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Conserved domains on  [gi|522125288|ref|WP_020636497|]
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acyl-CoA dehydrogenase family protein [Amycolatopsis alba]

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 ...
 3-377 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: 631.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   3 LTDEQRALRETAAEFAAEHLAPHAIEWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCPSLA 82
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  83 AYISIHNMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGISDV 162
Cdd:cd01162   81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 163 HVVLARTGGPGARGISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEGNGFRVAMSALDGGRLNI 242
Cdd:cd01162  161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 243 SACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATQLSAMAKRFCTD 322
Cdd:cd01162  241 ASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATD 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 522125288 323 TGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRMLQE 377
Cdd:cd01162  321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
 
Name Accession Description Interval E-value
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 3-377 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: 631.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   3 LTDEQRALRETAAEFAAEHLAPHAIEWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCPSLA 82
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  83 AYISIHNMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGISDV 162
Cdd:cd01162   81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 163 HVVLARTGGPGARGISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEGNGFRVAMSALDGGRLNI 242
Cdd:cd01162  161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 243 SACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATQLSAMAKRFCTD 322
Cdd:cd01162  241 ASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATD 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 522125288 323 TGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRMLQE 377
Cdd:cd01162  321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-379 1.14e-164

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: 465.85  E-value: 1.14e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   1 MRLTDEQRALRETAAEFAAEHLAPHAIEWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCPS 80
Cdd:COG1960    3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  81 LAAYISIHNMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGIS 160
Cdd:COG1960   83 LALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 161 DVHVVLARTGG-PGARGISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEGNGFRVAMSALDGGR 239
Cdd:COG1960  163 DVILVLARTDPaAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 240 LNISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATqLSAMAKRF 319
Cdd:COG1960  243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAAL-EAAMAKLF 321

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 320 CTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRMLQEAS 379
Cdd:COG1960  322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 3-377 1.37e-66

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 216.28  E-value: 1.37e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   3 LTDEQRALRETAAEFAAEHLAPHAIEWDQAKHFP--VDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCPS 80
Cdd:PLN02519  26 FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  81 LAAYISIH-NMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGI 159
Cdd:PLN02519 106 VGLSYGAHsNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 160 SDVHVVLARTG-GPGARGISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEGNGFRVAMSALDGG 238
Cdd:PLN02519 186 AQTLVVYAKTDvAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLE 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 239 RLNISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHG----EDTATQLSA 314
Cdd:PLN02519 266 RLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGkvdrKDCAGVILC 345

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522125288 315 MAKRfctdtGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRMLQE 377
Cdd:PLN02519 346 AAER-----ATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 225-374 1.45e-48

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: 161.27  E-value: 1.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  225 GNGFRVAMSALDGGRLNISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDH 304
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  305 GEDTATQlSAMAKRFCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRM 374
Cdd:pfam00441  81 GGPDGAE-ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
 
Name Accession Description Interval E-value
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 3-377 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: 631.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   3 LTDEQRALRETAAEFAAEHLAPHAIEWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCPSLA 82
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  83 AYISIHNMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGISDV 162
Cdd:cd01162   81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 163 HVVLARTGGPGARGISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEGNGFRVAMSALDGGRLNI 242
Cdd:cd01162  161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 243 SACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATQLSAMAKRFCTD 322
Cdd:cd01162  241 ASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATD 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 522125288 323 TGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRMLQE 377
Cdd:cd01162  321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-379 1.14e-164

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: 465.85  E-value: 1.14e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   1 MRLTDEQRALRETAAEFAAEHLAPHAIEWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCPS 80
Cdd:COG1960    3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  81 LAAYISIHNMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGIS 160
Cdd:COG1960   83 LALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 161 DVHVVLARTGG-PGARGISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEGNGFRVAMSALDGGR 239
Cdd:COG1960  163 DVILVLARTDPaAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 240 LNISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATqLSAMAKRF 319
Cdd:COG1960  243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAAL-EAAMAKLF 321

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 320 CTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRMLQEAS 379
Cdd:COG1960  322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 5-375 4.84e-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: 415.90  E-value: 4.84e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   5 DEQRALRETAAEFAAEHLAPHAIEWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCPSLAAY 84
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  85 ISIHN-MVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGISDVH 163
Cdd:cd01158   81 VSVHNsLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 164 VVLARTGGP-GARGISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEGNGFRVAMSALDGGRLNI 242
Cdd:cd01158  161 IVFAVTDPSkGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 243 SACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATQlSAMAKRFCTD 322
Cdd:cd01158  241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKE-AAMAKLFASE 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 522125288 323 TGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRML 375
Cdd:cd01158  320 VAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLL 372
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 5-372 8.69e-125

