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Conserved domains on  [gi|1084606126|gb|OGO59742|]
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hypothetical protein A2025_02570 [Chloroflexi bacterium RBG_19FT_COMBO_47_15]

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 ...
 11-395 6.01e-130

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 cd01152:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 380  Bit Score: 378.61  E-value: 6.01e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  11 ALKEEIRKFAKAELPPDLVRNTViDGEFRDFEFEISMSRKLAQRGWLVMSWPEKYGGRSASLLEQTIYEMEIAYWGIPGA 90
Cdd:cd01152     5 AFRAEVRAWLAAHLPPELREESA-LGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  91 wMGISGTQWVGPCLMMFGTEEQREKYLPLIASGQKdgVWCTGYSEPNAGSDFANIRTRALRDGDDYIINGQKVWTSVAHR 170
Cdd:cd01152    84 -FNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEE--IWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 171 ARWCWLAVRTNPnAAKKHHGISIFIVDMKSPGVTVNPILNYYGRHHFNEVFFDNVRVPASNLVGEENKGWYYLMQSLAFE 250
Cdd:cd01152   161 ADWAWLLVRTDP-EAPKHRGISILLVDMDSPGVTVRPIRSINGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 251 RRSIApttyGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQGQIPVYESSRNKIM 330
Cdd:cd01152   240 RVSIG----GSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLF 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084606126 331 GDDLMRQGAITGADILGMYSQVDPDSEWAKLNGAIQGAYLGFPGQAIAAGTAEIEKSIIAQFRLG 395
Cdd:cd01152   316 GSELAQELAELALELLGTAALLRDPAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAERLLG 380
 
Name Accession Description Interval E-value
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 11-395 6.01e-130

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: 378.61  E-value: 6.01e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  11 ALKEEIRKFAKAELPPDLVRNTViDGEFRDFEFEISMSRKLAQRGWLVMSWPEKYGGRSASLLEQTIYEMEIAYWGIPGA 90
Cdd:cd01152     5 AFRAEVRAWLAAHLPPELREESA-LGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  91 wMGISGTQWVGPCLMMFGTEEQREKYLPLIASGQKdgVWCTGYSEPNAGSDFANIRTRALRDGDDYIINGQKVWTSVAHR 170
Cdd:cd01152    84 -FNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEE--IWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 171 ARWCWLAVRTNPnAAKKHHGISIFIVDMKSPGVTVNPILNYYGRHHFNEVFFDNVRVPASNLVGEENKGWYYLMQSLAFE 250
Cdd:cd01152   161 ADWAWLLVRTDP-EAPKHRGISILLVDMDSPGVTVRPIRSINGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 251 RRSIApttyGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQGQIPVYESSRNKIM 330
Cdd:cd01152   240 RVSIG----GSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLF 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084606126 331 GDDLMRQGAITGADILGMYSQVDPDSEWAKLNGAIQGAYLGFPGQAIAAGTAEIEKSIIAQFRLG 395
Cdd:cd01152   316 GSELAQELAELALELLGTAALLRDPAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAERLLG 380
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-398 1.96e-113

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: 336.43  E-value: 1.96e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126   1 MDFRLGEKELALKEEIRKFAKAELPPdlvRNTVIDGEfRDFEFEISmsRKLAQRGWLVMSWPEKYGGRSASLLEQTIYEM 80
Cdd:COG1960     1 MDFELTEEQRALRDEVREFAEEEIAP---EAREWDRE-GEFPRELW--RKLAELGLLGLTIPEEYGGLGLSLVELALVLE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  81 EIAYWGIPGAwMGISGTQWVGPCLMMFGTEEQREKYLPLIASGQKdgVWCTGYSEPNAGSDFANIRTRALRDGDDYIING 160
Cdd:COG1960    75 ELARADASLA-LPVGVHNGAAEALLRFGTEEQKERYLPRLASGEW--IGAFALTEPGAGSDAAALRTTAVRDGDGYVLNG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 161 QKVWTSVAHRARWCWLAVRTNPnaAKKHHGISIFIVDMKSPGVTVNPILNYYGRH--HFNEVFFDNVRVPASNLVGEENK 238
Cdd:COG1960   152 QKTFITNAPVADVILVLARTDP--AAGHRGISLFLVPKDTPGVTVGRIEDKMGLRgsDTGELFFDDVRVPAENLLGEEGK 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 239 GWYYLMQSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQGQ 318
Cdd:COG1960   230 GFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 319 IPVYESSRNKIMGDDLMRQGAITGADILGMYSQVDpDSEWAKLngaiqgaYLGFPGQAIAAGTAEIEKSIIAQFRLGLPK 398
Cdd:COG1960   310 DAALEAAMAKLFATEAALEVADEALQIHGGYGYTR-EYPLERL-------YRDARILTIYEGTNEIQRLIIARRLLGRPG 381
PRK12341 PRK12341
acyl-CoA dehydrogenase;
1-325 2.24e-45

