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Conserved domains on  [gi|1024869198|ref|WP_063521074|]
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acyl-CoA dehydrogenase family protein, partial [Alcanivorax sp. HI0083]

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 ...
 1-262 0e+00

Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)


The actual alignment was detected with superfamily member cd01151:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 386  Bit Score: 516.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWANLD--GKINGFVVERGFDGFSTPK 78
Cdd:cd01151   122 ASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADVFVVWARNDetGKIRGFILERGMKGLSAPK 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  79 IEGKFSLRASITGQIMLDDCFVPEENRL-DVEGLKGPFSCLNKARYGISWGAMGAAEFCWQAARQYTLDRKQFGRPLAAT 157
Cdd:cd01151   202 IQGKFSLRASITGEIVMDNVFVPEENLLpGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAF 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 158 QLIQKKLADMQTEITLGLQGALQLGRLMDAGNWSPEMVSLMKRNNCGKAIDIARQARDMHGGNGISDEYHVIRHVMNLEA 237
Cdd:cd01151   282 QLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLES 361

                         250       260
                  ....*....|....*....|....*
gi 1024869198 238 VNTYEGTHDVHALILGRAQTGLQAF 262
Cdd:cd01151   362 VNTYEGTHDIHALILGRAITGIQAF 386
 
Name Accession Description Interval E-value
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 1-262 0e+00

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: 516.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWANLD--GKINGFVVERGFDGFSTPK 78
Cdd:cd01151   122 ASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADVFVVWARNDetGKIRGFILERGMKGLSAPK 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  79 IEGKFSLRASITGQIMLDDCFVPEENRL-DVEGLKGPFSCLNKARYGISWGAMGAAEFCWQAARQYTLDRKQFGRPLAAT 157
Cdd:cd01151   202 IQGKFSLRASITGEIVMDNVFVPEENLLpGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAF 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 158 QLIQKKLADMQTEITLGLQGALQLGRLMDAGNWSPEMVSLMKRNNCGKAIDIARQARDMHGGNGISDEYHVIRHVMNLEA 237
Cdd:cd01151   282 QLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLES 361

                         250       260
                  ....*....|....*....|....*
gi 1024869198 238 VNTYEGTHDVHALILGRAQTGLQAF 262
Cdd:cd01151   362 VNTYEGTHDIHALILGRAITGIQAF 386
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-261 2.48e-98

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: 292.51  E-value: 2.48e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWANLDGK-----INGFVVERGFDGFS 75
Cdd:COG1960   114 ASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADVILVLARTDPAaghrgISLFLVPKDTPGVT 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  76 TPKIEGKFSLRASITGQIMLDDCFVPEENRLDVE--GLKGPFSCLNKARYGISWGAMGAAEFCWQAARQYTLDRKQFGRP 153
Cdd:COG1960   194 VGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEgkGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRP 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 154 LAATQLIQKKLADMQTEITLGLQGALQLGRLMDAGNWSPEMVSLMKRNNCGKAIDIARQARDMHGGNGISDEYHVIRHVM 233
Cdd:COG1960   274 IADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYR 353

                         250       260
                  ....*....|....*....|....*...
gi 1024869198 234 NLEAVNTYEGTHDVHALILGRAQTGLQA 261
Cdd:COG1960   354 DARILTIYEGTNEIQRLIIARRLLGRPG 381
PLN02526 PLN02526
acyl-coenzyme A oxidase
 6-262 8.54e-67

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 212.79  E-value: 8.54e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   6 VGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWA-NLD-GKINGFVVERGFDGFSTPKIEGKF 83
Cdd:PLN02526  143 VACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFArNTTtNQINGFIVKKGAPGLKATKIENKI 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  84 SLRASITGQIMLDDCFVPEENRLdvEGLKGpFSCLNK----ARYGISWGAMGAAEFCWQAARQYTLDRKQFGRPLAATQL 159
Cdd:PLN02526  223 GLRMVQNGDIVLKDVFVPDEDRL--PGVNS-FQDTNKvlavSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQI 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 160 IQKKLADMQTEITLGLQGALQLGRLMDAGNWSPEMVSLMKRNNCGKAIDIARQARDMHGGNGISDEYHVIRHVMNLEAVN 239
Cdd:PLN02526  300 NQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIY 379

                         250       260
                  ....*....|....*....|...
gi 1024869198 240 TYEGTHDVHALILGRAQTGLQAF 262
Cdd:PLN02526  380 TYEGTYDINALVTGREITGIASF 402
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 109-255 1.49e-28