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: 362.37  E-value: 8.69e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   5 DEQRALRETAAEFAAEHLAPHAIEWDQAKHFPVDVLRKAAQLgmggvylpedlggsalgrldgvlvfealatgcpslaay 84
Cdd:cd00567    1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLL-------------------------------------- 42

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  85 isihnMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGISDVHV 164
Cdd:cd00567   43 -----LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 165 VLARTG--GPGARGISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEGNGFRVAMSALDGGRLNI 242
Cdd:cd00567  118 VLARTDeeGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 243 SACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATQLSAMAKRFCTD 322
Cdd:cd00567  198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATE 277

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 522125288 323 TGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISR 372
Cdd:cd00567  278 AAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 6-375 5.46e-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: 5.46e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   6 EQRALRETAAEFAAEHLAPHAIEWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALA-TGCPSLAay 84
Cdd:cd01160    2 EHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELArAGGSGPG-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  85 ISIHN-MVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGISDVH 163
Cdd:cd01160   80 LSLHTdIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 164 VVLARTGGP--GARGISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEGNGFRVAMSALDGGRLN 241
Cdd:cd01160  160 IVVARTGGEarGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 242 ISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGE-DTATqlSAMAKRFC 320
Cdd:cd01160  240 IAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRlDVAE--ASMAKYWA 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 522125288 321 TDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRML 375
Cdd:cd01160  318 TELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 3-376 1.46e-103

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: 310.50  E-value: 1.46e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   3 LTDEQRALRETAAEFAAEHLAPHAIEWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCPSLA 82
Cdd:cd01156    2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  83 AYISIH-NMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGISD 161
Cdd:cd01156   82 LSYGAHsNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 162 VHVVLARTGG-PGARGISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEGNGFRVAMSALDGGRL 240
Cdd:cd01156  162 TLVVYAKTDPsAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 241 NISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATQlSAMAKRFC 320
Cdd:cd01156  242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKD-AAGVILYA 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 522125288 321 TDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRMLQ 376
Cdd:cd01156  321 AEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 3-375 2.26e-102

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: 307.20  E-value: 2.26e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   3 LTDEQRALRETAAEFAAEHLAPHAIEWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCPSLA 82
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  83 AYISIHNMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGISDV 162
Cdd:cd01157   81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 163 HVVLARTG----GPGARGISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEGNGFRVAMSALDGG 238
Cdd:cd01157  161 YFLLARSDpdpkCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 239 RLNISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTaTQLSAMAKR 318
Cdd:cd01157  241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRN-TYYASIAKA 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 522125288 319 FCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRML 375
Cdd:cd01157  320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 3-378 4.76e-93

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: 284.75  E-value: 4.76e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   3 LTDEQRALRETAAEFAAEHLAPHAIewDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCpSLA 82
Cdd:cd01161   27 QTEELNMLVGPVEKFFEEVNDPAKN--DQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDL-GFS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  83 AYISIHNMVATM-IDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARR--EGDEYVLDGVKQFISGAGI 159
Cdd:cd01161  104 VTLGAHQSIGFKgILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWITNGGI 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 160 SDVHVVLART-----GGPGARGISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEGNGFRVAMSA 234
Cdd:cd01161  184 ADIFTVFAKTevkdaTGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNI 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 235 LDGGRLNISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATQL-S 313
Cdd:cd01161  264 LNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQIeA 343

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522125288 314 AMAKRFCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRMLQEA 378
Cdd:cd01161  344 AISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHA 408
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 3-372 1.72e-75

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: 238.80  E-value: 1.72e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   3 LTDEQRALRETAAEFAAEHLAPHAIEWDQAKHFPVDVLRKAAQLGMGGVyLPEDLGGSALGRLDGVLVFEALATGCPSLA 82
Cdd:cd01151   13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVERVDSGYR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  83 AYISIH-NMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGISD 161
Cdd:cd01151   92 SFMSVQsSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 162 VHVVLARTGGPGarGISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGeGNGFRVAMSALDGGRLN 241
Cdd:cd01151  172 VFVVWARNDETG--KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPG-AEGLRGPFKCLNNARYG 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 242 ISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATQLSaMAKRFCT 321
Cdd:cd01151  249 IAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQIS-LLKRNNC 327

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 522125288 322 DTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISR 372
Cdd:cd01151  328 GKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGR 378
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 3-377 1.37e-66

