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Conserved domains on  [gi|1144346276|gb|ONT99571|]
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acyl-CoA dehydrogenase [Burkholderia cenocepacia]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 11449292)

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

CATH:  1.10.540.10
EC:  1.-.-.-
Gene Ontology:  GO:0003995|GO:0050660
PubMed:  10760462|12504675
SCOP:  3001580|3001701

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-340 1.37e-40

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: 146.52  E-value: 1.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276   1 MDFVFDEDQEALADSVKRLLMTEMTPElIRELWATPtGRSDELWALFASQGLTAVSVPEAHGGLGLTEAEWALLAQAYGY 80
Cdd:COG1960     1 MDFELTEEQRALRDEVREFAEEEIAPE-AREWDREG-EFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELAR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276  81 FGSPEPL-LDTALVSAGVLARLPASDWRDALLRDIAEGRARVALV--------HPVNP------------------YAAD 133
Cdd:COG1960    79 ADASLALpVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFAltepgagsDAAALrttavrdgdgyvlngqktFITN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 134 VHVADTLLCehrgeLHRVDPAQCAWRT----VDSVDP----SRRLFTLDWEPS-------------AATRIASADEAAPL 192
Cdd:COG1960   159 APVADVILV-----LARTDPAAGHRGIslflVPKDTPgvtvGRIEDKMGLRGSdtgelffddvrvpAENLLGEEGKGFKI 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 193 LNRALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIaDDHPQRA 272
Cdd:COG1960   234 AMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLL-DAGEDAA 312

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 273 VFVSHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMK--RIWALSGswGDSAFHKARVADAILGDA 340
Cdd:COG1960   313 LEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRdaRILTIYE--GTNEIQRLIIARRLLGRP 380
 
Name Accession Description Interval E-value
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-340 1.37e-40

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: 146.52  E-value: 1.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276   1 MDFVFDEDQEALADSVKRLLMTEMTPElIRELWATPtGRSDELWALFASQGLTAVSVPEAHGGLGLTEAEWALLAQAYGY 80
Cdd:COG1960     1 MDFELTEEQRALRDEVREFAEEEIAPE-AREWDREG-EFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELAR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276  81 FGSPEPL-LDTALVSAGVLARLPASDWRDALLRDIAEGRARVALV--------HPVNP------------------YAAD 133
Cdd:COG1960    79 ADASLALpVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFAltepgagsDAAALrttavrdgdgyvlngqktFITN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 134 VHVADTLLCehrgeLHRVDPAQCAWRT----VDSVDP----SRRLFTLDWEPS-------------AATRIASADEAAPL 192
Cdd:COG1960   159 APVADVILV-----LARTDPAAGHRGIslflVPKDTPgvtvGRIEDKMGLRGSdtgelffddvrvpAENLLGEEGKGFKI 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 193 LNRALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIaDDHPQRA 272
Cdd:COG1960   234 AMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLL-DAGEDAA 312

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 273 VFVSHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMK--RIWALSGswGDSAFHKARVADAILGDA 340
Cdd:COG1960   313 LEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRdaRILTIYE--GTNEIQRLIIARRLLGRP 380
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 187-333 2.67e-24

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: 101.21  E-value: 2.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 187 DEAAPLLNRALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIAD 266
Cdd:cd00567   180 GGGFELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ 259

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1144346276 267 DHPQRAVFVSHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMKRIWALSGSWGDSAFHKARVA 333
Cdd:cd00567   260 GPDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 196-336 2.40e-22

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: 91.55  E-value: 2.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 196 ALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIADDHPQRAvFV 275
Cdd:pfam00441  10 TLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGA-EA 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1144346276 276 SHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMKRIWALSGSWGDSAFHKARVADAI 336
Cdd:pfam00441  89 SMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
PRK12341 PRK12341
acyl-CoA dehydrogenase;
1-316 2.53e-16

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 79.39  E-value: 2.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276   1 MDFVFDEDQEALADSVKRLLMTEMTPELIRElWATPTGRSDELWALFASQGLTAVSVPEAHGGLGLTEAEWALLAQAYGY 80
Cdd:PRK12341    1 MDFSLTEEQELLLASIRELITRNFPEEYFRT-CDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276  81 FGSPEPLLDTALVSAGVLARlpASDWRDALLRDIAEGRARVALVHPVN-PYA-ADVHVADTLLCEHRGELH--------- 149
Cdd:PRK12341   80 CGAPAFLITNGQCIHSMRRF--GSAEQLRKTAESTLETGDPAYALALTePGAgSDNNSATTTYTRKNGKVYlngqktfit 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 150 ---RVDPAQCAWRTVDSVDPsRRLFTLDWEPSAATRIASAD-----------------------------EAAPLLN--R 195
Cdd:PRK12341  158 gakEYPYMLVLARDPQPKDP-KKAFTLWWVDSSKPGIKINPlhkigwhmlstcevyldnveveesdlvgeEGMGFLNvmY 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 196 ALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAiADDHPQRAVFV 275
Cdd:PRK12341  237 NFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQ-ADNGQSLRTSA 315

