|
Name |
Accession |
Description |
Interval |
E-value |
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
5-377 |
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: 538.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 5 LTEEQRAFAKSAHDFARAEFAPHAAQWDEQAIFPRAAIAKAGALGFCGLYACEAAGGLALPRLDATLVFEELAAIDPSTT 84
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 85 AFISIHNMATWMLGRWATPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRAERVGSDYVINGSKAFISGAGSTDM 164
Cdd:cd01162 81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 165 LVLMARTGAAGAGGISAFAVPADTPGISYGKKERKLGWNSQPTRSIGLEQLRIPAEHLLGRVGEGFKIAMQGLDGGRINI 244
Cdd:cd01162 161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 245 ASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDTGAPDASTYCAMAKRFATD 324
Cdd:cd01162 241 ASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 500135244 325 IGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIARRIL 377
Cdd:cd01162 321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALL 373
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-380 |
8.87e-144 |
|
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: 413.08 E-value: 8.87e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 1 MDFELTEEQRAFAKSAHDFARAEFAPHAAQWDEQAIFPRAAIAKAGALGFCGLYACEAAGGLALPRLDATLVFEELAAID 80
Cdd:COG1960 1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 81 PSTTAFISIHNMATWMLGRWATPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRAERVGSDYVINGSKAFISGAG 160
Cdd:COG1960 81 ASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 161 STDMLVLMARTGAAGAGGISAF-AVPADTPGISYGKKERKLGWNSQPTRSIGLEQLRIPAEHLLGRVGEGFKIAMQGLDG 239
Cdd:COG1960 161 VADVILVLARTDPAAGHRGISLfLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 240 GRINIASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDTGApDASTYCAMAK 319
Cdd:COG1960 241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE-DAALEAAMAK 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500135244 320 RFATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIARRILDGA 380
Cdd:COG1960 320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRP 380
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
7-378 |
5.43e-128 |
|
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: 372.76 E-value: 5.43e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 7 EEQRAFAKSAHDFARAEFAPHAAQWDEQAIFPRAAIAKAGALGFCGLYACEAAGGLALPRLDATLVFEELAAIDPSTTAF 86
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 87 ISIHN-MATWMLGRWATPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRAERVGSDYVINGSKAFISGAGSTDML 165
Cdd:cd01158 81 VSVHNsLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 166 VLMARTGAAGAGGISAF-AVPADTPGISYGKKERKLGWNSQPTRSIGLEQLRIPAEHLLGRVGEGFKIAMQGLDGGRINI 244
Cdd:cd01158 161 IVFAVTDPSKGYRGITAfIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 245 ASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDTGAP---DAstycAMAKRF 321
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPfikEA----AMAKLF 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 500135244 322 ATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIARRILD 378
Cdd:cd01158 317 ASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
7-374 |
1.34e-104 |
|
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: 311.53 E-value: 1.34e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 7 EEQRAFAKSAHDFARAEFAPHAAQWDEQAIFPRAAIAKAGALgfcglyaceaagglalprldatlvfeelaaidpsttaf 86
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLL-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 87 isihnMATWMLGRWATPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRAERVGSDYVINGSKAFISGAGSTDMLV 166
Cdd:cd00567 43 -----LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 167 LMARTGAAGAGGISAFA--VPADTPGISYGKKERKLGWNSQPTRSIGLEQLRIPAEHLLGRVGEGFKIAMQGLDGGRINI 244
Cdd:cd00567 118 VLARTDEEGPGHRGISAflVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 245 ASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDTGAPDASTYCAMAKRFATD 324
Cdd:cd00567 198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATE 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 500135244 325 IGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIAR 374
Cdd:cd00567 278 AAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
7-377 |
4.50e-94 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 286.32 E-value: 4.50e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 7 EEQRAFAKSAHDFARAEFAPHAAQWDEQAIFPRAAIAKAGALGFCGLYACEAAGGLALPRLDATLVFEELAAIDPSTTAF 86