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 216.28  E-value: 1.37e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   3 LTDEQRALRETAAEFAAEHLAPHAIEWDQAKHFP--VDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCPS 80
Cdd:PLN02519  26 FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  81 LAAYISIH-NMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGI 159
Cdd:PLN02519 106 VGLSYGAHsNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 160 SDVHVVLARTG-GPGARGISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEGNGFRVAMSALDGG 238
Cdd:PLN02519 186 AQTLVVYAKTDvAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLE 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 239 RLNISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHG----EDTATQLSA 314
Cdd:PLN02519 266 RLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGkvdrKDCAGVILC 345

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522125288 315 MAKRfctdtGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRMLQE 377
Cdd:PLN02519 346 AAER-----ATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
PRK12341 PRK12341
acyl-CoA dehydrogenase;
2-377 3.47e-65

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 211.90  E-value: 3.47e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   2 RLTDEQRALRETAAEFAAEHlAPHAI--EWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALA-TGC 78
Cdd:PRK12341   4 SLTEEQELLLASIRELITRN-FPEEYfrTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSkCGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  79 PslaAYI-----SIHNMVatmidKFGDDAQRhrylpRMSTMDTFG----SYCL--TEPDAGSDAAALSTRA-RREGDEYv 146
Cdd:PRK12341  83 P---AFLitngqCIHSMR-----RFGSAEQL-----RKTAESTLEtgdpAYALalTEPGAGSDNNSATTTYtRKNGKVY- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 147 LDGVKQFISGAGISDVHVVLARTGGPGA--RGISAFIVDRDTPGVSFGPNEiKMGWNAQPTRQVIFDGARVPASALLGGE 224
Cdd:PRK12341 149 LNGQKTFITGAKEYPYMLVLARDPQPKDpkKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEE 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 225 GNGFRVAMSALDGGRLNISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDH 304
Cdd:PRK12341 228 GMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADN 307

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522125288 305 GEDTATQlSAMAKRFCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRMLQE 377
Cdd:PRK12341 308 GQSLRTS-AALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKD 379
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 12-365 2.58e-62

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: 205.32  E-value: 2.58e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  12 ETAAEFAAEHLAPHAIEWDQ--------AKHFP---VDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCPS 80
Cdd:cd01153    3 EEVARLAENVLAPLNADGDRegpvfddgRVVVPppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  81 LAAYISIHNMVATMIdKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGD-EYVLDGVKQFISgAGI 159
Cdd:cd01153   83 LMYASGTQGAAATLL-AHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFIS-AGE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 160 SD-----VHVVLARTGG--PGARGISAFIV-----DRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPasaLLGGEGNG 227
Cdd:cd01153  161 HDmseniVHLVLARSEGapPGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 228 FRVAMSALDGGRLNISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQF--------RLADMRTDLEAARTL---LW 296
Cdd:cd01153  238 LAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVTIihhpdvrrSLMTQKAYAEGSRALdlyTA 317

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522125288 297 RAAD----ALDHGEDTATQ------LSAMAKRFCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEI 365
Cdd:cd01153  318 TVQDlaerKATEGEDRKALsaladlLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 4-377 3.96e-60

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 199.78  E-value: 3.96e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   4 TDEQRALRETAAEFAAEHLAPHAIEWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCPSLA- 82
Cdd:PTZ00461  38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCl 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  83 AYISiHNMVatMIDKF---GDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDE-YVLDGVKQFISGAG 158
Cdd:PTZ00461 118 AYLA-HSML--FVNNFyysASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGnYVLNGSKIWITNGT 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 159 ISDVHVVLARTGGPgargISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEGNGFRVAMSALDGG 238
Cdd:PTZ00461 195 VADVFLIYAKVDGK----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELE 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 239 RLNISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATQlSAMAKR 318
Cdd:PTZ00461 271 RVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLG-SDAAKL 349

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 522125288 319 FCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRMLQE 377
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKG 408
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 5-376 1.24e-54

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: 184.47  E-value: 1.24e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   5 DEQRALRETAAEFAAEHLAP-----HAIEWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCP 79
Cdd:cd01152    1 PSEEAFRAEVRAWLAAHLPPelreeSALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  80 SLAAYISIHNMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGI 159
Cdd:cd01152   81 PVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 160 SDVHVVLARTG--GPGARGISAFIVDRDTPGVSFGPNEIKMGwnAQPTRQVIFDGARVPASALLGGEGNGFRVAMSALDG 237
Cdd:cd01152  161 ADWAWLLVRTDpeAPKHRGISILLVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNF 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 238 GRLNIsacsLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATQlSAMAK 317
Cdd:cd01152  239 ERVSI----GGSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAE-ASIAK 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522125288 318 RFCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDL--------RVHQILEGTNEIMRVIISRRMLQ 376
Cdd:cd01152  314 LFGSELAQELAELALELLGTAALLRDPAPGAELAGRweadylrsRATTIYGGTSEIQRNIIAERLLG 380
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 2-377 2.31e-52