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1144346276 276 SHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQifmkRIW 316
Cdd:PRK12341  316 ALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVS----RFW 352
 
Name Accession Description Interval E-value
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-340 1.37e-40

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: 146.52  E-value: 1.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276   1 MDFVFDEDQEALADSVKRLLMTEMTPElIRELWATPtGRSDELWALFASQGLTAVSVPEAHGGLGLTEAEWALLAQAYGY 80
Cdd:COG1960     1 MDFELTEEQRALRDEVREFAEEEIAPE-AREWDREG-EFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELAR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276  81 FGSPEPL-LDTALVSAGVLARLPASDWRDALLRDIAEGRARVALV--------HPVNP------------------YAAD 133
Cdd:COG1960    79 ADASLALpVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFAltepgagsDAAALrttavrdgdgyvlngqktFITN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 134 VHVADTLLCehrgeLHRVDPAQCAWRT----VDSVDP----SRRLFTLDWEPS-------------AATRIASADEAAPL 192
Cdd:COG1960   159 APVADVILV-----LARTDPAAGHRGIslflVPKDTPgvtvGRIEDKMGLRGSdtgelffddvrvpAENLLGEEGKGFKI 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 193 LNRALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIaDDHPQRA 272
Cdd:COG1960   234 AMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLL-DAGEDAA 312

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 273 VFVSHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMK--RIWALSGswGDSAFHKARVADAILGDA 340
Cdd:COG1960   313 LEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRdaRILTIYE--GTNEIQRLIIARRLLGRP 380
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 187-333 2.67e-24

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: 101.21  E-value: 2.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 187 DEAAPLLNRALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIAD 266
Cdd:cd00567   180 GGGFELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ 259

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1144346276 267 DHPQRAVFVSHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMKRIWALSGSWGDSAFHKARVA 333
Cdd:cd00567   260 GPDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 196-336 2.40e-22

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: 91.55  E-value: 2.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 196 ALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIADDHPQRAvFV 275
Cdd:pfam00441  10 TLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGA-EA 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1144346276 276 SHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMKRIWALSGSWGDSAFHKARVADAI 336
Cdd:pfam00441  89 SMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 196-313 2.09e-19

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: 88.09  E-value: 2.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 196 ALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQaIADDHPQRAVFV 275
Cdd:cd01158   232 TLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAAR-LKDNGEPFIKEA 310

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1144346276 276 SHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMK 313
Cdd:cd01158   311 AMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYR 348
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 166-315 1.37e-17

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: 82.88  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 166 PSRRLFTLDWEPSAATRIASADEAAPLLNRALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLAD 245
Cdd:cd01162   202 PTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLAD 281

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 246 VAIRYEFARPVVARAAQAIADDHPQRAVFVSHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMKRI 315
Cdd:cd01162   282 MATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDL 351
PRK12341 PRK12341
acyl-CoA dehydrogenase;
1-316 2.53e-16

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 79.39  E-value: 2.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276   1 MDFVFDEDQEALADSVKRLLMTEMTPELIRElWATPTGRSDELWALFASQGLTAVSVPEAHGGLGLTEAEWALLAQAYGY 80
Cdd:PRK12341    1 MDFSLTEEQELLLASIRELITRNFPEEYFRT-CDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276  81 FGSPEPLLDTALVSAGVLARlpASDWRDALLRDIAEGRARVALVHPVN-PYA-ADVHVADTLLCEHRGELH--------- 149
Cdd:PRK12341   80 CGAPAFLITNGQCIHSMRRF--GSAEQLRKTAESTLETGDPAYALALTePGAgSDNNSATTTYTRKNGKVYlngqktfit 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 150 ---RVDPAQCAWRTVDSVDPsRRLFTLDWEPSAATRIASAD-----------------------------EAAPLLN--R 195
Cdd:PRK12341  158 gakEYPYMLVLARDPQPKDP-KKAFTLWWVDSSKPGIKINPlhkigwhmlstcevyldnveveesdlvgeEGMGFLNvmY 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 196 ALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAiADDHPQRAVFV 275
Cdd:PRK12341  237 NFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQ-ADNGQSLRTSA 315