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: 106.18  E-value: 1.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 109 EGLKGPFSCLNKARYGISWGAMGAAEFCWQAARQYTLDRKQFGRPLAATQLIQKKLADMQTEITLGLQGALQLGRLMDAG 188
Cdd:pfam00441   2 RGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024869198 189 NWSPEMVSLMKRNNCGKAIDIARQARDMHGGNGISDEYHVIRHVMNLEAVNTYEGTHDVHALILGRA 255
Cdd:pfam00441  82 GPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARR 148
 
Name Accession Description Interval E-value
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 1-262 0e+00

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: 516.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWANLD--GKINGFVVERGFDGFSTPK 78
Cdd:cd01151   122 ASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADVFVVWARNDetGKIRGFILERGMKGLSAPK 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  79 IEGKFSLRASITGQIMLDDCFVPEENRL-DVEGLKGPFSCLNKARYGISWGAMGAAEFCWQAARQYTLDRKQFGRPLAAT 157
Cdd:cd01151   202 IQGKFSLRASITGEIVMDNVFVPEENLLpGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAF 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 158 QLIQKKLADMQTEITLGLQGALQLGRLMDAGNWSPEMVSLMKRNNCGKAIDIARQARDMHGGNGISDEYHVIRHVMNLEA 237
Cdd:cd01151   282 QLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLES 361

                         250       260
                  ....*....|....*....|....*
gi 1024869198 238 VNTYEGTHDVHALILGRAQTGLQAF 262
Cdd:cd01151   362 VNTYEGTHDIHALILGRAITGIQAF 386
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 1-261 2.48e-98

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: 292.51  E-value: 2.48e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWANLDGK-----INGFVVERGFDGFS 75
Cdd:COG1960   114 ASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADVILVLARTDPAaghrgISLFLVPKDTPGVT 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  76 TPKIEGKFSLRASITGQIMLDDCFVPEENRLDVE--GLKGPFSCLNKARYGISWGAMGAAEFCWQAARQYTLDRKQFGRP 153
Cdd:COG1960   194 VGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEgkGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRP 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 154 LAATQLIQKKLADMQTEITLGLQGALQLGRLMDAGNWSPEMVSLMKRNNCGKAIDIARQARDMHGGNGISDEYHVIRHVM 233
Cdd:COG1960   274 IADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYR 353

                         250       260
                  ....*....|....*....|....*...
gi 1024869198 234 NLEAVNTYEGTHDVHALILGRAQTGLQA 261
Cdd:COG1960   354 DARILTIYEGTNEIQRLIIARRLLGRPG 381
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 1-254 4.19e-81

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: 246.81  E-value: 4.19e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWANLDGKING------FVVERGFDGF 74
Cdd:cd00567    65 ASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEEGPGhrgisaFLVPADTPGV 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  75 STPKIEGKFSLRASITGQIMLDDCFVPEENRLDVEG--LKGPFSCLNKARYGISWGAMGAAEFCWQAARQYTLDRKQFGR 152
Cdd:cd00567   145 TVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGggFELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGK 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 153 PLAATQLIQKKLADMQTEITLGLQGALQLGRLMDAG-NWSPEMVSLMKRNNCGKAIDIARQARDMHGGNGISDEYHVIRH 231
Cdd:cd00567   225 PLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGpDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERY 304

                         250       260
                  ....*....|....*....|...
gi 1024869198 232 VMNLEAVNTYEGTHDVHALILGR 254
Cdd:cd00567   305 LRDARAARIAEGTAEIQRLIIAR 327
PLN02526 PLN02526
acyl-coenzyme A oxidase
 6-262 8.54e-67

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 212.79  E-value: 8.54e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   6 VGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWA-NLD-GKINGFVVERGFDGFSTPKIEGKF 83
Cdd:PLN02526  143 VACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFArNTTtNQINGFIVKKGAPGLKATKIENKI 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  84 SLRASITGQIMLDDCFVPEENRLdvEGLKGpFSCLNK----ARYGISWGAMGAAEFCWQAARQYTLDRKQFGRPLAATQL 159
Cdd:PLN02526  223 GLRMVQNGDIVLKDVFVPDEDRL--PGVNS-FQDTNKvlavSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQI 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 160 IQKKLADMQTEITLGLQGALQLGRLMDAGNWSPEMVSLMKRNNCGKAIDIARQARDMHGGNGISDEYHVIRHVMNLEAVN 239
Cdd:PLN02526  300 NQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIY 379

                         250       260
                  ....*....|....*....|...
gi 1024869198 240 TYEGTHDVHALILGRAQTGLQAF 262
Cdd:PLN02526  380 TYEGTYDINALVTGREITGIASF 402
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 1-255 9.23e-66