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 160.66  E-value: 2.24e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126   1 MDFRLGEKELALKEEIRKFAKAELPPDLVRNTVIDGEFRDfEFeismSRKLAQRGWLVMSWPEKYGGRSASLLEQTIYEM 80
Cdd:PRK12341    1 MDFSLTEEQELLLASIRELITRNFPEEYFRTCDENGTYPR-EF----MRALADNGISMLGVPEEFGGTPADYVTQMLVLE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  81 EIAYWGIPGAWMGisgtqwVGPCL---MMFGTEEQREKYLpLIASGQKDGVWCTGYSEPNAGSDFANIRTRALRDGDDYI 157
Cdd:PRK12341   76 EVSKCGAPAFLIT------NGQCIhsmRRFGSAEQLRKTA-ESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVY 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 158 INGQKVWTSVAHRARWCwLAVRTNPNAAKKHHGISIFIVDMKSPGVTVNPiLNYYGRH--HFNEVFFDNVRVPASNLVGE 235
Cdd:PRK12341  149 LNGQKTFITGAKEYPYM-LVLARDPQPKDPKKAFTLWWVDSSKPGIKINP-LHKIGWHmlSTCEVYLDNVEVEESDLVGE 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 236 ENKGWYYLMQSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRIS 315
Cdd:PRK12341  227 EGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQAD 306

                         330
                  ....*....|
gi 1084606126 316 QGqIPVYESS 325
Cdd:PRK12341  307 NG-QSLRTSA 315
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 237-391 1.33e-23

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: 95.78  E-value: 1.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 237 NKGWYYLMQSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQ 316
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084606126 317 GQIPVYESSRNKIMGDDLMRQGAITGADILGMYSqVDPDSEWAKLngaiqgaYLGFPGQAIAAGTAEIEKSIIAQ 391
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYG-YLREYPVERL-------YRDARVLRIGEGTSEIQRNIIAR 147
 
Name Accession Description Interval E-value
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 11-395 6.01e-130

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: 378.61  E-value: 6.01e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  11 ALKEEIRKFAKAELPPDLVRNTViDGEFRDFEFEISMSRKLAQRGWLVMSWPEKYGGRSASLLEQTIYEMEIAYWGIPGA 90
Cdd:cd01152     5 AFRAEVRAWLAAHLPPELREESA-LGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  91 wMGISGTQWVGPCLMMFGTEEQREKYLPLIASGQKdgVWCTGYSEPNAGSDFANIRTRALRDGDDYIINGQKVWTSVAHR 170
Cdd:cd01152    84 -FNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEE--IWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 171 ARWCWLAVRTNPnAAKKHHGISIFIVDMKSPGVTVNPILNYYGRHHFNEVFFDNVRVPASNLVGEENKGWYYLMQSLAFE 250
Cdd:cd01152   161 ADWAWLLVRTDP-EAPKHRGISILLVDMDSPGVTVRPIRSINGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 251 RRSIApttyGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQGQIPVYESSRNKIM 330
Cdd:cd01152   240 RVSIG----GSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLF 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084606126 331 GDDLMRQGAITGADILGMYSQVDPDSEWAKLNGAIQGAYLGFPGQAIAAGTAEIEKSIIAQFRLG 395
Cdd:cd01152   316 GSELAQELAELALELLGTAALLRDPAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAERLLG 380
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-398 1.96e-113

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: 336.43  E-value: 1.96e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126   1 MDFRLGEKELALKEEIRKFAKAELPPdlvRNTVIDGEfRDFEFEISmsRKLAQRGWLVMSWPEKYGGRSASLLEQTIYEM 80
Cdd:COG1960     1 MDFELTEEQRALRDEVREFAEEEIAP---EAREWDRE-GEFPRELW--RKLAELGLLGLTIPEEYGGLGLSLVELALVLE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  81 EIAYWGIPGAwMGISGTQWVGPCLMMFGTEEQREKYLPLIASGQKdgVWCTGYSEPNAGSDFANIRTRALRDGDDYIING 160
Cdd:COG1960    75 ELARADASLA-LPVGVHNGAAEALLRFGTEEQKERYLPRLASGEW--IGAFALTEPGAGSDAAALRTTAVRDGDGYVLNG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 161 QKVWTSVAHRARWCWLAVRTNPnaAKKHHGISIFIVDMKSPGVTVNPILNYYGRH--HFNEVFFDNVRVPASNLVGEENK 238
Cdd:COG1960   152 QKTFITNAPVADVILVLARTDP--AAGHRGISLFLVPKDTPGVTVGRIEDKMGLRgsDTGELFFDDVRVPAENLLGEEGK 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 239 GWYYLMQSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQGQ 318
Cdd:COG1960   230 GFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 319 IPVYESSRNKIMGDDLMRQGAITGADILGMYSQVDpDSEWAKLngaiqgaYLGFPGQAIAAGTAEIEKSIIAQFRLGLPK 398
Cdd:COG1960   310 DAALEAAMAKLFATEAALEVADEALQIHGGYGYTR-EYPLERL-------YRDARILTIYEGTNEIQRLIIARRLLGRPG 381
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 104-391 5.82e-73

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: 231.02  E-value: 5.82e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 104 LMMFGTEEQREKYLPLIASGQKdgVWCTGYSEPNAGSDFANIRTRALRDGDDYIINGQKVWTSVAHRARWCWLAVRTNPN 183
Cdd:cd00567    48 LLAYGTEEQKERYLPPLASGEA--IAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEE 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 184 AAKkHHGISIFIVDMKSPGVTVNPILNYYGRHH--FNEVFFDNVRVPASNLVGEENKGWYYLMQSLAFERRSIAPTTYGN 261
Cdd:cd00567   126 GPG-HRGISAFLVPADTPGVTVGRIWDKMGMRGsgTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVALGA 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 262 LKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQGQIPV-YESSRNKIMGDDLMRQGAI 340
Cdd:cd00567   205 ARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEArLEAAMAKLFATEAAREVAD 284

