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Conserved domains on  [gi|494645808|ref|WP_007403752|]
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MULTISPECIES: acyl-CoA dehydrogenase family protein [Sphingomonas]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 550)

acyl-CoA dehydrogenase (ACAD) family protein similar to acyl-CoA dehydrogenase that catalyzes the alpha,beta dehydrogenation of an acyl-CoA to form 2,3-dehydroacyl-CoA; requires an acceptor such as FAD, which becomes reduced

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACAD super family cl09933
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 6-378 0e+00

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)


The actual alignment was detected with superfamily member cd01162:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 375  Bit Score: 605.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   6 LTDEQREIQDLARRFTADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGCPSTS 85
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  86 AFISIHNMASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGDHYVVSGSKQFISGGGENEV 165
Cdd:cd01162   81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 166 YVTMVRTGEDGPKGISCLVIDKDTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRLGAEGEGFRIAMMGLDGGRLNI 245
Cdd:cd01162  161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 246 GACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVTDNAPDKTRFAAMAKRLATD 325
Cdd:cd01162  241 ASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATD 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 494645808 326 TGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLL 378
Cdd:cd01162  321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALL 373
 
Name Accession Description Interval E-value
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 6-378 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: 605.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   6 LTDEQREIQDLARRFTADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGCPSTS 85
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  86 AFISIHNMASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGDHYVVSGSKQFISGGGENEV 165
Cdd:cd01162   81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 166 YVTMVRTGEDGPKGISCLVIDKDTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRLGAEGEGFRIAMMGLDGGRLNI 245
Cdd:cd01162  161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 246 GACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVTDNAPDKTRFAAMAKRLATD 325
Cdd:cd01162  241 ASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATD 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 494645808 326 TGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLL 378
Cdd:cd01162  321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALL 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 4-380 3.38e-158

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: 449.29  E-value: 3.38e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   4 FDLTDEQREIQDLARRFTADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGCPS 83
Cdd:COG1960    3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  84 TSAFISIHNMASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGDHYVVSGSKQFISGGGEN 163
Cdd:COG1960   83 LALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 164 EVYVTMVRTGED-GPKGISCLVIDKDTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRLGAEGEGFRIAMMGLDGGR 242
Cdd:COG1960  163 DVILVLARTDPAaGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 243 LNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVtDNAPDKTRFAAMAKRL 322
Cdd:COG1960  243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLL-DAGEDAALEAAMAKLF 321

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 494645808 323 ATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLLKD 380
Cdd:COG1960  322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
PRK12341 PRK12341
acyl-CoA dehydrogenase;
4-380 1.89e-67

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 217.67  E-value: 1.89e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   4 FDLTDEQ-------REIqdLARRFTADritpFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEA 76
Cdd:PRK12341   3 FSLTEEQelllasiREL--ITRNFPEE----YFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  77 MAYGC---PSTSAFISIHNMAswmidRFGDADVKGRYLPDLVTMDRMAsYCL--TEPGSGSDAAALKTRAVR-DGDHYVv 150
Cdd:PRK12341  77 VSKCGapaFLITNGQCIHSMR-----RFGSAEQLRKTAESTLETGDPA-YALalTEPGAGSDNNSATTTYTRkNGKVYL- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 151 SGSKQFISGGGENEVYVTMVRTGE--DGPKGISCLVIDKDTPGVSFGANErKLGWHSQPTRQVMFDNVRIPVANRLGAEG 228
Cdd:PRK12341 150 NGQKTFITGAKEYPYMLVLARDPQpkDPKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEG 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 229 EGFRIAMMGLDGGRLNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVTDN 308
Cdd:PRK12341 229 MGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNG 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494645808 309 APDKTRfAAMAKRLATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLLKD 380
Cdd:PRK12341 309 QSLRTS-AALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKD 379
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 228-375 1.17e-43

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: 148.56  E-value: 1.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  228 GEGFRIAMMGLDGGRLNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVtD 307
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEAL-D 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494645808  308 NAPDKTRFAAMAKRLATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGR 375
Cdd:pfam00441  80 AGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
sulfur_SfnB TIGR04022
sulfur acquisition oxidoreductase, SfnB family; Members of this protein family belong to the ...
 12-359 3.81e-08