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1144346276 276 SHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQifmkRIW 316
Cdd:PRK12341  316 ALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVS----RFW 352
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 7-305 2.51e-14

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: 73.30  E-value: 2.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276   7 EDQEALADSVKRLLMTEMTPELIRelWATPTGRSDELWALFASQGLTAVSVPEAHGGLGLTEAEWALLAQAYGYFG--SP 84
Cdd:cd01160     1 EEHDAFRDVVRRFFAKEVAPFHHE--WEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGgsGP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276  85 EPLLDTALVSAgVLARLPASDWRDALLRDIAEGR--ARVALVHP-----------------------------VNPYAAD 133
Cdd:cd01160    79 GLSLHTDIVSP-YITRAGSPEQKERVLPQMVAGKkiGAIAMTEPgagsdlqgirttarkdgdhyvlngsktfiTNGMLAD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 134 VH--VADT-----------LLCEHRGE--LHRVDP-AQCAWRTVDSVDpsrrLFTLDWEPSAATRIASADEAAPLLNRAL 197
Cdd:cd01160   158 VVivVARTggeargaggisLFLVERGTpgFSRGRKlKKMGWKAQDTAE----LFFDDCRVPAENLLGEENKGFYYLMQNL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 198 DHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQaiadDHPQRAVFVSH 277
Cdd:cd01160   234 PQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAW----RHEQGRLDVAE 309

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1144346276 278 AKLAAMSAAQLAAR---HAMQVHGAIGYTWE 305
Cdd:cd01160   310 ASMAKYWATELQNRvayECVQLHGGWGYMRE 340
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 204-313 1.22e-12

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: 68.38  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 204 VAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIaDDHPQRAVFVSHAKLAAM 283
Cdd:cd01157   244 VAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEV-DSGRRNTYYASIAKAFAA 322

                          90       100       110
                  ....*....|....*....|....*....|
gi 1144346276 284 SAAQLAARHAMQVHGAIGYTWELDLQIFMK 313
Cdd:cd01157   323 DIANQLATDAVQIFGGNGFNSEYPVEKLMR 352
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 197-302 2.07e-11

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: 64.35  E-value: 2.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 197 LDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIADDHPQRAVFVS 276
Cdd:cd01156   236 LDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAG 315

                          90       100
                  ....*....|....*....|....*.
gi 1144346276 277 hAKLAAMSAAQLAARHAMQVHGAIGY 302
Cdd:cd01156   316 -VILYAAEKATQVALDAIQILGGNGY 340
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 6-84 1.91e-08

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: 51.70  E-value: 1.91e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1144346276   6 DEDQEALADSVKRLLMTEMTPeLIRELWATPTGrSDELWALFASQGLTAVSVPEAHGGLGLTEAEWALLAQAYGYFGSP 84
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAP-HAAEWDEEGEF-PRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADAS 77
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 7-118 2.50e-08

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: 55.05  E-value: 2.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276   7 EDQEALADSVKRLLMTEMTPELIRELWAT--PTGRSDELW-ALFASQGLTAVSVPEAHGGLGLTEAEWALLAQAYGYFGS 83
Cdd:cd01152     1 PSEEAFRAEVRAWLAAHLPPELREESALGyrEGREDRRRWqRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1144346276  84 PEPLLDTALVSAG-VLARLPASDWRDALLRDIAEGR 118
Cdd:cd01152    81 PVPFNQIGIDLAGpTILAYGTDEQKRRFLPPILSGE 116
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 197-271 8.76e-08

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 53.34  E-value: 8.76e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1144346276 197 LDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIADDHPQR 271
Cdd:PLN02519  262 LDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDR 336
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 7-316 3.05e-07

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: 51.70  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276   7 EDQEALADSVKRLLMTEMTPELIRELWATPTGRSDELWALfasqGLTAVSVPEAHGGLGLTEAEWALLAQAYGYFGSPEP 86
Cdd:cd01161    29 EELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKEL----GLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLGFSV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276  87 LLDtALVSAGVLARLPAS--DWRDALLRDIAEGR--ARVALVHP-------------------------------VNPYA 131
Cdd:cd01161   105 TLG-AHQSIGFKGILLFGteAQKEKYLPKLASGEwiAAFALTEPssgsdaasirttavlsedgkhyvlngskiwiTNGGI 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 132 ADVHV--ADTLLCEHRGELHRVDPAQCAWRTVDSVDPSRRLFTLDWEPSAATRIASADEAAPLLN-------------RA 196
Cdd:cd01161   184 ADIFTvfAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENvlgevgdgfkvamNI 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 197 LDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAA-----QAIADDHPQR 271
Cdd:cd01161   264 LNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSgnmdrGLKAEYQIEA 343