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 178.49  E-value: 2.31e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   2 RLTDEQRALRETAAEF-AAEHLAPHAIEWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALA-TGCP 79
Cdd:PRK03354   4 NLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGrLGAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  80 SLAAYiSIHNMVATMIdKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGI 159
Cdd:PRK03354  84 TYVLY-QLPGGFNTFL-REGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 160 SDVHVVLARTGGPGARGI-SAFIVDRDTPGVSFGPNEiKMGWNAQPTRQVIFDGARVPASALLGGEGNGFRVAMSALDGG 238
Cdd:PRK03354 162 TPYIVVMARDGASPDKPVyTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 239 RLNISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATQlSAMAKR 318
Cdd:PRK03354 241 RFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGD-AAMCKY 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 522125288 319 FCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRMLQE 377
Cdd:PRK03354 320 FCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 225-374 1.45e-48

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: 161.27  E-value: 1.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  225 GNGFRVAMSALDGGRLNISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDH 304
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  305 GEDTATQlSAMAKRFCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRM 374
Cdd:pfam00441  81 GGPDGAE-ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 9-376 1.94e-48

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: 168.34  E-value: 1.94e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   9 ALRETAAEFAAEHLAPHAIE----------WDQAKHFPVDVLR-KAAQLGMGGVYLPEDLGGSALGRLD--------GVL 69
Cdd:cd01155    5 ELRARVKAFMEEHVYPAEQEfleyyaeggdRWWTPPPIIEKLKaKAKAEGLWNLFLPEVSGLSGLTNLEyaylaeetGRS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  70 VFEALATGCpslaAYISIHNMvaTMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPD-AGSDAAALSTRARREGDEYVLD 148
Cdd:cd01155   85 FFAPEVFNC----QAPDTGNM--EVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVIN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 149 GVKQFISGAGISD--VHVVLARTGGPGA---RGISAFIVDRDTPGVSFGPNEIKMGWNAQPT--RQVIFDGARVPASALL 221
Cdd:cd01155  159 GRKWWSSGAGDPRckIAIVMGRTDPDGAprhRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHghAEITFDNVRVPASNLI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 222 GGEGNGFRVAMSALDGGRLNISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADA 301
Cdd:cd01155  239 LGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHM 318

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522125288 302 LD-HGEDTATQLSAMAKRFCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRMLQ 376
Cdd:cd01155  319 IDtVGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
PLN02526 PLN02526
acyl-coenzyme A oxidase
 3-379 7.59e-43

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 154.24  E-value: 7.59e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   3 LTDEQRALRETAAEFAAEHLAPHAIE-WDQAKhFPVDVLRKAAQLGMGGVYLpEDLGGSALGRLDGVLVFEALATGCPSL 81
Cdd:PLN02526  29 LTPEEQALRKRVRECMEKEVAPIMTEyWEKAE-FPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVARVDASC 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  82 AAYISIHNMVATM-IDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGDEYVLDGVKQFISGAGIS 160
Cdd:PLN02526 107 STFILVHSSLAMLtIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFA 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 161 DVHVVLARTggPGARGISAFIVDRDTPGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEgNGFRVAMSALDGGRL 240
Cdd:PLN02526 187 DVLVIFARN--TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAVSRV 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 241 NISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATQLSaMAKRFC 320
Cdd:PLN02526 264 MVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHAS-LGKAWI 342

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 522125288 321 TDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRMLQEAS 379
Cdd:PLN02526 343 TKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIAS 401
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 77-374 3.13e-42

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: 152.53  E-value: 3.13e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  77 GCPslaayISIHNMVATMIDKFGDDAQRHrYLPRMSTMDT----FGSYCLTEPDAGSDAAALSTRARR-EGDEYVLDGVK 151
Cdd:cd01154  110 LCP-----LTMTDAAVYALRKYGPEELKQ-YLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 152 QFISGAgISDVHVVLARTGG--PGARGISAFIVDRDTPGVSFGPNEI-----KMGWNAQPTRQVIFDGArvpASALLGGE 224
Cdd:cd01154  184 WFASAP-LADAALVLARPEGapAGARGLSLFLVPRLLEDGTRNGYRIrrlkdKLGTRSVATGEVEFDDA---EAYLIGDE 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 225 GNGFRVAMSALDGGRLNISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDH 304
Cdd:cd01154  260 GKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDR 339

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522125288 305 GEDT-------ATQLSAMAKRFCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRM 374
Cdd:cd01154  340 AAADkpveahmARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVL 416
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 4-115 3.52e-41

Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.