sulfur acquisition oxidoreductase, SfnB family; Members of this protein family belong to the greater family of acyl-CoA dehydrogenases. This family includes the sulfate starvation induced protein SfnB of Pseudomonas putida strain DS1, which is both encoded nearby to and phylogenetically closely correlated with the dimethyl sulphone monooxygenase SfnG. This family shows considerable sequence similarity to the Rhodococcus dibenzothiophene desulfurization enzyme DszC, although that enzyme falls outside of the scope of this family. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 274924 [Multi-domain]  Cd Length: 391  Bit Score: 54.58  E-value: 3.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   12 EIQDLARRFtADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGCPSTSAFISIH 91
Cdd:TIGR04022   9 EALEIARRL-AAEFAPGAAERDRERRLPWAELDAFSQSGLWGITVPRAYGGAGVSYATLAEVIAIISAADPSLGQIPQNH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   92 NMASWMIDRFGDADVKGRYLPDLVTMDRMASyCLTEPGSgSDAAALKTRAVRDGDHYVVSGSKqFISGGGENEVYVTMVR 171
Cdd:TIGR04022  88 FYALEVLRLTGSEEQKRFFFGEVLAGERFGN-AFSERGT-RNVLDFQTRLRRDGDGYRLNGRK-FYSTGALFAHWIPVLA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  172 TGEDGPKGISclVIDKDTPGV-------SFGanerklgwhsQPTR---QVMFDNVRIPVAN---------RLGAEGEGFR 232
Cdd:TIGR04022 165 LDDEGRAVLA--FVPRDAPGLtviddwsGFG----------QRTTasgTVLLDDVRVPAEHvvpiqrafdRPTAAGPVAQ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  233 IAMMGLDggrlnigacsLGGAQRCLDEAVAYVKDR-RQFGKAIAEFQN----TQFTLADMATELEAARALLYLAAAKVtD 307
Cdd:TIGR04022 233 IIHAAID----------AGIARAALADTLAFVRERaRPWIDSGVERASddplTIAEVGDLAIRLHAAEALLERAGRAV-D 301

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494645808  308 NA---PDKTRFA------AMAKRLATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVH 359
Cdd:TIGR04022 302 AAraePTEESVAaasiavAEAKVLTTEIALLAASKLFELAGTRSTLAEHNLDRHWRNARTH 362
 
Name Accession Description Interval E-value
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 6-378 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: 605.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   6 LTDEQREIQDLARRFTADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGCPSTS 85
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  86 AFISIHNMASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGDHYVVSGSKQFISGGGENEV 165
Cdd:cd01162   81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 166 YVTMVRTGEDGPKGISCLVIDKDTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRLGAEGEGFRIAMMGLDGGRLNI 245
Cdd:cd01162  161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 246 GACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVTDNAPDKTRFAAMAKRLATD 325
Cdd:cd01162  241 ASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATD 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 494645808 326 TGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLL 378
Cdd:cd01162  321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALL 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 4-380 3.38e-158

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: 449.29  E-value: 3.38e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   4 FDLTDEQREIQDLARRFTADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGCPS 83
Cdd:COG1960    3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  84 TSAFISIHNMASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGDHYVVSGSKQFISGGGEN 163
Cdd:COG1960   83 LALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 164 EVYVTMVRTGED-GPKGISCLVIDKDTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRLGAEGEGFRIAMMGLDGGR 242
Cdd:COG1960  163 DVILVLARTDPAaGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 243 LNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVtDNAPDKTRFAAMAKRL 322
Cdd:COG1960  243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLL-DAGEDAALEAAMAKLF 321

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 494645808 323 ATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLLKD 380
Cdd:COG1960  322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 8-379 2.42e-145

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: 416.67  E-value: 2.42e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   8 DEQREIQDLARRFTADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGCPSTSAF 87
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  88 ISIHN-MASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGDHYVVSGSKQFISGGGENEVY 166
Cdd:cd01158   81 VSVHNsLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 167 VTMVRTGED-GPKGISCLVIDKDTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRLGAEGEGFRIAMMGLDGGRLNI 245
Cdd:cd01158  161 IVFAVTDPSkGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 246 GACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKvTDNAPDKTRFAAMAKRLATD 325
Cdd:cd01158  241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARL-KDNGEPFIKEAAMAKLFASE 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494645808 326 TGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLLK 379
Cdd:cd01158  320 VAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 8-375 3.22e-116

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: 340.80  E-value: 3.22e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   8 DEQREIQDLARRFTADRITPFAAEWDEKHIFPRDTIREAAELgfaaiyvseesggialgrleaalimeamaygcpstsaf 87
Cdd:cd00567    1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLL-------------------------------------- 42

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  88 isihnMASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGDHYVVSGSKQFISGGGENEVYV 167
Cdd:cd00567   43 -----LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 168 TMVRTGEDGP--KGISCLVIDKDTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRLGAEGEGFRIAMMGLDGGRLNI 245
Cdd:cd00567  118 VLARTDEEGPghRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 246 GACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVTDNAPDKTRFAAMAKRLATD 325
Cdd:cd00567  198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATE 277

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 494645808 326 TGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGR 375
Cdd:cd00567  278 AAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 9-378 6.37e-105

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: 313.67  E-value: 6.37e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   9 EQREIQDLARRFTADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAY-GCPSTSaf 87
Cdd:cd01160    2 EHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARaGGSGPG-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  88 ISIHN-MASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGDHYVVSGSKQFISGGGENEVY 166
Cdd:cd01160   80 LSLHTdIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 167 VTMVRTGED--GPKGISCLVIDKDTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRLGAEGEGFRIAMMGLDGGRLN 244
Cdd:cd01160  160 IVVARTGGEarGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 245 IGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVTDNAPDKTRfAAMAKRLAT 324
Cdd:cd01160  240 IAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAE-ASMAKYWAT 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494645808 325 DTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLL 378
Cdd:cd01160  319 ELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 6-378 1.88e-98