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 87 ISIHNMATWMLGRWATPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRAERVGSDYVINGSKAFISGAGSTDMLV 166
Cdd:cd01160 81 SLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 167 LMARTGAAGAGGISAFA--VPADTPGISYGKKERKLGWNSQPTRSIGLEQLRIPAEHLLGRVGEGFKIAMQGLDGGRINI 244
Cdd:cd01160 161 VVARTGGEARGAGGISLflVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 245 ASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDTGAPDASTYCaMAKRFATD 324
Cdd:cd01160 241 AAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEAS-MAKYWATE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 500135244 325 IGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIARRIL 377
Cdd:cd01160 320 LQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
5-376 |
1.45e-84 |
|
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: 261.96 E-value: 1.45e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 5 LTEEQRAFAKSAHDFARAEFAPHAAQWDEQAIFPRAAIAKAGALGFCGLYACEAAGGLALPRLDATLVFEELAAIDPSTT 84
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 85 AFISIH-NMATWMLGRWATPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRAERVGSDYVINGSKAFISGAGSTD 163
Cdd:cd01156 82 LSYGAHsNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 164 MLVLMARTGAAGAGGISAF-AVPADTPGISYGKKERKLGWNSQPTRSIGLEQLRIPAEHLLGRVGEGFKIAMQGLDGGRI 242
Cdd:cd01156 162 TLVVYAKTDPSAGAHGITAfIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 243 NIASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDTGAPDASTyCAMAKRFA 322
Cdd:cd01156 242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKD-AAGVILYA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 500135244 323 TDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIARRI 376
Cdd:cd01156 321 AEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGREL 374
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
5-378 |
1.96e-79 |
|
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: 249.04 E-value: 1.96e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 5 LTEEQRAFAKSAHDFARAEFAPHAAQWDEQAIFPRAAIAKAGALGFCGLYACEAAGGLALPRLDATLVFEELA------- 77
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAygctgvq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 78 -AIDPSTTAFISI-----HNMATWMLGRwatpavrdhwgplLTRGEKLASYCLTEPGAGSDAAALTTRAERVGSDYVING 151
Cdd:cd01157 81 tAIEANSLGQMPViisgnDEQKKKYLGR-------------MTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIING 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 152 SKAFISGAGSTDMLVLMART----GAAGAGGISAFAVPADTPGISYGKKERKLGWNSQPTRSIGLEQLRIPAEHLLGRVG 227
Cdd:cd01157 148 QKMWITNGGKANWYFLLARSdpdpKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 228 EGFKIAMQGLDGGRINIASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDTG 307
Cdd:cd01157 228 AGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSG 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500135244 308 APDaSTYCAMAKRFATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIARRILD 378
Cdd:cd01157 308 RRN-TYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
1-380 |
1.50e-78 |
|
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: 247.38 E-value: 1.50e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 1 MDFELTEEQRAFAKSAHDFARAEFAPhaAQWDEQAIFPRAAIAKAGALGFCGLYACEAAGGLALPRLDATLVFEELAAiD 80
Cdd:cd01161 23 LTEEQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGM-D 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 81 PSTTAFISIHNmATWMLG--RWATPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRAER--VGSDYVINGSKAFI 156
Cdd:cd01161 100 LGFSVTLGAHQ-SIGFKGilLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 157 SGAGSTDMLVLMARTGAAGAGGISAFAVPA-----DTPGISYGKKERKLGWNSQPTRSIGLEQLRIPAEHLLGRVGEGFK 231
Cdd:cd01161 179 TNGGIADIFTVFAKTEVKDATGSVKDKITAfiverSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 232 IAMQGLDGGRINIASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDTGA-PD 310
Cdd:cd01161 259 VAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLkAE 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 311 ASTYCAMAKRFATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIARRILDGA 380
Cdd:cd01161 339 YQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHA 408
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
5-376 |
2.46e-58 |
|