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1144346276 272 AVfvshAKLAAMSAAQLAARHAMQVHGAIGYTWEL-------DLQIFmkRIW 316
Cdd:cd01161   344 AI----SKVFASEAAWLVVDEAIQIHGGMGFMREYgvervlrDLRIF--RIF 389
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 195-316 1.58e-06

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 49.55  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 195 RALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIADDHPQRaVF 274
Cdd:PTZ00461  265 RNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNR-LG 343

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1144346276 275 VSHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQifmkRIW 316
Cdd:PTZ00461  344 SDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVE----RLW 381
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 197-302 6.29e-06

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: 47.75  E-value: 6.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 197 LDHGAFAvaaqlLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAA----QAIADD----H 268
Cdd:cd01154   275 LDNAVAA-----LGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAArafdRAAADKpveaH 349

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1144346276 269 PQRAvFVSHAKLAAMSAAQLAARHAMQVHGAIGY 302
Cdd:cd01154   350 MARL-ATPVAKLIACKRAAPVTSEAMEVFGGNGY 382
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 208-301 6.60e-05

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: 44.30  E-value: 6.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 208 LLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIaDDHPQRAV--FVSHAKLAAMSA 285
Cdd:cd01155   263 LIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMI-DTVGNKAArkEIAMIKVAAPRM 341

                          90
                  ....*....|....*.
gi 1144346276 286 AQLAARHAMQVHGAIG 301
Cdd:cd01155   342 ALKIIDRAIQVHGAAG 357
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 1-316 2.01e-04

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 42.90  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276   1 MDFVFDEDQEALADSVKRLLMTEMTPELIRElwATPTGRSDELW-ALFASQGLTAVSVPEAHGGLGlteAEWALLAQAY- 78
Cdd:PRK03354    1 MDFNLNDEQELFVAGIRELMASENWEAYFAE--CDRDSVYPERFvKALADMGIDSLLIPEEHGGLD---AGFVTLAAVWm 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276  79 --GYFGSPEPLLDTALVSAGVLARLPASDWRDALLRDIAEGRA--RVALVHPvnPYAADVHVADTLLCEHRGELH----- 149
Cdd:PRK03354   76 elGRLGAPTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTGKQmwNSAITEP--GAGSDVGSLKTTYTRRNGKVYlngsk 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 150 --RVDPAQCAWRTV---DSVDPSRRLFTlDW-------------EPSAATRIASADE----------------AAPLLNR 195
Cdd:PRK03354  154 cfITSSAYTPYIVVmarDGASPDKPVYT-EWfvdmskpgikvtkLEKLGLRMDSCCEitfddveldekdmfgrEGNGFNR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 196 A---LDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAiADDHPQRA 272
Cdd:PRK03354  233 VkeeFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWK-ADNGTITS 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1144346276 273 VFVSHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQifmkRIW 316
Cdd:PRK03354  312 GDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRIS----RFW 351
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 210-320 1.96e-03

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 40.12  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 210 GLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPV---VARAAQAIADDHPQ--RAVFVSHAKLAAMS 284
Cdd:PRK11561  308 GLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALlfrLARAWDRRADAKEAlwARLFTPAAKFVICK 387

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1144346276 285 AAQLAARHAMQVHGAIGYTWELDL-----QIFMKRIWALSG 320
Cdd:PRK11561  388 RGIPFVAEAMEVLGGIGYCEESELprlyrEMPVNSIWEGSG 428
PLN02876 PLN02876
acyl-CoA dehydrogenase
 207-301 2.67e-03

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 39.78  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 207 QLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIaDDHPQRAV--FVSHAKLAAMS 284
Cdd:PLN02876  686 RLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQL-DRLGNKKArgIIAMAKVAAPN 764

                          90
                  ....*....|....*..
gi 1144346276 285 AAQLAARHAMQVHGAIG 301
Cdd:PLN02876  765 MALKVLDMAMQVHGAAG 781
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 193-248 6.09e-03

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: 38.11  E-value: 6.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1144346276 193 LNRAldhgAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAI 248
Cdd:cd01151   242 LNNA----RYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLT 293
 
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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