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: 297.57  E-value: 1.88e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   6 LTDEQREIQDLARRFTADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGCPSTS 85
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  86 AFISIHNMASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGDHYVVSGSKQFISGGGENEV 165
Cdd:cd01157   81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 166 YVTMVRTGED----GPKGISCLVIDKDTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRLGAEGEGFRIAMMGLDGG 241
Cdd:cd01157  161 YFLLARSDPDpkcpASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 242 RLNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVtDNAPDKTRFAAMAKR 321
Cdd:cd01157  241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEV-DSGRRNTYYASIAKA 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 494645808 322 LATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLL 378
Cdd:cd01157  320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 5-379 1.46e-94

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: 287.39  E-value: 1.46e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   5 DLTDEQREIQDLARRFTADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGCPST 84
Cdd:cd01156    1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  85 SAFISIH-NMASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGDHYVVSGSKQFISGGGEN 163
Cdd:cd01156   81 ALSYGAHsNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 164 EVYVTMVRTGED-GPKGISCLVIDKDTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRLGAEGEGFRIAMMGLDGGR 242
Cdd:cd01156  161 DTLVVYAKTDPSaGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYER 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 243 LNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVtDNAPDKTRFAAMAKRL 322
Cdd:cd01156  241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKAC-DRGNMDPKDAAGVILY 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 494645808 323 ATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLLK 379
Cdd:cd01156  320 AAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 3-380 2.24e-92

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: 282.82  E-value: 2.24e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   3 QFDLTDEQREIQDLARRFTADRITPFAAEWDEKHifPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGCp 82
Cdd:cd01161   24 TEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKI--PRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDL- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  83 STSAFISIH-NMASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVR--DGDHYVVSGSKQFISG 159
Cdd:cd01161  101 GFSVTLGAHqSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWITN 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 160 GGENEVYVTMVRT---GEDGPK--GISCLVIDKDTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRLGAEGEGFRIA 234
Cdd:cd01161  181 GGIADIFTVFAKTevkDATGSVkdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVA 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 235 MMGLDGGRLNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVtdNAPDKTR 314
Cdd:cd01161  261 MNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNM--DRGLKAE 338

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494645808 315 F---AAMAKRLATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLLKD 380
Cdd:cd01161  339 YqieAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQH 407
PRK12341 PRK12341
acyl-CoA dehydrogenase;
4-380 1.89e-67

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 217.67  E-value: 1.89e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   4 FDLTDEQ-------REIqdLARRFTADritpFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEA 76
Cdd:PRK12341   3 FSLTEEQelllasiREL--ITRNFPEE----YFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  77 MAYGC---PSTSAFISIHNMAswmidRFGDADVKGRYLPDLVTMDRMAsYCL--TEPGSGSDAAALKTRAVR-DGDHYVv 150
Cdd:PRK12341  77 VSKCGapaFLITNGQCIHSMR-----RFGSAEQLRKTAESTLETGDPA-YALalTEPGAGSDNNSATTTYTRkNGKVYL- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 151 SGSKQFISGGGENEVYVTMVRTGE--DGPKGISCLVIDKDTPGVSFGANErKLGWHSQPTRQVMFDNVRIPVANRLGAEG 228
Cdd:PRK12341 150 NGQKTFITGAKEYPYMLVLARDPQpkDPKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEG 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 229 EGFRIAMMGLDGGRLNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVTDN 308
Cdd:PRK12341 229 MGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNG 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494645808 309 APDKTRfAAMAKRLATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLLKD 380
Cdd:PRK12341 309 QSLRTS-AALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKD 379
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 2-380 7.17e-63

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 206.65  E-value: 7.17e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   2 TQFDLTDEQREIQDLARRFTADRITPFAAEWDEKHIFPRDT--IREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAY 79
Cdd:PLN02519  22 SSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISR 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  80 GCPSTSAFISIH-NMASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGDHYVVSGSKQFIS 158
Cdd:PLN02519 102 ASGSVGLSYGAHsNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCT 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 159 GGGENEVYVTMVRTG-EDGPKGISCLVIDKDTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRLGAEGEGFRIAMMG 237
Cdd:PLN02519 182 NGPVAQTLVVYAKTDvAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSG 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 238 LDGGRLNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATElEAARALLYLAAAKVTDNAPDKTRFAA 317
Cdd:PLN02519 262 LDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTS-LQSSRSYVYSVARDCDNGKVDRKDCA 340

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494645808 318 MAKRLATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLLKD 380
Cdd:PLN02519 341 GVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 6-375 2.13e-62

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: 204.90  E-value: 2.13e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   6 LTDEQREIQDLARRFTADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVsEESGGIALGRLEAALIMEAMAYGCPSTS 85
Cdd:cd01151   13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATI-KGYGCAGLSSVAYGLIAREVERVDSGYR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  86 AFISIH-NMASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGDHYVVSGSKQFISGGGENE 164
Cdd:cd01151   92 SFMSVQsSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 165 VYVTMVRTGEDGpkGISCLVIDKDTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRLgAEGEGFRIAMMGLDGGRLN 244
Cdd:cd01151  172 VFVVWARNDETG--KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNARYG 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 245 IGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATElEAARALLYLAAAKVTDNAPDKTRFAAMAKRLAT 324
Cdd:cd01151  249 IAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTE-IALGLLACLRVGRLKDQGKATPEQISLLKRNNC 327

