYGYLNDYPLERwvRDTRVHQILEGTNEIM 368
Cdd:PLN02636 408 KTHDDQLVA-DVHALSAGlKAYITSYTAKA--------LSTCREACGGH-GYAAVNRFGSLR--NDHDIFQTFEGDNTVL 475
|
250
....*....|.
gi 15595943 369 RVIVARRLLEQ 379
Cdd:PLN02636 476 LQQVAADLLKQ 486
|
|
| |