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: 209.05  E-value: 9.23e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWANLDGK-----INGFVVERGFDGFS 75
Cdd:cd01158   109 ATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFYIVFAVTDPSkgyrgITAFIVERDTPGLS 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  76 TPKIEGKFSLRASITGQIMLDDCFVPEENRLDVE--GLKGPFSCLNKARYGISWGAMGAAEFCWQAARQYTLDRKQFGRP 153
Cdd:cd01158   189 VGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEgeGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKP 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 154 LAATQLIQKKLADMQTEIT----LGLQGAlqlgRLMDAGNWSPEMVSLMKRNNCGKAIDIARQARDMHGGNGISDEYHVI 229
Cdd:cd01158   269 IADFQGIQFKLADMATEIEaarlLTYKAA----RLKDNGEPFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVE 344

                         250       260
                  ....*....|....*....|....*.
gi 1024869198 230 RHVMNLEAVNTYEGTHDVHALILGRA 255
Cdd:cd01158   345 RYYRDAKITEIYEGTSEIQRLVIAKH 370
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 1-255 4.88e-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: 184.15  E-value: 4.88e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWANLDGK-----INGFVVERGFDGFS 75
Cdd:cd01156   112 ISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDADTLVVYAKTDPSagahgITAFIVEKGMPGFS 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  76 TPKIEGKFSLRASITGQIMLDDCFVPEENRLDVE--GLKGPFSCLNKARYGISWGAMGAAEFCWQAARQYTLDRKQFGRP 153
Cdd:cd01156   192 RAQKLDKLGMRGSNTCELVFEDCEVPEENILGGEnkGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQP 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 154 LAATQLIQKKLADMQTEITLGLQGALQLGRLMDAGNwspemvslMKRNNCGKAI--------DIARQARDMHGGNGISDE 225
Cdd:cd01156   272 IGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGN--------MDPKDAAGVIlyaaekatQVALDAIQILGGNGYIND 343

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1024869198 226 YHVIRHvmnLEAVNTYE---GTHDVHALILGRA 255
Cdd:cd01156   344 YPTGRL---LRDAKLYEigaGTSEIRRMVIGRE 373
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 1-263 1.08e-49

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: 168.42  E-value: 1.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHAKKVDGG--YVLNGAKTWITNSPIADVAVVWANLDG---------KINGFVVER 69
Cdd:cd01161   134 ASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGkhYVLNGSKIWITNGGIADIFTVFAKTEVkdatgsvkdKITAFIVER 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  70 GFDGFSTPKIEGKFSLRASITGQIMLDDCFVPEENRLDVEG--LKGPFSCLNKARYGISWGAMGAAEFCWQAARQYTLDR 147
Cdd:cd01161   214 SFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGdgFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNR 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 148 KQFGRPLAATQLIQKKLADMQTEITLGLQGALQLGRLMDAG---NWSPEmVSLMKRNNCGKAIDIARQARDMHGGNGISD 224
Cdd:cd01161   294 KQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGlkaEYQIE-AAISKVFASEAAWLVVDEAIQIHGGMGFMR 372

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1024869198 225 EYHVIRHVMNLEAVNTYEGTHDVHALILgrAQTGLQAFG 263
Cdd:cd01161   373 EYGVERVLRDLRIFRIFEGTNEILRLFI--ALTGLQHAG 409
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 1-255 1.36e-49

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: 167.23  E-value: 1.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWANLDGK----INGFVVERGFDGFST 76
Cdd:cd01162   110 CTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVYVVMARTGGEgpkgISCFVVEKGTPGLSF 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  77 PKIEGKFSLRASITGQIMLDDCFVPEENRLDVEG------LKGpfscLNKARYGISWGAMGAAEFCWQAARQYTLDRKQF 150
Cdd:cd01162   190 GANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGqgfgiaMAG----LNGGRLNIASCSLGAAQAALDLARAYLEERKQF 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 151 GRPLAATQLIQKKLADMQTEIT----LGLQGALQLGR-LMDAGNWSpEMVSLMKRNNCgkaIDIARQARDMHGGNGISDE 225
Cdd:cd01162   266 GKPLADFQALQFKLADMATELVasrlMVRRAASALDRgDPDAVKLC-AMAKRFATDEC---FDVANQALQLHGGYGYLKD 341

                         250       260       270
                  ....*....|....*....|....*....|
gi 1024869198 226 YHVIRHVMNLEAVNTYEGTHDVHALILGRA 255
Cdd:cd01162   342 YPVEQYVRDLRVHQILEGTNEIMRLIIARA 371
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 2-254 2.91e-48