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 494645808 325 DTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGR 375
Cdd:cd01151  328 GKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGR 378
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 4-380 7.07e-50

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 171.94  E-value: 7.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   4 FDLTDEQREIQDLARRFTA-DRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMA-YGC 81
Cdd:PRK03354   3 FNLNDEQELFVAGIRELMAsENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGrLGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  82 PSTSAFISIHNMASWMidRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGDHYVVSGSKQFISGGG 161
Cdd:PRK03354  83 PTYVLYQLPGGFNTFL--REGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 162 ENEVYVTMVRTGEDGPKGI-SCLVIDKDTPGVSFGANErKLGWHSQPTRQVMFDNVRIPVANRLGAEGEGFRIAMMGLDG 240
Cdd:PRK03354 161 YTPYIVVMARDGASPDKPVyTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDH 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 241 GRLNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKvTDNAPDKTRFAAMAK 320
Cdd:PRK03354 240 ERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWK-ADNGTITSGDAAMCK 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 321 RLATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLLKD 380
Cdd:PRK03354 319 YFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 1-379 8.18e-50

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 172.43  E-value: 8.18e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   1 MTQFDLTDEQREIQDLARRFTADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYG 80
Cdd:PTZ00461  32 MDLYNPTPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKY 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  81 CPSTSAFISIHNMAswMIDRF---GDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGD-HYVVSGSKQF 156
Cdd:PTZ00461 112 DPGFCLAYLAHSML--FVNNFyysASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIW 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 157 ISGGGENEVYVTMVRTgeDGPkgISCLVIDKDTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRLGAEGEGFRIAMM 236
Cdd:PTZ00461 190 ITNGTVADVFLIYAKV--DGK--ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMR 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 237 GLDGGRLNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVtdnAPD-KTRF 315
Cdd:PTZ00461 266 NLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNV---HPGnKNRL 342

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494645808 316 AAMAKRL-ATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLLK 379
Cdd:PTZ00461 343 GSDAAKLfATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLK 407
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 33-368 1.89e-48

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: 168.72  E-value: 1.89e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  33 DEKHIFP---RDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGC-PSTSAFISIHNMASwmIDRFGDADVKG 108
Cdd:cd01153   29 DGRVVVPppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDaPLMYASGTQGAAAT--LLAHGTEAQRE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 109 RYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGD-HYVVSGSKQFISGG----GENEVYVTMVRTGEDGP--KGIS 181
Cdd:cd01153  107 KWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGehdmSENIVHLVLARSEGAPPgvKGLS 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 182 CLVIDK-----DTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVanrLGAEGEGFRIAMMGLDGGRLNIGACSLGGAQRC 256
Cdd:cd01153  187 LFLVPKflddgERNGVTVARIEEKMGLHGSPTCELVFDNAKGEL---IGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAA 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 257 LDEAVAYVKDRRQFGKAIAEFQN--------------TQFTLADMATELEAARALLYLAAAKVTDNAPDKTRFAA----- 317
Cdd:cd01153  264 YLNALAYAKERKQGGDLIKAAPAvtiihhpdvrrslmTQKAYAEGSRALDLYTATVQDLAERKATEGEDRKALSAladll 343

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 494645808 318 --MAKRLATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQV 368
Cdd:cd01153  344 tpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 8-378 9.67e-48

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: 166.37  E-value: 9.67e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   8 DEQREIQDLARRF-----TADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGCP 82
Cdd:cd01152    1 PSEEAFRAEVRAWlaahlPPELREESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  83 STSAFISIHNMASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGDHYVVSGSKQFISGGGE 162
Cdd:cd01152   81 PVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 163 NEVYVTMVRTGEDGPK--GISCLVIDKDTPGVSFGANERKLGWHSqpTRQVMFDNVRIPVANRLGAEGEGFRIAMMGLDG 240
Cdd:cd01152  161 ADWAWLLVRTDPEAPKhrGISILLVDMDSPGVTVRPIRSINGGEF--FNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNF 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 241 GRLNIG---ACSLGGAQRCLDEAVAY----VKD---RRQFGKAIAEFQNTQ---FTLADMATELEAARALlylaaakvtd 307
Cdd:cd01152  239 ERVSIGgsaATFFELLLARLLLLTRDgrplIDDplvRQRLARLEAEAEALRllvFRLASALAAGKPPGAE---------- 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494645808 308 napdktrfAAMAKRLATDTGSSVVDRALQLHG-----GYGYLMDYPIERFWRDL---RVHSILEGTNQVMRMIVGRDLL 378
Cdd:cd01152  309 --------ASIAKLFGSELAQELAELALELLGtaallRDPAPGAELAGRWEADYlrsRATTIYGGTSEIQRNIIAERLL 379
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 12-379 1.55e-45