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: 194.50 E-value: 2.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 5 LTEEQRAFAKSAHDFARAEFAPHAAQWDEQAIFPRAAIAKAGALGFCGLyACEAAGGLALPRLDATLVFEELAAIDPSTT 84
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 85 AFISIH-NMATWMLGRWATPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRAERVGSDYVINGSKAFISGAGSTD 163
Cdd:cd01151 92 SFMSVQsSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 164 MLVLMARTGAAGAGGISAfaVPADTPGISYGKKERKLGWNSQPTRSIGLEQLRIPAEHLLGRVgEGFKIAMQGLDGGRIN 243
Cdd:cd01151 172 VFVVWARNDETGKIRGFI--LERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA-EGLRGPFKCLNNARYG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 244 IASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQM-VRLAASKlDTG--APDASTycaMAKR 320
Cdd:cd01151 249 IAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLAcLRVGRLK-DQGkaTPEQIS---LLKR 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 500135244 321 FATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIARRI 376
Cdd:cd01151 325 NNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAI 380
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
2-376 |
8.46e-58 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 193.55 E-value: 8.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 2 DFELTEEQRAFAKSAHDFARAEFAPHAAQWDEQAIFPRAA--IAKAGALGFCGLYACEAAGGLALPRLDATLVFEELAAI 79
Cdd:PLN02519 23 SLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 80 DPSTTAFISIH-NMATWMLGRWATPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRAERVGSDYVINGSKAFISG 158
Cdd:PLN02519 103 SGSVGLSYGAHsNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 159 AGSTDMLVLMARTGAAGAGGISAF-AVPADTPGISYGKKERKLGWNSQPTRSIGLEQLRIPAEHLLGRVGEGFKIAMQGL 237
Cdd:PLN02519 183 GPVAQTLVVYAKTDVAAGSKGITAfIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 238 DGGRINIASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDTGAPDASTyCAM 317
Cdd:PLN02519 263 DLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKD-CAG 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 500135244 318 AKRFATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIARRI 376
Cdd:PLN02519 342 VILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
1-377 |
1.95e-56 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 189.17 E-value: 1.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 1 MDFELTEEQRAFAKSAHDFARAEFaPHA--AQWDEQAIFPRAaIAKAGA-LGFCGLYACEAAGGLALPRLDATLVFEELA 77
Cdd:PRK12341 1 MDFSLTEEQELLLASIRELITRNF-PEEyfRTCDENGTYPRE-FMRALAdNGISMLGVPEEFGGTPADYVTQMLVLEEVS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 78 ---AIDPSTTAFISIHNMAtwmlgRWATP-AVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRAERVGSDYVINGSK 153
Cdd:PRK12341 79 kcgAPAFLITNGQCIHSMR-----RFGSAeQLRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 154 AFISGAGSTD-MLVLMARTGAAGAGGISAF-AVPADTPGISYGKKErKLGWNSQPTRSIGLEQLRIPAEHLLGRVGEGFK 231
Cdd:PRK12341 154 TFITGAKEYPyMLVLARDPQPKDPKKAFTLwWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 232 IAMQGLDGGRINIASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDTGAPdA 311
Cdd:PRK12341 233 NVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQS-L 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500135244 312 STYCAMAKRFATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIARRIL 377
Cdd:PRK12341 312 RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQIL 377
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
1-377 |
2.44e-49 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 170.78 E-value: 2.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 1 MDFELTEEQRAFAKSAHDFARAE-FAPHAAQWDEQAIFPRAAIAKAGALGFCGLYACEAAGGLALPRLDATLVFEELAAI 79
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELMASEnWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 80 DPSTTAFISIHNMATWMLgRWATPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRAERVGSDYVINGSKAFISGA 159
Cdd:PRK03354 81 GAPTYVLYQLPGGFNTFL-REGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 160 GSTDMLVLMARTGAAGAGGISAF-AVPADTPGISYGKKErKLGWNSQPTRSIGLEQLRIPAEHLLGRVGEGFKIAMQGLD 238
Cdd:PRK03354 160 AYTPYIVVMARDGASPDKPVYTEwFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 239 GGRINIASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDTGAPDaSTYCAMA 318
Cdd:PRK03354 239 HERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT-SGDAAMC 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 500135244 319 KRFATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIARRIL 377