Pssm-ID: 460686 [Multi-domain]  Cd Length: 113  Bit Score: 140.68  E-value: 3.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288    4 TDEQRALRETAAEFAAEHLAPHAIEWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCPSLAA 83
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 522125288   84 YISIHN-MVATMIDKFGDDAQRHRYLPRMSTMD 115
Cdd:pfam02771  81 ALSVHSsLGAPPILRFGTEEQKERYLPKLASGE 113
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 9-375 1.00e-35

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 137.69  E-value: 1.00e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   9 ALRETAAEFAAEHLAP-------HAIEWDQAKHFPVDVLRKAA--QLGMGG---VYLPEDLGGSALGRLDGVLVFEALAT 76
Cdd:PTZ00456  62 SLLEEASKLATQTLLPlyessdsEGCVLLKDGNVTTPKGFKEAyqALKAGGwtgISEPEEYGGQALPLSVGFITRELMAT 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  77 GCPSLAAY--ISIHNMVATMIdkFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRARREGD-EYVLDGVKQF 153
Cdd:PTZ00456 142 ANWGFSMYpgLSIGAANTLMA--WGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIF 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 154 ISgAGISD-----VHVVLARTGG--PGARGISAFIVDRDTP----------GVSFGPNEIKMGWNAQPTRQVIFDGArvp 216
Cdd:PTZ00456 220 IS-AGDHDlteniVHIVLARLPNslPTTKGLSLFLVPRHVVkpdgsletakNVKCIGLEKKMGIKGSSTCQLSFENS--- 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 217 ASALLGGEGNGFRVAMSALDGGRLNISACSLGGAEAALGMAVRH----LSERSAFGEKLSEKQALQF-RLADMRTDL--- 288
Cdd:PTZ00456 296 VGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYarerRSMRALSGTKEPEKPADRIiCHANVRQNIlfa 375

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 289 ----EAARTLLWRAADALD--HGEDTATQLSAM----------AKRFCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRD 352
Cdd:PTZ00456 376 kavaEGGRALLLDVGRLLDihAAAKDAATREALdheigfytpiAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRD 455

                        410       420
                 ....*....|....*....|....
gi 522125288 353 LRVHQILEGTNEIMRV-IISRRML 375
Cdd:PTZ00456 456 ARIGTLYEGTTGIQALdFIGRKVL 479
PLN02876 PLN02876
acyl-CoA dehydrogenase
 97-378 4.66e-32

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 127.99  E-value: 4.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  97 KFGDDAQRHRYLPRMSTMDTFGSYCLTEPD-AGSDAAALSTRARREGDEYVLDGVKQFISGA--GISDVHVVLART--GG 171
Cdd:PLN02876 531 RYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTdfNA 610

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 172 PGARGISAFIVDRDTPGVSFGPNEIKMGWNAQPT--RQVIFDGARVPASALLGGEGNGFRVAMSALDGGRLNISACSLGG 249
Cdd:PLN02876 611 PKHKQQSMILVDIQTPGVQIKRPLLVFGFDDAPHghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGA 690

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 250 AEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALD-HGEDTATQLSAMAKRFCTDTGFEVA 328
Cdd:PLN02876 691 AERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDrLGNKKARGIIAMAKVAAPNMALKVL 770

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 522125288 329 NQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEIMRVIISRRMLQEA 378
Cdd:PLN02876 771 DMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKLELQRA 820
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 119-211 2.75e-30

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: 111.60  E-value: 2.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  119 SYCLTEPDAGSDAAALSTRA-RREGDEYVLDGVKQFISGAGISDVHVVLARTGGP-GARGISAFIVDRDTPGVSFGPNEI 196
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDdRHGGISLFLVPKDAPGVSVRRIET 80

                          90
                  ....*....|....*
gi 522125288  197 KMGWNAQPTRQVIFD 211
Cdd:pfam02770  81 KLGVRGLPTGELVFD 95
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 72-366 1.56e-19

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: 90.08  E-value: 1.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  72 EALATGCPSLAAYISIH-NMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRAR--REGDEYVLD 148
Cdd:cd01150   89 NSLGGYDLSLGAKLGLHlGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATydPLTQEFVIN 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 149 -----GVKQFISGAGISDVH-VVLARTGGPGAR-GISAFIV---DRDT----PGVSFGPNEIKMGWNAQPTRQVIFDGAR 214
Cdd:cd01150  169 tpdftATKWWPGNLGKTATHaVVFAQLITPGKNhGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVR 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 215 VPASALLGGEGN----------------GFRVAMSALDGGRLNISACSLGGAEAALGMAVRHLSERSAFGEK--LSEKQA 276
Cdd:cd01150  249 IPRENLLNRFGDvspdgtyvspfkdpnkRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKpsDPEVQI 328