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: 160.63  E-value: 1.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  12 EIQDLARRFTADRITPFAAE-----------WDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAM--- 77
Cdd:cd01155    5 ELRARVKAFMEEHVYPAEQEfleyyaeggdrWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETgrs 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  78 -----AYGC--PSTSafisihNMAswMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPG-SGSDAAALKTRAVRDGDHYV 149
Cdd:cd01155   85 ffapeVFNCqaPDTG------NME--VLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 150 VSGSKQFISGGGEN--EVYVTMVRTGEDGP---KGISCLVIDKDTPGVSFGANERKLGWHSQPT--RQVMFDNVRIPVAN 222
Cdd:cd01155  157 INGRKWWSSGAGDPrcKIAIVMGRTDPDGAprhRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHghAEITFDNVRVPASN 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 223 RLGAEGEGFRIAMMGLDGGRLNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLAD--MATELEAARALLYL 300
Cdd:cd01155  237 LILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKsrIEIEQARLLVLKAA 316

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494645808 301 AAAKVTDNAPDKTRFaAMAKRLATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLLK 379
Cdd:cd01155  317 HMIDTVGNKAARKEI-AMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 228-375 1.17e-43

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: 148.56  E-value: 1.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  228 GEGFRIAMMGLDGGRLNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVtD 307
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEAL-D 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494645808  308 NAPDKTRFAAMAKRLATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGR 375
Cdd:pfam00441  80 AGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 7-118 3.59e-43

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: 146.07  E-value: 3.59e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808    7 TDEQREIQDLARRFTADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGCPSTSA 86
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 494645808   87 FISIHN-MASWMIDRFGDADVKGRYLPDLVTMD 118
Cdd:pfam02771  81 ALSVHSsLGAPPILRFGTEEQKERYLPKLASGE 113
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 12-369 1.35e-33

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: 129.03  E-value: 1.35e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  12 EIQDLARRftADRITPFAAEWD------EKHIFP---RDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYG-- 80
Cdd:cd01154   33 ELYELARL--ADRNPPVLEMWDrwgrrvDRVWVHpawHALMRRLIEEGVINIEDGPAGEGRRHVHFAAGYLLSDAAAGll 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  81 CPstsafISIHNMASWMIDRFGDADVKGRYLPDLVTMDR---MASYCLTEPGSGSDAAALKTRAVRD-GDHYVVSGSKQF 156
Cdd:cd01154  111 CP-----LTMTDAAVYALRKYGPEELKQYLPGLLSDRYKtglLGGTWMTEKQGGSDLGANETTAERSgGGVYRLNGHKWF 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 157 ISGGgENEVYVTMVRT--GEDGPKGISCLVIDKDTP-----GVSFGANERKLGWHSQPTRQVMFDNVripVANRLGAEGE 229
Cdd:cd01154  186 ASAP-LADAALVLARPegAPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGK 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 230 GFRIAMMGLDGGRLNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVTDNA 309
Cdd:cd01154  262 GIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAA 341

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494645808 310 PDKTRFAAMAkRLAT--------DTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVM 369
Cdd:cd01154  342 ADKPVEAHMA-RLATpvakliacKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
PLN02526 PLN02526
acyl-coenzyme A oxidase
 3-377 4.25e-29

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 116.88  E-value: 4.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   3 QFD--LTDEQREIQDLARRFTADRITPFAAEWDEKHIFPRDTIREAAELGFAaiyvseesGGI-------ALGRLEAALI 73
Cdd:PLN02526  24 QFDdlLTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIA--------GGTikgygcpGLSITASAIA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  74 MEAMAYGCPSTSAFISIHN-MASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRDGDHYVVSG 152
Cdd:PLN02526  96 TAEVARVDASCSTFILVHSsLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNG 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 153 SKQFISGGGENEVYVTMVRTGEDgpKGISCLVIDKDTPGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRL-GAegEGF 231
Cdd:PLN02526 176 QKRWIGNSTFADVLVIFARNTTT--NQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLpGV--NSF 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 232 RIAMMGLDGGRLNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATElEAARALLYLAAAKVTDNAPD 311
Cdd:PLN02526 252 QDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGN-IQAMFLVGWRLCKLYESGKM 330

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494645808 312 KTRFAAMAKRLATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDL 377
Cdd:PLN02526 331 TPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 122-214 1.89e-26

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: 101.20  E-value: 1.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  122 SYCLTEPGSGSDAAALKTRAV-RDGDHYVVSGSKQFISGGGENEVYVTMVRTGEDGPK-GISCLVIDKDTPGVSFGANER 199
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAAdGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHgGISLFLVPKDAPGVSVRRIET 80

                          90
                  ....*....|....*
gi 494645808  200 KLGWHSQPTRQVMFD 214
Cdd:pfam02770  81 KLGVRGLPTGELVFD 95
PLN02876 PLN02876
acyl-CoA dehydrogenase
 100-368 3.05e-24

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 104.49  E-value: 3.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 100 RFGDADVKGRYLPDLVTMDRMASYCLTEPG-SGSDAAALKTRAVRDGDHYVVSGSKQFISGGGEN--EVYVTMVRTGEDG 176
Cdd:PLN02876 531 RYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPrcRVLIVMGKTDFNA 610

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 177 P--KGISCLVIDKDTPGVS-------FGANERKLGwHSQptrqVMFDNVRIPVANRLGAEGEGFRIAMMGLDGGRLNIGA 247
Cdd:PLN02876 611 PkhKQQSMILVDIQTPGVQikrpllvFGFDDAPHG-HAE----ISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCM 685