Cdd:PRK03354 318 KYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVL 376
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
227-376 |
5.27e-46 |
|
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: 154.72 E-value: 5.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 227 GEGFKIAMQGLDGGRINIASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDT 306
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 307 GAPDaSTYCAMAKRFATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIARRI 376
Cdd:pfam00441 81 GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
3-379 |
1.36e-42 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 153.55 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 3 FELTEEQRAFAKSAHDFARAEFAPHAAQWDEQAIFPRAAIAKAGALGFCGLYACEAAGGLALPRLDATLVFEELAAIDPS 82
Cdd:PTZ00461 35 YNPTPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 83 TTAFISIHNMA-TWMLGRWATPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRAERVGS-DYVINGSKAFISGAG 160
Cdd:PTZ00461 115 FCLAYLAHSMLfVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 161 STDMLVLMARTGAAGAGGIsafaVPADTPGISYGKKERKLGWNSQPTRSIGLEQLRIPAEHLLGRVGEGFKIAMQGLDGG 240
Cdd:PTZ00461 195 VADVFLIYAKVDGKITAFV----VERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 241 RINIASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDTGAPDASTYCAmAKR 320
Cdd:PTZ00461 271 RVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDA-AKL 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 500135244 321 FATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIARRILDG 379
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKG 408
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
18-377 |
3.42e-40 |
|
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: 147.15 E-value: 3.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 18 DFARAEFAPHAAQWDEQ------------AIFPRAAIAKAGAlGFCGLYACEAAGGLALPRLDATLVFEE-LAAIDPSTT 84
Cdd:cd01153 7 RLAENVLAPLNADGDREgpvfddgrvvvpPPFKEALDAFAEA-GWMALGVPEEYGGQGLPITVYSALAEIfSRGDAPLMY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 85 AFISIHNMATwmLGRWATPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRAE-RVGSDYVINGSKAFISgAGSTD 163
Cdd:cd01153 86 ASGTQGAAAT--LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVyQADGSWRINGVKRFIS-AGEHD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 164 M------LVLmartgaagaggISAFAVPADTPGISY-----------------GKKERKLGWNSQPTRSIGLEQLRIPae 220
Cdd:cd01153 163 MsenivhLVL-----------ARSEGAPPGVKGLSLflvpkflddgerngvtvARIEEKMGLHGSPTCELVFDNAKGE-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 221 hLLGRVGEGFKIAMQGLDGGRINIASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQF--------KLADMATELVA 292
Cdd:cd01153 230 -LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVTIihhpdvrrSLMTQKAYAEG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 293 ARQMVRLAASKLDTGAPDAST-------------YCAMAKRFATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQ 359
Cdd:cd01153 309 SRALDLYTATVQDLAERKATEgedrkalsaladlLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITT 388
|
410
....*....|....*...
gi 500135244 360 ILEGSNEIMRLIIARRIL 377
Cdd:cd01153 389 IYEGTTGIQALDLIGRKI 406
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
43-377 |
4.18e-37 |
|
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: 138.29 E-value: 4.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 43 AKAGALGFCGLYACEAAGGLALPRLDATLVFEELA----AIDPSTTAFISIHNMAtwMLGRWATPAVRDHW-GPLLtRGE 117
Cdd:cd01155 48 AKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGrsffAPEVFNCQAPDTGNME--VLHRYGSEEQKKQWlEPLL-DGK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 118 KLASYCLTEPG-AGSDAAALTTRAERVGSDYVINGSKAFISGAGSTD--MLVLMARTGAAGAGGISAFA---VPADTPGI 191
Cdd:cd01155 125 IRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGDPRckIAIVMGRTDPDGAPRHRQQSmilVPMDTPGV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 192 sygKKERKL---GWNSQPT--RSIGLEQLRIPAEHLLGRVGEGFKIAMQGLDGGRINIASCSVGAAQGALQAARQYMQQR 266
Cdd:cd01155 205 ---TIIRPLsvfGYDDAPHghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 267 RQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDT-GAPDASTYCAMAKRFATDIGFAVCNEALQLHGGYGYIRE 345
Cdd:cd01155 282 EAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTvGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQD 361
|
330 340 350
....*....|....*....|....*....|..