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1084606126 341 TGADILGMYSqVDPDSewaklngAIQGAYLGFPGQAIAAGTAEIEKSIIAQ 391
Cdd:cd00567   285 LAMQIHGGRG-YSREY-------PVERYLRDARAARIAEGTAEIQRLIIAR 327
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 11-391 1.31e-67

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: 218.52  E-value: 1.31e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  11 ALKEEIRKFAKAELPP---DLVRNTVIDGEfrdfefeisMSRKLAQRGWLVMSWPEKYGGRSASLLEQTIYEMEIAYWGI 87
Cdd:cd01160     5 AFRDVVRRFFAKEVAPfhhEWEKAGEVPRE---------VWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  88 PGAWMGISgTQWVGPCLMMFGTEEQREKYLPLIASGQKDGVwcTGYSEPNAGSDFANIRTRALRDGDDYIINGQKVWTSV 167
Cdd:cd01160    76 SGPGLSLH-TDIVSPYITRAGSPEQKERVLPQMVAGKKIGA--IAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 168 AHRARWCWLAVRTNPNAaKKHHGISIFIVDMKSPGVTVNPILNYYGRHHFN--EVFFDNVRVPASNLVGEENKGWYYLMQ 245
Cdd:cd01160   153 GMLADVVIVVARTGGEA-RGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDtaELFFDDCRVPAENLLGEENKGFYYLMQ 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 246 SLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQGQIPVYESS 325
Cdd:cd01160   232 NLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEAS 311

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084606126 326 RNKIMGDDLMRQGAITGADILGmysqvdpdsEWAKLNGA-IQGAYLGFPGQAIAAGTAEIEKSIIAQ 391
Cdd:cd01160   312 MAKYWATELQNRVAYECVQLHG---------GWGYMREYpIARAYRDARVQPIYGGTTEIMKELISR 369
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 7-390 1.40e-60

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: 200.19  E-value: 1.40e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126   7 EKELALKEEIRKFAKAELPPdLVRNtvIDgefRDFEFEISMSRKLAQRGWLVMSWPEKYGGRSASLLEQTIYEMEIAYwG 86
Cdd:cd01158     1 EEHQMIRKTVRDFAEKEIAP-LAAE--MD---EKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAK-V 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  87 IPGAWMGISG-TQWVGPCLMMFGTEEQREKYLPLIASGQKDGvwCTGYSEPNAGSDFANIRTRALRDGDDYIINGQKVWT 165
Cdd:cd01158    74 DASVAVIVSVhNSLGANPIIKFGTEEQKKKYLPPLATGEKIG--AFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 166 SVAHRARWCWLAVRTNPnaAKKHHGISIFIVDMKSPGVTVNPILNYYGRHHFN--EVFFDNVRVPASNLVGEENKGWYYL 243
Cdd:cd01158   152 TNGGEADFYIVFAVTDP--SKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSttELIFEDVRVPKENILGEEGEGFKIA 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 244 MQSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQGQIPVYE 323
Cdd:cd01158   230 MQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKE 309

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084606126 324 SSRNKIMGDDLMRQGAITGADILGMYSQV-DPDSEW----AKLNgaiqgaylgfpgqAIAAGTAEIEKSIIA 390
Cdd:cd01158   310 AAMAKLFASEVAMRVTTDAVQIFGGYGYTkDYPVERyyrdAKIT-------------EIYEGTSEIQRLVIA 368
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 5-391 3.59e-56

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: 188.77  E-value: 3.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126   5 LGEKELALKEEIRKFAKAELPPdlvRNTVIDgefRDFEFEISMSRKLAQRGWLVMSWPEKYGGRSASLLEQTIYEMEIAY 84
Cdd:cd01156     2 LDDEIEMLRQSVREFAQKEIAP---LAAKID---RDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  85 wgiPGAWMGISGTQWVGPCLMMF---GTEEQREKYLPLIASGQKDGVWCTgySEPNAGSDFANIRTRALRDGDDYIINGQ 161
Cdd:cd01156    76 ---ASGSVALSYGAHSNLCINQIyrnGSAAQKEKYLPKLISGEHIGALAM--SEPNAGSDVVSMKLRAEKKGDRYVLNGS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 162 KVWTSVAHRARWCWLAVRTNPNAAKkhHGISIFIVDMKSPGVTVNPILNYYGRHHFN--EVFFDNVRVPASNLVGEENKG 239
Cdd:cd01156   151 KMWITNGPDADTLVVYAKTDPSAGA--HGITAFIVEKGMPGFSRAQKLDKLGMRGSNtcELVFEDCEVPEENILGGENKG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 240 WYYLMQSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQGQI 319
Cdd:cd01156   229 VYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNM 308

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084606126 320 PVYESSRNKIMGDDLMRQGAITGADILGMYSQVDpDSEWAKLngaIQGAYLGfpgqAIAAGTAEIEKSIIAQ 391
Cdd:cd01156   309 DPKDAAGVILYAAEKATQVALDAIQILGGNGYIN-DYPTGRL---LRDAKLY----EIGAGTSEIRRMVIGR 372
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 5-347 3.63e-47