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 248 CSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMATELEAARALLYLAAAKVTDNAPDKTRFA-AMAKRLATDT 326
Cdd:PLN02876 686 RLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRLGNKKARGIiAMAKVAAPNM 765

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 494645808 327 GSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQV 368
Cdd:PLN02876 766 ALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 50-379 2.05e-23

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 101.87  E-value: 2.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  50 GFAAIYVSEESGGIALGRLEAALIMEAMAYGCPSTSAF--ISIHNMASWMIdrFGDADVKGRYLPDLVTMDRMASYCLTE 127
Cdd:PTZ00456 112 GWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYpgLSIGAANTLMA--WGSEEQKEQYLTKLVSGEWSGTMCLTE 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 128 PGSGSDAAALKTRAVRDGD-HYVVSGSKQFISGGG----ENEVYVTMVRTGEDGP--KGISCLVIDKDTP---------- 190
Cdd:PTZ00456 190 PQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDhdltENIVHIVLARLPNSLPttKGLSLFLVPRHVVkpdgsletak 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 191 GVSFGANERKLGWHSQPTRQVMFDNvriPVANRLGAEGEGFRIAMMGLDGGRLNIGACSLGGAQRCLDEAVAYVKDRRQ- 269
Cdd:PTZ00456 270 NVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSm 346

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 270 ---------------------------FGKAIAEFQNTQFT----LADMATeleaarallylaaakvtdNAPDKTRFAAM 318
Cdd:PTZ00456 347 ralsgtkepekpadriichanvrqnilFAKAVAEGGRALLLdvgrLLDIHA------------------AAKDAATREAL 408

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494645808 319 ----------AKRLATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRM-IVGRDLLK 379
Cdd:PTZ00456 409 dheigfytpiAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVLS 480
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
245-367 8.00e-19

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 81.62  E-value: 8.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  245 IGACSLGGAQRCLDEAVAYVKDRRQ--FGKAIAEFQNTQFTLADMATE-------LEAARALLYLAAAKVTDNAPDKTRF 315
Cdd:pfam08028   2 IAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARidaarllLERAAARIEAAAAAGKPVTPALRAE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 494645808  316 AAMAKRLATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQ 367
Cdd:pfam08028  82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 29-378 4.27e-13

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: 69.69  E-value: 4.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  29 AAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGCPSTSAFISIHNMASWMIDRFGD---AD 105
Cdd:cd01159   14 APEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATHSRMLAAFPPeaqEE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 106 VKGRYLPDLVtmdrmasycltepgsgSDAAALKTRAVRDGDHYVVSGSKQFISG-GGENEVYVTMVRTGEDGPKGISCLV 184
Cdd:cd01159   94 VWGDGPDTLL----------------AGSYAPGGRAERVDGGYRVSGTWPFASGcDHADWILVGAIVEDDDGGPLPRAFV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 185 IDK------DTpgvsfganerklgWHSQPTR-----QVMFDNVRIPVANRL-----------GAEGEGFRIAMMGLDGgr 242
Cdd:cd01159  158 VPRaeyeivDT-------------WHVVGLRgtgsnTVVVDDVFVPEHRTLtagdmmagdgpGGSTPVYRMPLRQVFP-- 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 243 LNIGACSLGGAQRCLDEAVAYVKDRRQFGKA---IAEFQNTQFTLADMATELEAARALLYLAAAKVTDNAPDKTRFAAMA 319
Cdd:cd01159  223 LSFAAVSLGAAEGALAEFLELAGKRVRQYGAavkMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGGPIDVEE 302

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494645808 320 KR-------LATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRV---HSILEGTNQVmrMIVGRDLL 378
Cdd:cd01159  303 RArirrdaaYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHAaaqHAALNPETAA--EAYGRALL 369
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 56-259 1.70e-12

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 68.37  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  56 VSEESGGIALGRLEAALIMEAMAYGCPSTSAFISIH-NMASWMIDRFGDADVKGRYLPDLVTMDRMASYClTEPGSGSDA 134
Cdd:PTZ00457  70 IATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHsGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDI 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 135 AALKTRAV-RDGDHYVVSGSKQFISGGGENEVYV---TMVRT-GEDGPKGI---SCLVIDKDTPGVSFGANerklgwhsq 206
Cdd:PTZ00457 149 SMNTTKASlTDDGSYVLTGQKRCEFAASATHFLVlakTLTQTaAEEGATEVsrnSFFICAKDAKGVSVNGD--------- 219