gi 500135244 346 YPIERLLRDTRVHQILEGSNEIMRLIIARRIL 377
Cdd:cd01155 362 TPLANMYAWARTLRIADGPDEVHLRSIARMEL 393
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
6-117 |
6.70e-35 |
|
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: 124.50 E-value: 6.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 6 TEEQRAFAKSAHDFARAEFAPHAAQWDEQAIFPRAAIAKAGALGFCGLYACEAAGGLALPRLDATLVFEELAAIDPSTTA 85
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 500135244 86 FISIHN-MATWMLGRWATPAVRDHWGPLLTRGE 117
Cdd:pfam02771 81 ALSVHSsLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
4-378 |
2.18e-33 |
|
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: 127.85 E-value: 2.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 4 ELTEEQRAF-AKSAHDFARAEFAPHAAQWDEQAIFPRAAIAKAGALGfcgLYACEAAGGLALPRLDATLVFEELAAIDPS 82
Cdd:cd01152 5 AFRAEVRAWlAAHLPPELREESALGYREGREDRRRWQRALAAAGWAA---PGWPKEYGGRGASLMEQLIFREEMAAAGAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 83 TTAFISIHNMATWMLGRWATPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRAERVGSDYVINGSKAFISGAGST 162
Cdd:cd01152 82 VPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 163 DMLVLMARTGAAGAGGI--SAFAVPADTPGISYgkkerklgwnsQPTRSIG---------LEQLRIPAEHLLGRVGEGFK 231
Cdd:cd01152 162 DWAWLLVRTDPEAPKHRgiSILLVDMDSPGVTV-----------RPIRSINggeffnevfLDDVRVPDANRVGEVNDGWK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 232 IAMQGLDGGRINIAscSVGAAQGALQAARQYMQQRRqfGQPLASFQALQFKLADMATELVAARQMV-RLAASKLDTGAPD 310
Cdd:cd01152 231 VAMTTLNFERVSIG--GSAATFFELLLARLLLLTRD--GRPLIDDPLVRQRLARLEAEAEALRLLVfRLASALAAGKPPG 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500135244 311 ASTycAMAKRFATDIGFAVCNEALQLHGGYGYIREYP--------IERLLRDTRVHQILEGSNEIMRLIIARRILD 378
Cdd:cd01152 307 AEA--SIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIAERLLG 380
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
5-376 |
6.39e-32 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 124.58 E-value: 6.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 5 LTEEQRAFAKSAHDFARAEFAPHAAQWDEQAIFPRAAIAKAGALGFCGL----YACEaagGLALprLDATLVFEELAAID 80
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGtikgYGCP---GLSI--TASAIATAEVARVD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 81 PSTTAFISIHN-MATWMLGRWATPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRAERVGSDYVINGSKAFISGA 159
Cdd:PLN02526 104 ASCSTFILVHSsLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 160 GSTDMLVLMarTGAAGAGGISAFAVPADTPGISYGKKERKLGWNSQPTRSIGLEQLRIPAEHLLGRVgEGFKIAMQGLDG 239
Cdd:PLN02526 184 TFADVLVIF--ARNTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 240 GRINIASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADM-----ATELVAARQMVRLAASKLDTGapdastY 314
Cdd:PLN02526 261 SRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMlgniqAMFLVGWRLCKLYESGKMTPG------H 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500135244 315 CAMAKRFATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIARRI 376
Cdd:PLN02526 335 ASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
87-376 |
8.45e-30 |
|
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: 119.01 E-value: 8.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 87 ISIHNMATWMLGRWATPAVRDHWGPLLTRGEK---LASYCLTEPGAGSDAAALTTRAERVGSD-YVINGSKAFISGAGST 162
Cdd:cd01154 113 LTMTDAAVYALRKYGPEELKQYLPGLLSDRYKtglLGGTWMTEKQGGSDLGANETTAERSGGGvYRLNGHKWFASAPLAD 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 163 DMLVLMARTGAAGAGGISAF-AVPADTP-----GISYGKKERKLGWNSQPTRSIGLEQlripAE-HLLGRVGEGFKIAMQ 235
Cdd:cd01154 193 AALVLARPEGAPAGARGLSLfLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDD----AEaYLIGDEGKGIYYILE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 236 GLDGGRINIASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDTGAPDASTYC 315
Cdd:cd01154 269 MLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEA 348
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500135244 316 AMA-------KRFATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIARRI 376