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: 165.45  E-value: 3.63e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126   5 LGEKELALKEEIRKFAKAELPPdlvrntvIDGEF-RDFEFEISMSRKLAQRGWLVMSWPEKYGGRSASLLEQTIYEMEIA 83
Cdd:cd01157     1 LTEQQKEFQETARKFAREEIIP-------VAAEYdKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  84 YwGIPGAWMGISGTQWVGPCLMMFGTEEQREKYL------PLIASgqkdgvWCTgySEPNAGSDFANIRTRALRDGDDYI 157
Cdd:cd01157    74 Y-GCTGVQTAIEANSLGQMPVIISGNDEQKKKYLgrmteePLMCA------YCV--TEPGAGSDVAGIKTKAEKKGDEYI 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 158 INGQKVWTSVAHRARWCWLAVRTNPN----AAKKHHGisiFIVDMKSPGVTVnpilnyyGRHHFNE---------VFFDN 224
Cdd:cd01157   145 INGQKMWITNGGKANWYFLLARSDPDpkcpASKAFTG---FIVEADTPGIQP-------GRKELNMgqrcsdtrgITFED 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 225 VRVPASNLVGEENKGWYYLMQSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLK 304
Cdd:cd01157   215 VRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELAR 294

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1084606126 305 MFAFQLAWRISQGQIPVYESSRNKIMGDDLMRQGAITGADILG 347
Cdd:cd01157   295 LAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFG 337
PRK12341 PRK12341
acyl-CoA dehydrogenase;
1-325 2.24e-45

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 160.66  E-value: 2.24e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126   1 MDFRLGEKELALKEEIRKFAKAELPPDLVRNTVIDGEFRDfEFeismSRKLAQRGWLVMSWPEKYGGRSASLLEQTIYEM 80
Cdd:PRK12341    1 MDFSLTEEQELLLASIRELITRNFPEEYFRTCDENGTYPR-EF----MRALADNGISMLGVPEEFGGTPADYVTQMLVLE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  81 EIAYWGIPGAWMGisgtqwVGPCL---MMFGTEEQREKYLpLIASGQKDGVWCTGYSEPNAGSDFANIRTRALRDGDDYI 157
Cdd:PRK12341   76 EVSKCGAPAFLIT------NGQCIhsmRRFGSAEQLRKTA-ESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVY 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 158 INGQKVWTSVAHRARWCwLAVRTNPNAAKKHHGISIFIVDMKSPGVTVNPiLNYYGRH--HFNEVFFDNVRVPASNLVGE 235
Cdd:PRK12341  149 LNGQKTFITGAKEYPYM-LVLARDPQPKDPKKAFTLWWVDSSKPGIKINP-LHKIGWHmlSTCEVYLDNVEVEESDLVGE 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 236 ENKGWYYLMQSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRIS 315
Cdd:PRK12341  227 EGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQAD 306

                         330
                  ....*....|
gi 1084606126 316 QGqIPVYESS 325
Cdd:PRK12341  307 NG-QSLRTSA 315
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 50-331 2.06e-38

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: 142.61  E-value: 2.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  50 KLAQRGWLVMSWPEKYGGRSASLLEQTIYEMEIAYWGIPGAWMGI-SGTQWVGpcLMMFGTEEQREKYLPLIASGQKDGV 128
Cdd:cd01161    64 QLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLGFSVTLGAhQSIGFKG--ILLFGTEAQKEKYLPKLASGEWIAA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 129 WCtgYSEPNAGSDFANIRTRALR--DGDDYIINGQKVWTSVAHRARWCWLAVRT---NPNAAKKHHgISIFIVDMKSPGV 203
Cdd:cd01161   142 FA--LTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWITNGGIADIFTVFAKTevkDATGSVKDK-ITAFIVERSFGGV 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 204 TVNPILNYYGRHHFN--EVFFDNVRVPASNLVGEENKGWYYLMQSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQ 281
Cdd:cd01161   219 TNGPPEKKMGIKGSNtaEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGK 298

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1084606126 282 PLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQGQIPVY--ESSRNKIMG 331
Cdd:cd01161   299 KIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYqiEAAISKVFA 350
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 104-317 3.06e-37

Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.


Pssm-ID: 173844 [Multi-domain]  Cd Length: 394  Bit Score: 139.06  E-value: 3.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 104 LMMFGTEEQREKYLPLIASGQKDGVWCTgySEPN-AGSDFANIRTRALRDGDDYIINGQKVWTSVAHRARwCWLAV---R 179
Cdd:cd01155   104 LHRYGSEEQKKQWLEPLLDGKIRSAFAM--TEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGDPR-CKIAIvmgR 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 180 TNPNAAKKHHGISIFIVDMKSPGVTVNPILNYYG----RHHFNEVFFDNVRVPASNLVGEENKGWYYLMQSLAFERRSIA 255
Cdd:cd01155   181 TDPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGyddaPHGHAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHC 260

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084606126 256 PTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQG 317
Cdd:cd01155   261 MRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTV 322
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 5-317 4.83e-37