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 277 LQFRLADMRTDLEAARTLLWRAA------------DALDHGEDTATQ----LSAMAKRFCTDTGFEVANQALQLHGGYGY 340
Cdd:cd01150  329 LDYQLQQYRLFPQLAAAYAFHFAakslvemyheiiKELLQGNSELLAelhaLSAGLKAVATWTAAQGIQECREACGGHGY 408

                        330       340
                 ....*....|....*....|....*.
gi 522125288 341 LAEYGLEKIVRDLRVHQILEGTNEIM 366
Cdd:cd01150  409 LAMNRLPTLRDDNDPFCTYEGDNTVL 434
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 122-366 3.66e-19

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 89.04  E-value: 3.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 122 LTEPDAGSDAAALSTRARR-EGDEYVLDGVKQFISgAGISDVHVVLARTGGpgarGISAFIVDRDTP-----GVSFGPNE 195
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERlADGSYRLVGHKWFFS-VPQSDAHLVLAQAKG----GLSCFFVPRFLPdgqrnAIRLERLK 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 196 IKMGWNAQPTRQVIFDGArvpASALLGGEGNGFRVAMSALDGGRLNISACSLGGAEAALGMAVRHLSERSAFGEKLSEKQ 275
Cdd:PRK11561 259 DKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQP 335

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 276 ALQFRLADMRTDLEAARTLLWRAADALDHGEDTATQLSA-----MAKRFCTDTGFEVANQALQLHGGYGYLAEYGLEKIV 350
Cdd:PRK11561 336 LMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEALWArlftpAAKFVICKRGIPFVAEAMEVLGGIGYCEESELPRLY 415

                        250
                 ....*....|....*.
gi 522125288 351 RDLRVHQILEGTNEIM 366
Cdd:PRK11561 416 REMPVNSIWEGSGNIM 431
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 8-356 7.96e-19

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: 86.99  E-value: 7.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   8 RALRETAAEFAAEhlaphAIEWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCPSLAAYISI 87
Cdd:cd01163    1 ARARPLAARIAEG-----AAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  88 HNMVATMIDKFGDDAQRHRYLPRMSTMDTFGSyCLTEPDaGSDAAALSTRARREGDEYVLDGVKQFISGAGISDVHVVLA 167
Cdd:cd01163   76 HFGFVEALLLAGPEQFRKRWFGRVLNGWIFGN-AVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 168 RTggPGARGISAfIVDRDTPGVSFGPNeikmgWNAQPTRQ-----VIFDGARVPASALLGG----EGNGFRVAMSaldgg 238
Cdd:cd01163  154 LD--EEGKLVFA-AVPTDRPGITVVDD-----WDGFGQRLtasgtVTFDNVRVEPDEVLPRpnapDRGTLLTAIY----- 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 239 RLNISACSLGGAEAALGMAVRHLSERS-----AFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALD-----HGEDT 308
Cdd:cd01163  221 QLVLAAVLAGIARAALDDAVAYVRSRTrpwihSGAESARDDPYVQQVVGDLAARLHAAEALVLQAARALDaaaaaGTALT 300

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 522125288 309 ATQL------SAMAKRFCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVH 356
Cdd:cd01163  301 AEARgeaalaVAAAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNARTH 354
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 97-339 1.61e-18

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 87.18  E-value: 1.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  97 KFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALS-----TRARREGDEyVLdGV-----KQFISGAGISDVhVVL 166
Cdd:PRK09463 174 HYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEE-VL-GMrltwnKRYITLAPIATV-LGL 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 167 A-RT-------GGPGARGISAFIVDRDTPGVSFGPNEIKMGWNAQ--PTR-QVIFdgarVPASALLGGE---GNGFRVAM 232
Cdd:PRK09463 251 AfKLydpdgllGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQngPTRgKDVF----IPLDYIIGGPkmaGQGWRMLM 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 233 SALDGGRlNIS--ACSLGGAEAALGMAVRHLSERSAFGEKLSEKQALQFRLADMRTD---LEAARTLlwrAADALDHGED 307
Cdd:PRK09463 327 ECLSVGR-GISlpSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTL---TTAAVDLGEK 402

                        250       260       270
                 ....*....|....*....|....*....|..
gi 522125288 308 TATqLSAMAKRFCTDTGFEVANQALQLHGGYG 339
Cdd:PRK09463 403 PSV-LSAIAKYHLTERGRQVINDAMDIHGGKG 433
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 2-339 1.70e-17