Cdd:cd01154 349 HMArlatpvaKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVL 416
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
121-213 |
2.78e-18 |
|
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: 79.25 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 121 SYCLTEPGAGSDAAALTTRA-ERVGSDYVINGSKAFISGAGSTD-MLVLMARTGAAGAGGISAFAVPADTPGISYGKKER 198
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADlFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 500135244 199 KLGWNSQPTRSIGLE 213
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
91-374 |
2.86e-18 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 86.77 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 91 NMAtwMLGRWATPAVRDHWGPLLTRGEKLASYCLTEPG-AGSDAAALTTRAERVGSDYVINGSKAFISGA--GSTDMLVL 167
Cdd:PLN02876 525 NME--VLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIV 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 168 MARTGAAGAGGISAFAVPAD--TPGISYGKKERKLGWNSQPT--RSIGLEQLRIPAEHLLGRVGEGFKIAMQGLDGGRIN 243
Cdd:PLN02876 603 MGKTDFNAPKHKQQSMILVDiqTPGVQIKRPLLVFGFDDAPHghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLH 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 244 IASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDT-GAPDASTYCAMAKRFA 322
Cdd:PLN02876 683 HCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRlGNKKARGIIAMAKVAA 762
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 500135244 323 TDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIAR 374
Cdd:PLN02876 763 PNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAK 814
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
39-383 |
6.18e-17 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 82.61 E-value: 6.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 39 RAAIAKAGALGFCGLYACEAAGGLALPRLDATLVFEELAAIDP--STTAFISIHNMATWMLgrWATPAVRDHWGPLLTRG 116
Cdd:PTZ00456 102 KEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWgfSMYPGLSIGAANTLMA--WGSEEQKEQYLTKLVSG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 117 EKLASYCLTEPGAGSDAAALTTRAERVGS-DYVINGSKAFISgAGSTDM------LVLMARTGAagaggisafavPADTP 189
Cdd:PTZ00456 180 EWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFIS-AGDHDLtenivhIVLARLPNS-----------LPTTK 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 190 GISY----------------------GKKERKLGWNSQPTRSIGLEQlriPAEHLLGRVGEGFKIAMQGLDGGRINIASC 247
Cdd:PTZ00456 248 GLSLflvprhvvkpdgsletaknvkcIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 248 SVGAAQGALQAARQYMQQRRqfgqplaSFQALQ-FKLADMATELVA----ARQMVRLA--------ASKLDTG------- 307
Cdd:PTZ00456 325 GVCHAELAFQNALRYARERR-------SMRALSgTKEPEKPADRIIchanVRQNILFAkavaeggrALLLDVGrlldiha 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 308 -APDAST----------YCAMAKRFATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRL-IIARR 375
Cdd:PTZ00456 398 aAKDAATrealdheigfYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRK 477
|
....*...
gi 500135244 376 ILDGACGD 383
Cdd:PTZ00456 478 VLSLKGGN 485
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
102-341 |
1.69e-15 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 78.08 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 102 TPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALT-----TRAERVGSDYV---INGSKAFISGAGSTDMLVLMARTG- 172
Cdd:PRK13026 176 TQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEVLglrLTWDKRYITLAPVATVLGLAFKLRd 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 173 ------AAGAGGISAFAVPADTPGISYGKKERKLGWNSQ--PTRSiglEQLRIPAEHLLG---RVGEGFKIAMQGLDGGR 241
Cdd:PRK13026 256 pdgllgDKKELGITCALIPTDHPGVEIGRRHNPLGMAFMngTTRG---KDVFIPLDWIIGgpdYAGRGWRMLVECLSAGR 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 242 -INIASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAASKLDTGA-PDASTycAMAK 319
Cdd:PRK13026 333 gISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVkPSVVT--AIAK 410
|
250 260
....*....|....*....|..