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: 138.34  E-value: 4.83e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126   5 LGEKELALKEEIRKFAKAELPPDLVrntviDGEfRDFEFEISMSRKLAQRGWLVMSWPEKYGGRSASLLEQTIYEMEIAY 84
Cdd:cd01162     1 LNEEQRAIQEVARAFAAKEMAPHAA-----DWD-QKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALST 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  85 wGIPG--AWMGISGTqwvgpCLMM---FGTEEQREKYLPLIASGQKDGVWCtgYSEPNAGSDFANIRTRALRDGDDYIIN 159
Cdd:cd01162    75 -GCVStaAYISIHNM-----CAWMidsFGNDEQRERFLPDLCTMEKLASYC--LTEPGSGSDAAALRTRAVREGDHYVLN 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 160 GQKVWTSVAHRARWCWLAVRTNPNAAKkhhGISIFIVDMKSPGVTvnpilnyYGRhhfNE------------VFFDNVRV 227
Cdd:cd01162   147 GSKAFISGAGDSDVYVVMARTGGEGPK---GISCFVVEKGTPGLS-------FGA---NEkkmgwnaqptraVIFEDCRV 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 228 PASNLVGEENKGWYYLMQSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFA 307
Cdd:cd01162   214 PVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMV 293

                         330
                  ....*....|
gi 1084606126 308 FQLAWRISQG 317
Cdd:cd01162   294 RRAASALDRG 303
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 5-316 3.17e-36

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: 136.33  E-value: 3.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126   5 LGEKELALKEEIRKFAKAELPPdlvRNTvidGEFRDFEFEISMSRKLAQRGWLVMSwPEKYGGRSASLLEQTIYEMEIAY 84
Cdd:cd01151    13 LTEEERAIRDTAREFCQEELAP---RVL---EAYREEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVER 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  85 wgipgAWMGISGTQWVGPCLMM-----FGTEEQREKYLPLIASGQKDGvwCTGYSEPNAGSDFANIRTRALRDGDDYIIN 159
Cdd:cd01151    86 -----VDSGYRSFMSVQSSLVMlpiydFGSEEQKQKYLPKLASGELIG--CFGLTEPNHGSDPGGMETRARKDGGGYKLN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 160 GQKVWTSVAHRAR----WCWLaVRTNpnaakkhhGISIFIVDMKSPGVTVNPILNYYG-RHHFN-EVFFDNVRVPASNLV 233
Cdd:cd01151   159 GSKTWITNSPIADvfvvWARN-DETG--------KIRGFILERGMKGLSAPKIQGKFSlRASITgEIVMDNVFVPEENLL 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 234 gEENKGWYYLMQSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVlkmfAFQLAWR 313
Cdd:cd01151   230 -PGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIAL----GLLACLR 304


                  ...
gi 1084606126 314 ISQ 316
Cdd:cd01151   305 VGR 307
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 2-391 9.18e-35

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 132.69  E-value: 9.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126   2 DFRLGEKELALKEEIRKFAKAELPPDLVRntvIDGEfRDFEFEISMSRKLAQRGWLVMSWPEKYGGRSASLLEQTIYEME 81
Cdd:PLN02519   23 SLLFDDTQLQFKESVQQFAQENIAPHAAA---IDAT-NSFPKDVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  82 IAYwgIPGAwMGISGTQWVGPC---LMMFGTEEQREKYLPLIASGQKDGVwcTGYSEPNAGSDFANIRTRALRDGDDYII 158
Cdd:PLN02519   99 ISR--ASGS-VGLSYGAHSNLCinqLVRNGTPAQKEKYLPKLISGEHVGA--LAMSEPNSGSDVVSMKCKAERVDGGYVL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 159 NGQKVWTSVAHRARWCWLAVRTNPNAAKkhHGISIFIVDMKSPGVTVNPILNYYGRHHFN--EVFFDNVRVPASNLVGEE 236
Cdd:PLN02519  174 NGNKMWCTNGPVAQTLVVYAKTDVAAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDtcELVFENCFVPEENVLGQE 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 237 NKGWYYLMQSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQ 316
Cdd:PLN02519  252 GKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDN 331

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084606126 317 GQIPVYESSRNKIMGDDLMRQGAITGADILGMYSQVDpDSEWAKLngaIQGAYLgfpgQAIAAGTAEIEKSIIAQ 391
Cdd:PLN02519  332 GKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYIN-EYPTGRL---LRDAKL----YEIGAGTSEIRRMLIGR 398
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 11-354 1.54e-29

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 118.50  E-value: 1.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  11 ALKEEIRKFAKAELPPDLVRNTVidgefrDFEFEISMSRKLAQRGWLVMSWPEKYGGRSASLLEQTIYEMEIAYWGiPG- 89
Cdd:PTZ00461   43 ALRETVAKFSREVVDKHAREDDI------NMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYD-PGf 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  90 --AWMGISgtqwvgpclMMF-------GTEEQREKYLPLIASGQKDGVwcTGYSEPNAGSDFANIRTRALRDGD-DYIIN 159
Cdd:PTZ00461  116 clAYLAHS---------MLFvnnfyysASPAQRARWLPKVLTGEHVGA--MGMSEPGAGTDVLGMRTTAKKDSNgNYVLN 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 160 GQKVWTSVAHRARWCWLAvrtnpnaAKKHHGISIFIVDMKSPGVTVNPILNYYGRH--HFNEVFFDNVRVPASNLVGEEN 237
Cdd:PTZ00461  185 GSKIWITNGTVADVFLIY-------AKVDGKITAFVVERGTKGFTQGPKIDKCGMRasHMCQLFFEDVVVPAENLLGEEG 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 238 KGWYYLMQSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQG 317
Cdd:PTZ00461  258 KGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPG 337