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 494645808 207 ptrQVMFDNVriPVANRLGAEGEGFRIAMMGLDGGRLNIGACSLGGAQRCLDE 259
Cdd:PTZ00457 220 ---SVVFENT--PAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQE 267
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 68-379 1.31e-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: 62.73  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  68 LEAALIMEAMAYGCPSTSAFISIH-NMASWMIDRFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRD-- 144
Cdd:cd01150   82 EKMLALTNSLGGYDLSLGAKLGLHlGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDpl 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 145 GDHYVV-----SGSKQFISGGGENE----VYVTMVRTGEDgpKGISCLVI---DKDT----PGVSFGANERKLGWHSQPT 208
Cdd:cd01150  162 TQEFVIntpdfTATKWWPGNLGKTAthavVFAQLITPGKN--HGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDN 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 209 RQVMFDNVRIPVANRLG------AEG----------EGFRIAMMGLDGGRLNIGACSLGGAQRCLDEAVAYVKDRRQFGK 272
Cdd:cd01150  240 GFLQFRNVRIPRENLLNrfgdvsPDGtyvspfkdpnKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGP 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 273 -------AIAEFQN-----------------TQFTLADMATELEAARALlylaaaKVTDNAPDKTRFAAMAKRLATDTGS 328
Cdd:cd01150  320 kpsdpevQILDYQLqqyrlfpqlaaayafhfAAKSLVEMYHEIIKELLQ------GNSELLAELHALSAGLKAVATWTAA 393

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 494645808 329 SVVDRALQLHGGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGRDLLK 379
Cdd:cd01150  394 QGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLK 444
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 125-379 1.78e-10

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 62.46  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 125 LTEPGSGSDAAALKTRAVR-DGDHYVVSGSKQFISGGgENEVYVTMVRTgedgPKGISCLVIDKDTPGVSFGAN--ER-- 199
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERlADGSYRLVGHKWFFSVP-QSDAHLVLAQA----KGGLSCFFVPRFLPDGQRNAIrlERlk 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 200 -KLGWHSQPTRQVMFDNVripVANRLGAEGEGFR--IAMMGLDggRLNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAE 276
Cdd:PRK11561 259 dKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRliLKMGGMT--RFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIE 333

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 277 FQNTQFTLADMAT--ELEAARALLYLAAAKVTDNAPDKTR---FAAMAKRLATDTGSSVVDRALQLHGGYGYLMDYPIER 351
Cdd:PRK11561 334 QPLMRQVLSRMALqlEGQTALLFRLARAWDRRADAKEALWarlFTPAAKFVICKRGIPFVAEAMEVLGGIGYCEESELPR 413

                        250       260
                 ....*....|....*....|....*...
gi 494645808 352 FWRDLRVHSILEGTNQVMRMIVGRDLLK 379
Cdd:PRK11561 414 LYREMPVNSIWEGSGNIMCLDVLRVLNK 441
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 100-342 4.74e-09

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 57.90  E-value: 4.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 100 RFGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVrdgdhyVVSGSKQfisggGENEV---------YVTM- 169
Cdd:PRK09463 174 HYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGV------VCKGEWQ-----GEEVLgmrltwnkrYITLa 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 170 -VRT---------------GEDGPKGISCLVIDKDTPGVSFGANERKLGWHSQ--PTRQvmfDNVRIPVANRLGAE---G 228
Cdd:PRK09463 243 pIATvlglafklydpdgllGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQngPTRG---KDVFIPLDYIIGGPkmaG 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 229 EGFRIAMMGLDGGR-LNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMAteleaARALLYLAAAKVTD 307
Cdd:PRK09463 320 QGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIA-----GNAYLMDAARTLTT 394

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 494645808 308 NAPDKTR----FAAMAKRLATDTGSSVVDRALQLHGGYG 342
Cdd:PRK09463 395 AAVDLGEkpsvLSAIAKYHLTERGRQVINDAMDIHGGKG 433
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 22-360 1.03e-08

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: 56.56  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  22 ADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGCPSTSAFISIHNMASWMIDRF 101
Cdd:cd01163    7 AARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVEALLLA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 102 GDADVKGRYLPDLVTMDRMASyCLTEPGSGSDAAALkTRAVRDGDHYVVSGSKQFISGGGENEvYVTMVRTGEDGPKGIs 181
Cdd:cd01163   87 GPEQFRKRWFGRVLNGWIFGN-AVSERGSVRPGTFL-TATVRDGGGYVLNGKKFYSTGALFSD-WVTVSALDEEGKLVF- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 182 cLVIDKDTPGVSFGANerklgWHSQPTRQ-----VMFDNVRIPVANRLGAEGEGFRIAMMGLdGGRLNIGACSLGGAQRC 256
Cdd:cd01163  163 -AAVPTDRPGITVVDD-----WDGFGQRLtasgtVTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLAAVLAGIARAA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 257 LDEAVAYVKDR-------------------RQFGKAIAEFQNTQfTLADMATELEAARALLYLAAAKVTDNAPDKTrfAA 317
Cdd:cd01163  236 LDDAVAYVRSRtrpwihsgaesarddpyvqQVVGDLAARLHAAE-ALVLQAARALDAAAAAGTALTAEARGEAALA--VA 312

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 494645808 318 MAKRLATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHS 360
Cdd:cd01163  313 AAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNARTHT 355
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 101-374 1.10e-08

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 56.89  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 101 FGDADVKGRYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVrdgdhyVVSGSKQfisgGGE--------NEVYVTM--V 170
Cdd:PRK13026 174 YGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGI------VCRGEFE----GEEvlglrltwDKRYITLapV 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 171 RT---------------GEDGPKGISCLVIDKDTPGVSFGANERKLG--WHSQPTRQvmfDNVRIPVANRLGAE---GEG 230
Cdd:PRK13026 244 ATvlglafklrdpdgllGDKKELGITCALIPTDHPGVEIGRRHNPLGmaFMNGTTRG---KDVFIPLDWIIGGPdyaGRG 320