gi 500135244 320 RFATDIGFAVCNEALQLHGGYG 341
Cdd:PRK13026 411 YHMTELARDVVNDAMDIHAGKG 432
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
97-344 |
9.39e-15 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 76.01 E-value: 9.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 97 LGRWATPAVRDHWGPLLTRGEKLASYCLTEPGAGSDAAALT-----TRAERVGSDYV---INGSKAFISGA--------- 159
Cdd:PRK09463 172 LLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLgmrLTWNKRYITLApiatvlgla 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 160 ----------------GSTDMLVlmartgaagaggisafavPADTPGISYGKKERKLGWNSQ--PTRSiglEQLRIPAEH 221
Cdd:PRK09463 252 fklydpdgllgdkedlGITCALI------------------PTDTPGVEIGRRHFPLNVPFQngPTRG---KDVFIPLDY 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 222 LLG---RVGEGFKIAMQGLDGGR-INIASCSVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMV 297
Cdd:PRK09463 311 IIGgpkMAGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAAR 390
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 500135244 298 RLAASKLDTGA-PdaSTYCAMAKRFATDIGFAVCNEALQLHGGYGYIR 344
Cdd:PRK09463 391 TLTTAAVDLGEkP--SVLSAIAKYHLTERGRQVINDAMDIHGGKGICL 436
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
264-366 |
8.80e-13 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 65.06 E-value: 8.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 264 QQRRQFGQPLASFQALQFKLADMATELVAARQMVRLAAS----KLDTGAPDASTYCA---MAKRFATDIGFAVCNEALQL 336
Cdd:pfam08028 24 RVRAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAArieaAAAAGKPVTPALRAearRAAAFATELAVAAVDALFRA 103
|
90 100 110
....*....|....*....|....*....|
gi 500135244 337 HGGYGYIREYPIERLLRDTRVHQILEGSNE 366
Cdd:pfam08028 104 AGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
22-358 |
6.60e-11 |
|
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: 63.11 E-value: 6.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 22 AEFAPHAAQWDEQAIFPRAAIAKAGALGFCGLYACEAAGGLALPRLDATLVFEELAAIDPSTTAFISIHNMATWMLGRWA 101
Cdd:cd01163 8 ARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVEALLLAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 102 TPAVRDHWGPLLTRGEkLASYCLTEPGaGSDAAALTTRAERVGSDYVINGSKAFISGAGSTDMLVLmarTGAAGAGGISA 181
Cdd:cd01163 88 PEQFRKRWFGRVLNGW-IFGNAVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTV---SALDEEGKLVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 182 FAVPADTPGIsygkkERKLGWNSQPTR-----SIGLEQLRIPAEHLLGRVGEGFKIAMQGLDGGRINIAScSVGAAQGAL 256
Cdd:cd01163 163 AAVPTDRPGI-----TVVDDWDGFGQRltasgTVTFDNVRVEPDEVLPRPNAPDRGTLLTAIYQLVLAAV-LAGIARAAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 257 QAARQYMQQR-RQFGQPLAS-----FQALQfKLADMATELVAARQMVRLAASKLDTGAP-----------DASTYCAMAK 319
Cdd:cd01163 237 DDAVAYVRSRtRPWIHSGAEsarddPYVQQ-VVGDLAARLHAAEALVLQAARALDAAAAagtaltaeargEAALAVAAAK 315
|
330 340 350
....*....|....*....|....*....|....*....