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1084606126 318 QIPVYESSRNKIMGDDLMRQGAITGADILG--MYSQVDP 354
Cdd:PTZ00461  338 NKNRLGSDAAKLFATPIAKKVADSAIQVMGgmGYSRDMP 376
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 1-319 7.78e-28

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 113.00  E-value: 7.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126   1 MDFRLGEKELALKEEIRkfakaelppDLVRNTVIDGEF----RDFEFEISMSRKLAQRGWLVMSWPEKYGGRSASLLEQT 76
Cdd:PRK03354    1 MDFNLNDEQELFVAGIR---------ELMASENWEAYFaecdRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  77 IYEMEIAYWG--------IPGAWMGIsgtqwvgpclMMFGTEEQREKYLPLIASGQKdgVWCTGYSEPNAGSDFANIRTR 148
Cdd:PRK03354   72 AVWMELGRLGaptyvlyqLPGGFNTF----------LREGTQEQIDKIMAFRGTGKQ--MWNSAITEPGAGSDVGSLKTT 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 149 ALRDGDDYIINGQKVW-TSVAHRArwcWLAVRTNPNAAKKHHGISIFIVDMKSPGVTVNPILNYYGR-HHFNEVFFDNVR 226
Cdd:PRK03354  140 YTRRNGKVYLNGSKCFiTSSAYTP---YIVVMARDGASPDKPVYTEWFVDMSKPGIKVTKLEKLGLRmDSCCEITFDDVE 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 227 VPASNLVGEENKGWYYLMQSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMF 306
Cdd:PRK03354  217 LDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNM 296

                         330
                  ....*....|...
gi 1084606126 307 AFQLAWRISQGQI 319
Cdd:PRK03354  297 LYEAAWKADNGTI 309
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 237-391 1.33e-23

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: 95.78  E-value: 1.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 237 NKGWYYLMQSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQ 316
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084606126 317 GQIPVYESSRNKIMGDDLMRQGAITGADILGMYSqVDPDSEWAKLngaiqgaYLGFPGQAIAAGTAEIEKSIIAQ 391
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYG-YLREYPVERL-------YRDARVLRIGEGTSEIQRNIIAR 147
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 7-123 3.55e-22

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: 90.60  E-value: 3.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126   7 EKELALKEEIRKFAKAELPPdlvrntVIDGEFRDFEFEISMSRKLAQRGWLVMSWPEKYGGRSASLLEQTIYEMEIAYwg 86
Cdd:pfam02771   2 EEQEALRDTVREFAEEEIAP------HAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELAR-- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1084606126  87 ipgAWMGISGTQWV-----GPCLMMFGTEEQREKYLPLIASG 123
Cdd:pfam02771  74 ---ADASVALALSVhsslgAPPILRFGTEEQKERYLPKLASG 112
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 49-255 8.60e-22

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: 96.30  E-value: 8.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  49 RKLAQRGWLVMSWPEKYGGRSaslLEQTIYEM--EIAYWGIPGAwMGISGTQWVGPCLMMFGTEEQREKYLPLIASGQKD 126
Cdd:cd01153    43 DAFAEAGWMALGVPEEYGGQG---LPITVYSAlaEIFSRGDAPL-MYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWT 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 127 GVWCtgYSEPNAGSDFANIRTRALRDGD-DYIINGQKVWTS-----VAHRARWCWLAVRTNPNAAKKhhGISIFIV---- 196
Cdd:cd01153   119 GTMC--LTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISagehdMSENIVHLVLARSEGAPPGVK--GLSLFLVpkfl 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084606126 197 -DMKSPGVTVNPILNYYGRHHFN--EVFFDNVRVPasnLVGEENKGWYYLMQSLAFERRSIA 255
Cdd:cd01153   195 dDGERNGVTVARIEEKMGLHGSPtcELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVG 253
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 130-223 1.14e-21

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: 88.49  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 130 CTGYSEPNAGSDFANIRTRAL-RDGDDYIINGQKVWTSVAHRARWCWLAVRTNPnaAKKHHGISIFIVDMKSPGVTVNPI 208
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAAdGDGGGWVLNGTKWWITNAGIADLFLVLARTGG--DDRHGGISLFLVPKDAPGVSVRRI 78

                          90
                  ....*....|....*..
gi 1084606126 209 LNYYGR--HHFNEVFFD 223
Cdd:pfam02770  79 ETKLGVrgLPTGELVFD 95
PLN02876 PLN02876
acyl-CoA dehydrogenase
 104-311 1.24e-20

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 94.09  E-value: 1.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 104 LMMFGTEEQREKYL-PLIASGQKDGVWCTgysEPN-AGSDFANIRTRALRDGDDYIINGQKVWTSVAHRARWCWLAV--R 179
Cdd:PLN02876  529 LLRYGNKEQQLEWLiPLLEGKIRSGFAMT---EPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVmgK 605

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 180 TNPNAAkKHHGISIFIVDMKSPGVTVNPILNYYG----RHHFNEVFFDNVRVPASNLVGEENKGWYYLMQSLAFERRSIA 255
Cdd:PLN02876  606 TDFNAP-KHKQQSMILVDIQTPGVQIKRPLLVFGfddaPHGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHC 684

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1084606126 256 PTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLA 311
Cdd:PLN02876  685 MRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAA 740
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 94-311 3.74e-15