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 84.24  E-value: 1.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288   2 RLTDEQRALRETAAEFAAEHLAPHAIEWdQAKHFPVDV---LRKAAQLGMggvYLPEDLGGSALGRLDGVLVFEALATgc 78
Cdd:PRK13026  77 TLTAEEQAFIDNEVETLLTMLDDWDIVQ-NRKDLPPEVwdyLKKEGFFAL---IIPKEYGGKGFSAYANSTIVSKIAT-- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  79 PSLAAYISIhnMV------ATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALS-----TRARREGDEyVL 147
Cdd:PRK13026 151 RSVSAAVTV--MVpnslgpGELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEE-VL 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 148 dGV-----KQFISGAGISDVhVVLA--------RTGGPGARGISAFIVDRDTPGVSFGP--NEIKMGWNAQPTR-QVIFd 211
Cdd:PRK13026 228 -GLrltwdKRYITLAPVATV-LGLAfklrdpdgLLGDKKELGITCALIPTDHPGVEIGRrhNPLGMAFMNGTTRgKDVF- 304

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 212 garVPASALLGGE---GNGFRVAMSALDGGRlNISACSLGgaeAALG-MAVRHLSE----RSAFG------EKLSEKQAl 277
Cdd:PRK13026 305 ---IPLDWIIGGPdyaGRGWRMLVECLSAGR-GISLPALG---TASGhMATRTTGAyayvRRQFGmpigqfEGVQEALA- 376

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522125288 278 qfRLADMRTDLEAARTLlwrAADALDHGEDTATqLSAMAKRFCTDTGFEVANQALQLHGGYG 339
Cdd:PRK13026 377 --RIAGNTYLLEAARRL---TTTGLDLGVKPSV-VTAIAKYHMTELARDVVNDAMDIHAGKG 432
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
242-364 1.25e-15

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 72.76  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  242 ISACSLGGAEAALGMAVRHLSERS--AFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATQLS------ 313
Cdd:pfam08028   2 IAAAALGAARAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKPVTpalrae 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 522125288  314 -AMAKRFCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNE 364
Cdd:pfam08028  82 aRRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 18-355 7.48e-14

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: 72.00  E-value: 7.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  18 AAEHLAP----HAIEWDQAKHFPVDVLRKAAQLGMGGVYLPEDLGGSALGRLDGVLVFEALATGCPSLAAYISIHNMVAT 93
Cdd:cd01159    2 RAEDLAPlireRAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATHSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  94 MIDKFGDDAQRhrylprmstmDTFGSycltEPDAG-SDAAALSTRARREGDEYVLDGVKQFISGAGISDVHVVLARTGGP 172
Cdd:cd01159   82 MLAAFPPEAQE----------EVWGD----GPDTLlAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDD 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 173 GARG-ISAFIVDRDtpGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALL-----------GGEGNGFRVAMSALDGgrL 240
Cdd:cd01159  148 DGGPlPRAFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtagdmmagdgpGGSTPVYRMPLRQVFP--L 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 241 NISACSLGGAEAALGMAVRHLSER---SAFGEKLSEKQALQFRLADMRTDLEAARTLLWRAADALDHGEDTATQLSAMAK 317
Cdd:cd01159  224 SFAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGGPIDVEER 303

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 522125288 318 R-------FCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRV 355
Cdd:cd01159  304 ArirrdaaYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHA 348
PLN02443 PLN02443
acyl-coenzyme A oxidase
 83-379 2.02e-06

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 49.84  E-value: 2.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  83 AYISIH-NMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRAR--REGDEYV-----LDGVKQFI 154
Cdd:PLN02443  97 GYTDLHwGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATfdPKTDEFVihsptLTSSKWWP 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 155 SGAGISDVH-VVLARTGGPGA-RGISAFIVDRDT-------PGVSFGPNEIKMG---WNAQPTRQVIFDGARVPASALLg 222
Cdd:PLN02443 177 GGLGKVSTHaVVYARLITNGKdHGIHGFIVQLRSlddhsplPGVTVGDIGMKFGngaYNTMDNGFLRFDHVRIPRDQML- 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 223 gegngFRVAMSALDGG------------------RLNISACSLGGAEAALGMAVRHLSERSAFGEKLS--EKQALQF--- 279
Cdd:PLN02443 256 -----MRLSKVTREGKyvqsdvprqlvygtmvyvRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGgpETQVIDYktq 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 280 --RLADMRTDLEAART----LLWRAADALDHGE--DTATQLSAMA-----KRFCTDTGFEVANQALQLHGGYGYLAEYGL 346
Cdd:PLN02443 331 qsRLFPLLASAYAFRFvgewLKWLYTDVTQRLEanDFSTLPEAHActaglKSLTTSATADGIEECRKLCGGHGYLCSSGL 410