gi 500135244 320 RFATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVH 358
Cdd:cd01163 316 VVVTRLALDATSRLFEVGGASATAREHNLDRHWRNARTH 354
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
100-374 |
1.07e-09 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 59.77 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 100 WATPAVRDHWGP-LLTRGEK---LASYCLTEPGAGSDAAALTTRAERV-GSDYVINGSKAFISGAGSTDMLVLmartgAA 174
Cdd:PRK11561 156 WLTPLLSDRYDShLLPGGQKrglLIGMGMTEKQGGSDVLSNTTRAERLaDGSYRLVGHKWFFSVPQSDAHLVL-----AQ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 175 GAGGISAFAVPADTP-----GISYGKKERKLGWNSQPTRSIgleQLRIPAEHLLGRVGEGFK--IAMQGLDggRINIASC 247
Cdd:PRK11561 231 AKGGLSCFFVPRFLPdgqrnAIRLERLKDKLGNRSNASSEV---EFQDAIGWLLGEEGEGIRliLKMGGMT--RFDCALG 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 248 SVGAAQGALQAARQYMQQRRQFGQPLASFQALQFKLADMATELVAARQMV-RLAASKLDTGAPDAStycAMAKRFATDIG 326
Cdd:PRK11561 306 SHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLfRLARAWDRRADAKEA---LWARLFTPAAK 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 500135244 327 FAVCN-------EALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIAR 374
Cdd:PRK11561 383 FVICKrgipfvaEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
106-377 |
2.94e-07 |
|
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: 52.33 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 106 RDHWGPLLTRGEKLASYCLTEPGAGSDAAALTTRA--ERVGSDYVIN-----GSKAFISGAG--STDMLVLMARTGAAGA 176
Cdd:cd01150 122 QDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWWPGNLGktATHAVVFAQLITPGKN 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 177 GGISAFAVP---ADT----PGISYGKKERKLGWNSQPTRSIGLEQLRIPAEHLLGRVGE----------------GFKIA 233
Cdd:cd01150 202 HGLHAFIVPirdPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDvspdgtyvspfkdpnkRYGAM 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 234 MQGLDGGRINIASCSVGAAQGALQAARQYMQQRRQFGQ-------PLASFQALQFKLADM-ATELV---AARQMV----- 297
Cdd:cd01150 282 LGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPkpsdpevQILDYQLQQYRLFPQlAAAYAfhfAAKSLVemyhe 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 298 ---RLAASKLDTGaPDASTYCAMAKRFATDIGFAVCNEALQLHGGYGYIREYPIERLLRDTRVHQILEGSNEIMRLIIAR 374
Cdd:cd01150 362 iikELLQGNSELL-AELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTAN 440
|
...
gi 500135244 375 RIL 377
Cdd:cd01150 441 YLL 443
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
189-368 |
7.83e-05 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 44.85 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 189 PGISYGKKERKLGWNSQPTRSIGLEQLRIPAEHLLGRVGE----------------GFKIAMQGLDGGRINIASCSVGAA 252
Cdd:PLN02636 266 PGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDvsrdgkytsslptinkRFAATLGELVGGRVGLAYGSVGVL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 253 QGALQAARQYMQQRRQFGQP------LASFQALQFKLADM---------ATELVAAR--QMVRlaaSKLDTGAPDASTYC 315
Cdd:PLN02636 346 KASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQHKLMPMlastyafhfATEYLVERysEMKK---THDDQLVADVHALS 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500135244 316 AMAKRFATDI---GFAVCNEALqlhGGYGYIREYPIERLLRDTRVHQILEGSNEIM 368
Cdd:PLN02636 423 AGLKAYITSYtakALSTCREAC---GGHGYAAVNRFGSLRNDHDIFQTFEGDNTVL 475
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
60-234 |
2.41e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 39.86 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 60 GGLALPRLDATLVFEELAA-IDPSTTAFISIHNMATWMLGRWATPAVRDHWGPLLTRGEKLASYClTEPGAGSDAAALTT 138
Cdd:PTZ00457 75 GGLGLGHTAHALIYEEVGTnCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISMNTT 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500135244 139 RAE-RVGSDYVINGSKAFISGAGSTDMLVLMARTGAAGAGGISAFA-------VPADTPGISYGKKerklgwnsqptrSI 210
Cdd:PTZ00457 154 KASlTDDGSYVLTGQKRCEFAASATHFLVLAKTLTQTAAEEGATEVsrnsffiCAKDAKGVSVNGD------------SV 221
|
170 180
....*....|....*....|....
gi 500135244 211 GLEQlrIPAEHLLGRVGEGFKIAM 234
Cdd:PTZ00457 222 VFEN--TPAADVVGVVGEGFKDAM 243
|
|
| |