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: 76.64  E-value: 3.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  94 ISGTQWVGPCLMMFGTEEQREKYLPLIASGQKDGVWC-TGYSEPNAGSDFANIRTRALRDGDD-YIINGQKVWTSVAHRA 171
Cdd:cd01154   113 LTMTDAAVYALRKYGPEELKQYLPGLLSDRYKTGLLGgTWMTEKQGGSDLGANETTAERSGGGvYRLNGHKWFASAPLAD 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 172 RWCWLAvRTnPNAAKKHHGISIFIVDMKSPGVTVNPIL-----NYYGRHHF--NEVFFDNVrvpASNLVGEENKGWYYLM 244
Cdd:cd01154   193 AALVLA-RP-EGAPAGARGLSLFLVPRLLEDGTRNGYRirrlkDKLGTRSVatGEVEFDDA---EAYLIGDEGKGIYYIL 267

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 245 QSLAFERRSIAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLE---VLKMFAFQLA 311
Cdd:cd01154   268 EMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEaatALTFRAARAF 337
PLN02526 PLN02526
acyl-coenzyme A oxidase
 103-347 4.02e-15

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 76.43  E-value: 4.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 103 CLMMFGTEEQREKYLPLIAsgQKDGVWCTGYSEPNAGSDFANIRTRALRDGDDYIINGQKVWTSVAHRARWCWLAVR-TN 181
Cdd:PLN02526  120 TIALCGSEAQKQKYLPSLA--QLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFARnTT 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 182 PNAakkhhgISIFIVDMKSPGVTVNPILNYYGRH-------HFNEVFF-DNVRVPASNLVGEENKgwyylmqSLAFERRS 253
Cdd:PLN02526  198 TNQ------INGFIVKKGAPGLKATKIENKIGLRmvqngdiVLKDVFVpDEDRLPGVNSFQDTNK-------VLAVSRVM 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 254 IAPTTYGNLKRILEELARYAGQTEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQLAWRISQGQIPVYESSRNKIMGDD 333
Cdd:PLN02526  265 VAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAWITK 344

                         250
                  ....*....|....
gi 1084606126 334 LMRQGAITGADILG 347
Cdd:PLN02526  345 KARETVALGRELLG 358
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 51-196 1.50e-14

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 75.29  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  51 LAQRGWLVMSWPEKYGGR----SASLLEQTIyeMEIAYWGI---PGAWMGISGTqwvgpcLMMFGTEEQREKYLPLIASG 123
Cdd:PTZ00456  108 LKAGGWTGISEPEEYGGQalplSVGFITREL--MATANWGFsmyPGLSIGAANT------LMAWGSEEQKEQYLTKLVSG 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084606126 124 QKDGVWCtgYSEPNAGSDFANIRTRALRDGD-DYIINGQKVWTSVAHR---ARWCWLAVRTNPNAAKKHHGISIFIV 196
Cdd:PTZ00456  180 EWSGTMC--LTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDHdltENIVHIVLARLPNSLPTTKGLSLFLV 254
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 42-248 3.35e-09

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 58.67  E-value: 3.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  42 EFEISMSRK---------LAQRGWLVMSWPEKYGGRSASLLEQTIYEMEIAywgipgawmGISGTQWV--------GP-- 102
Cdd:PRK09463  100 DWQITHELAdlppevwqfIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLA---------SRSGTLAVtvmvpnslGPge 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 103 CLMMFGTEEQREKYLPLIASGQKdgVWCTGYSEPNAGSDFANIR-----TRALRDGDDYI---INGQKVWTSVAHRARWC 174
Cdd:PRK09463  171 LLLHYGTDEQKDHYLPRLARGEE--IPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLgmrLTWNKRYITLAPIATVL 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 175 WLAVRT-NPN---AAKKHHGISIFIVDMKSPGVTVnpilnyyGRHHF--NEVFFD------NVRVPASNLVG-EEN--KG 239
Cdd:PRK09463  249 GLAFKLyDPDgllGDKEDLGITCALIPTDTPGVEI-------GRRHFplNVPFQNgptrgkDVFIPLDYIIGgPKMagQG 321


                  ....*....
gi 1084606126 240 WYYLMQSLA 248
Cdd:PRK09463  322 WRMLMECLS 330
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 42-251 2.11e-08

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 56.12  E-value: 2.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  42 EFEISMSRK---------LAQRGWLVMSWPEKYGGRSASLLEQTIYEMEIAYWGIPGAWmgisgTQWV----GP--CLMM 106
Cdd:PRK13026   99 DWDIVQNRKdlppevwdyLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAV-----TVMVpnslGPgeLLTH 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 107 FGTEEQREKYLPLIASGQKdgVWCTGYSEPNAGSDFANIR-----TRALRDGDDYI---INGQKVWTSVAHRARWCWLAV 178
Cdd:PRK13026  174 YGTQEQKDYWLPRLADGTE--IPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEVLglrLTWDKRYITLAPVATVLGLAF 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 179 RT-NPNA---AKKHHGISIFIVDMKSPGVTVnpilnyyGRHHF--NEVFFD------NVRVPASNLVGEEN---KGWYYL 243
Cdd:PRK13026  252 KLrDPDGllgDKKELGITCALIPTDHPGVEI-------GRRHNplGMAFMNgttrgkDVFIPLDWIIGGPDyagRGWRML 324


                  ....*...
gi 1084606126 244 MQSLAFER 251
Cdd:PRK13026  325 VECLSAGR 332
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 101-232 2.98e-08

Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.