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 231 FRIAMMGLDGGR-LNIGACSLGGAQRCLDEAVAYVKDRRQFGKAIAEFQNTQFTLADMAteleaARALLYLAAAKVTDNA 309
Cdd:PRK13026 321 WRMLVECLSAGRgISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIA-----GNTYLLEAARRLTTTG 395

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 310 PDKTR----FAAMAKRLATDTGSSVVDRALQLHGGYG-------YL----MDYPIerfwrdlrvhSI-LEGTNQVMR--M 371
Cdd:PRK13026 396 LDLGVkpsvVTAIAKYHMTELARDVVNDAMDIHAGKGiqlgpknYLghayMAVPI----------AItVEGANILTRnlM 465


                 ...
gi 494645808 372 IVG 374
Cdd:PRK13026 466 IFG 468
sulfur_SfnB TIGR04022
sulfur acquisition oxidoreductase, SfnB family; Members of this protein family belong to the ...
 12-359 3.81e-08

sulfur acquisition oxidoreductase, SfnB family; Members of this protein family belong to the greater family of acyl-CoA dehydrogenases. This family includes the sulfate starvation induced protein SfnB of Pseudomonas putida strain DS1, which is both encoded nearby to and phylogenetically closely correlated with the dimethyl sulphone monooxygenase SfnG. This family shows considerable sequence similarity to the Rhodococcus dibenzothiophene desulfurization enzyme DszC, although that enzyme falls outside of the scope of this family. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 274924 [Multi-domain]  Cd Length: 391  Bit Score: 54.58  E-value: 3.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   12 EIQDLARRFtADRITPFAAEWDEKHIFPRDTIREAAELGFAAIYVSEESGGIALGRLEAALIMEAMAYGCPSTSAFISIH 91
Cdd:TIGR04022   9 EALEIARRL-AAEFAPGAAERDRERRLPWAELDAFSQSGLWGITVPRAYGGAGVSYATLAEVIAIISAADPSLGQIPQNH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808   92 NMASWMIDRFGDADVKGRYLPDLVTMDRMASyCLTEPGSgSDAAALKTRAVRDGDHYVVSGSKqFISGGGENEVYVTMVR 171
Cdd:TIGR04022  88 FYALEVLRLTGSEEQKRFFFGEVLAGERFGN-AFSERGT-RNVLDFQTRLRRDGDGYRLNGRK-FYSTGALFAHWIPVLA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  172 TGEDGPKGISclVIDKDTPGV-------SFGanerklgwhsQPTR---QVMFDNVRIPVAN---------RLGAEGEGFR 232
Cdd:TIGR04022 165 LDDEGRAVLA--FVPRDAPGLtviddwsGFG----------QRTTasgTVLLDDVRVPAEHvvpiqrafdRPTAAGPVAQ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808  233 IAMMGLDggrlnigacsLGGAQRCLDEAVAYVKDR-RQFGKAIAEFQN----TQFTLADMATELEAARALLYLAAAKVtD 307
Cdd:TIGR04022 233 IIHAAID----------AGIARAALADTLAFVRERaRPWIDSGVERASddplTIAEVGDLAIRLHAAEALLERAGRAV-D 301

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494645808  308 NA---PDKTRFA------AMAKRLATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVH 359
Cdd:TIGR04022 302 AAraePTEESVAaasiavAEAKVLTTEIALLAASKLFELAGTRSTLAEHNLDRHWRNARTH 362
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 109-379 1.26e-06

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 50.23  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 109 RYLPDLVTMDRMASYCLTEPGSGSDAAALKTRAVRD--GDHYV-----VSGSKqFISG--GGENE---VYVTMVRTGEDg 176
Cdd:PTZ00460 117 LWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDkqTNEFVihtpsVEAVK-FWPGelGFLCNfalVYAKLIVNGKN- 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 177 pKGISCLVI---DKDT----PGVSFGANERKLGWHSQPTRQVMFDNVRIPVANRLGaegegfRIAMMGLDG-----GRLN 244
Cdd:PTZ00460 195 -KGVHPFMVrirDKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLA------RYIKVSEDGqverqGNPK 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 245 IGACSL------------GGAQRCLDEAVAYVKDRRQFGK------AIAEFQNTQFTLADMATELEAARALLYLAAAKVT 306
Cdd:PTZ00460 268 VSYASMmymrnliidqypRFAAQALTVAIRYSIYRQQFTNdnkqenSVLEYQTQQQKLLPLLAEFYACIFGGLKIKELVD 347

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494645808 307 DN--APDKTRFAAMAKRLATDTGSS------VVDRA--LQLH-GGYGYLMDYPIERFWRDLRVHSILEGTNQVMRMIVGR 375
Cdd:PTZ00460 348 DNfnRVQKNDFSLLQLTHAILSAAKanytyfVSNCAewCRLScGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQLAR 427


                 ....
gi 494645808 376 DLLK 379
Cdd:PTZ00460 428 YLLK 431
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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