                        330       340       350
                 ....*....|....*....|....*....|...
gi 522125288 347 EKIVRDLRVHQILEGTNEIMRVIISRRMLQEAS 379
Cdd:PLN02443 411 PELFAVYVPACTYEGDNVVLLLQVARFLMKTVS 443
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 50-235 2.26e-06

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 49.49  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  50 GVYLPEDLGGSALGRLDGVLVFEALATGCPSLAAYISIHNMVAT-MIDKFGDDAQRHRYLPRMSTMDTFGSYClTEPDAG 128
Cdd:PTZ00457  67 GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTyLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEEGCG 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 129 SDAAALSTRAR-REGDEYVLDGVKQFISGAGISDvHVVLART--------GGPGARGISAFIVDRDTPGVSFGPNEIKMg 199
Cdd:PTZ00457 146 SDISMNTTKASlTDDGSYVLTGQKRCEFAASATH-FLVLAKTltqtaaeeGATEVSRNSFFICAKDAKGVSVNGDSVVF- 223

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 522125288 200 wnaqptrqvifdgARVPASALLGGEGNGFRVAMSAL 235
Cdd:PTZ00457 224 -------------ENTPAADVVGVVGEGFKDAMITL 246
PLN02636 PLN02636
acyl-coenzyme A oxidase
 98-366 5.28e-06

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 48.32  E-value: 5.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  98 FGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRAR--REGDEYVLD-----GVKQFISGAGI-SDVHVVLAR- 168
Cdd:PLN02636 155 LGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATfdPLTDEFVINtpndgAIKWWIGNAAVhGKFATVFARl 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 169 ------TGGPGARGISAFIVD-RDT------PGVSFGPNEIKMGWNAQPTRQVIFDGARVPASALLGGEGN--------- 226
Cdd:PLN02636 235 klpthdSKGVSDMGVHAFIVPiRDMkthqvlPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDvsrdgkyts 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 227 -------GFRVAMSALDGGRLNISACSLGGAEAALGMAVRHLSERSAFG----EKLS--EKQALQFRLADMRTDLE---- 289
Cdd:PLN02636 315 slptinkRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGppkqPEISilDYQSQQHKLMPMLASTYafhf 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 290 AARTLLWRAAD-ALDHGEDTATQ---LSAMAKRFCTDTGFEVANQALQLHGGYGYLAEYGLEKIVRDLRVHQILEGTNEI 365
Cdd:PLN02636 395 ATEYLVERYSEmKKTHDDQLVADvhaLSAGLKAYITSYTAKALSTCREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTV 474


                 .
gi 522125288 366 M 366
Cdd:PLN02636 475 L 475
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 78-221 3.54e-05

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 45.61  E-value: 3.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  78 CPSLAAYISIH-NMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRAR--REGDEYVL-----DG 149
Cdd:PTZ00460  88 CPQGTFISTVHfAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATydKQTNEFVIhtpsvEA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 150 VKQFISGAG-ISDVHVVLARTGGPG-ARGISAFIV---DRDT----PGVSFGPNEIKMGWNAQPTRQVIFDGARVPASAL 220
Cdd:PTZ00460 168 VKFWPGELGfLCNFALVYAKLIVNGkNKGVHPFMVrirDKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSL 247


                 .
gi 522125288 221 L 221
Cdd:PTZ00460 248 L 248
PLN02312 PLN02312
acyl-CoA oxidase
 71-267 3.34e-03

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 39.37  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288  71 FEALATGCPSLAAYISIH-NMVATMIDKFGDDAQRHRYLPRMSTMDTFGSYCLTEPDAGSDAAALSTRAR--REGDEYVL 147
Cdd:PLN02312 139 LEVIGIYDHSLAIKLGVHfFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTydPKTEEFVI 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522125288 148 D-----GVKQFISGAGISDVH-VVLARTGGPGA-RGISAFIVD-RDT-----PGVSFGPNEIKMGWNAQPTRQVIFDGAR 214
Cdd:PLN02312 219 NtpcesAQKYWIGGAANHATHtIVFSQLHINGKnEGVHAFIAQiRDQdgnicPNIRIADCGHKIGLNGVDNGRIWFDNLR 298

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522125288 215 VPASALL--------GGE--------GNGFRVAMSALDGGRLNISACSLGGAEAALGMAVRHLSERSAF 267
Cdd:PLN02312 299 IPRENLLnsvadvspDGKyvsaikdpDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
 
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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