Pssm-ID: 173839 [Multi-domain]  Cd Length: 610  Bit Score: 55.41  E-value: 2.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 101 GPCLMMFGTEEQREKYLPLIASGQKDGvwCTGYSEPNAGSDFANIRTRALRD--GDDYIINGQKVwtsvahRARWCWLAv 178
Cdd:cd01150   110 GNAIKNLGTDEHQDYWLQGANNLEIIG--CFAQTELGHGSNLQGLETTATYDplTQEFVINTPDF------TATKWWPG- 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084606126 179 rtnpNAAK---------------KHHGISIFIV---DMKS----PGVTVNPILNYYGRHHFNEVF--FDNVRVPASNL 232
Cdd:cd01150   181 ----NLGKtathavvfaqlitpgKNHGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFlqFRNVRIPRENL 254
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 108-269 2.64e-07

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 52.58  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 108 GTEEQREKYLpliaSGQKDGVWCTGYS-EPNAGSDFANIRTRA-LRDGDDYIINGQKVWTSVAHRARWCWLA---VRTNP 182
Cdd:PTZ00457  117 GSKELKGKYL----TAMSDGTIMMGWAtEEGCGSDISMNTTKAsLTDDGSYVLTGQKRCEFAASATHFLVLAktlTQTAA 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 183 NA-AKKHHGISIFIVDMKSPGVTVNPilnyygrhhfNEVFFDNVrvPASNLVGEENKGWYYLMQSLAFERRSIAPTTYGN 261
Cdd:PTZ00457  193 EEgATEVSRNSFFICAKDAKGVSVNG----------DSVVFENT--PAADVVGVVGEGFKDAMITLFTEQYLYAASLLGI 260


                  ....*...
gi 1084606126 262 LKRILEEL 269
Cdd:PTZ00457  261 MKRVVQEL 268
PLN02443 PLN02443
acyl-coenzyme A oxidase
 108-233 2.45e-06

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 49.45  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 108 GTEEQREKYLPLIASGQKDGvwCTGYSEPNAGSDFANIRTRALRD--GDDYIINGQ-------------KVWTSVAHRAR 172
Cdd:PLN02443  114 GTEEQQKKWLPLAYKMQIIG--CYAQTELGHGSNVQGLETTATFDpkTDEFVIHSPtltsskwwpgglgKVSTHAVVYAR 191

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084606126 173 wcwlaVRTNpnaaKKHHGISIFIVDMKS-------PGVTVNPILNYYGRHHFNE-----VFFDNVRVPASNLV 233
Cdd:PLN02443  192 -----LITN----GKDHGIHGFIVQLRSlddhsplPGVTVGDIGMKFGNGAYNTmdngfLRFDHVRIPRDQML 255
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 51-234 1.04e-04

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: 44.24  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  51 LAQRGWLVMSWPEKYGGRSASLLeqTIYEM--EIA-----YWGIPGAWMGISGTqwvgpcLMMFGTEEQREKYLPLIASG 123
Cdd:cd01163    31 LRQSGLGTLRVPKEYGGLGASLP--DLYEVvrELAaadsnIAQALRAHFGFVEA------LLLAGPEQFRKRWFGRVLNG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 124 QkdgvWCTGYSEPNAGSDFANIRTRALRDGDDYIINGQKVWTSVAHRARWCWLAVrTNPNAAkkhhgISIFIVDMKSPGV 203
Cdd:cd01163   103 W----IFGNAVSERGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSA-LDEEGK-----LVFAAVPTDRPGI 172

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1084606126 204 TVNPILNYYGRHHFNE--VFFDNVRVPASNLVG 234
Cdd:cd01163   173 TVVDDWDGFGQRLTASgtVTFDNVRVEPDEVLP 205
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 49-326 1.38e-03

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: 40.41  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126  49 RKLAQRGWLVMSWPEKYGGRSASLLEQTIYEMEIAYWGIPGAWM-GISGTqwVGPCLMMFGTEEQREkylpliasgqkdg 127
Cdd:cd01159    29 RALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVaSIVAT--HSRMLAAFPPEAQEE------------- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 128 VWCTGYSEPNAGSdFANIRtRALRDGDDYIINGQKVWTSVAHRARWCWLAVRTNPNAAKKHhgISIFIVDMKspGVTVNP 207
Cdd:cd01159    94 VWGDGPDTLLAGS-YAPGG-RAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPL--PRAFVVPRA--EYEIVD 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084606126 208 I-----LNYYGRHHfneVFFDNVRVPASNL--VGEENKGWY-------YLMQSLAFERRSIAPTTYGNLKRILEELARYA 273
Cdd:cd01159   168 TwhvvgLRGTGSNT---VVVDDVFVPEHRTltAGDMMAGDGpggstpvYRMPLRQVFPLSFAAVSLGAAEGALAEFLELA 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1084606126 274 GQ---TEYEGQPLSKNPVVRGKLADLAIDLEVLKMFAFQL---AWRISQGQIPVYESSR 326
Cdd:cd01159   245 GKrvrQYGAAVKMAEAPITQLRLAEAAAELDAARAFLERAtrdLWAHALAGGPIDVEER 303
 
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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