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 164.66  E-value: 2.91e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   2 TGEWVGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWANLDGK-----INGFVVERGFDGFST 76
Cdd:PLN02519  139 SGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAagskgITAFIIEKGMPGFST 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  77 PKIEGKFSLRASITGQIMLDDCFVPEENRLDVEGlKGPF---SCLNKARYGISWGAMGAAEFCWQAARQYTLDRKQFGRP 153
Cdd:PLN02519  219 AQKLDKLGMRGSDTCELVFENCFVPEENVLGQEG-KGVYvmmSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRP 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 154 LAATQLIQKKLADMQTEITLGLQGALQLGRLMDAGNWSPE---MVSLMKRNNcgkAIDIARQARDMHGGNGISDEYHVIR 230
Cdd:PLN02519  298 IGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKdcaGVILCAAER---ATQVALQAIQCLGGNGYINEYPTGR 374

                         250       260
                  ....*....|....*....|....
gi 1024869198 231 HVMNLEAVNTYEGTHDVHALILGR 254
Cdd:PLN02519  375 LLRDAKLYEIGAGTSEIRRMLIGR 398
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 1-254 1.32e-43

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: 151.50  E-value: 1.32e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWANLDGKING------FVVERGFDGF 74
Cdd:cd01160   108 VAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGGEARGaggislFLVERGTPGF 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  75 STPKIEGKFSLRASITGQIMLDDCFVPEENRLDVEGlKGPFSC---LNKARYGISWGAMGAAEFCWQAARQYTLDRKQFG 151
Cdd:cd01160   188 SRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEEN-KGFYYLmqnLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFG 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 152 RPLAATQLIQKKLADMQTEITLGLQGALQLGRLMDAGNWSPEMVSLMKrNNCGKAID-IARQARDMHGGNGISDEYHVIR 230
Cdd:cd01160   267 KTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAK-YWATELQNrVAYECVQLHGGWGYMREYPIAR 345

                         250       260
                  ....*....|....*....|....
gi 1024869198 231 HVMNLEAVNTYEGTHDVHALILGR 254
Cdd:cd01160   346 AYRDARVQPIYGGTTEIMKELISR 369
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 2-166 1.45e-36

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 133.91  E-value: 1.45e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   2 TGEWVGCFGLTEPDHGSDPGSMSTHAKKV-DGGYVLNGAKTWITNSPIADVAVVWANLDGKINGFVVERGFDGFST-PKI 79
Cdd:PTZ00461  148 TGEHVGAMGMSEPGAGTDVLGMRTTAKKDsNGNYVLNGSKIWITNGTVADVFLIYAKVDGKITAFVVERGTKGFTQgPKI 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  80 EgKFSLRASITGQIMLDDCFVPEENRLDVE--GLKGPFSCLNKARYGISWGAMGAAEFCWQAARQYTLDRKQFGRPLAAT 157
Cdd:PTZ00461  228 D-KCGMRASHMCQLFFEDVVVPAENLLGEEgkGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNF 306


                  ....*....
gi 1024869198 158 QLIQKKLAD 166
Cdd:PTZ00461  307 GQIQRYIAE 315
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 11-258 4.93e-32

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: 121.15  E-value: 4.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  11 LTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWANLD-------GK-INGFVVERGFDGFSTPKIEGK 82
Cdd:cd01157   120 VTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDpdpkcpaSKaFTGFIVEADTPGIQPGRKELN 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  83 FSLRASITGQIMLDDCFVPEENRLDVEG--LKGPFSCLNKARYGISWGAMGAAEFCWQAARQYTLDRKQFGRPLAATQLI 160
Cdd:cd01157   200 MGQRCSDTRGITFEDVRVPKENVLIGEGagFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAV 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 161 QKKLADMQTEITLGLQGALQLGRLMDAGNWSPEMVSLMKRNNCGKAIDIARQARDMHGGNGISDEYHVIRHVMNLEAVNT 240
Cdd:cd01157   280 SFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQI 359

                         250
                  ....*....|....*...
gi 1024869198 241 YEGTHDVHALILGRAQTG 258
Cdd:cd01157   360 YEGTSQIQRLIISREHLG 377
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 109-255 1.49e-28

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: 106.18  E-value: 1.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 109 EGLKGPFSCLNKARYGISWGAMGAAEFCWQAARQYTLDRKQFGRPLAATQLIQKKLADMQTEITLGLQGALQLGRLMDAG 188
Cdd:pfam00441   2 RGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024869198 189 NWSPEMVSLMKRNNCGKAIDIARQARDMHGGNGISDEYHVIRHVMNLEAVNTYEGTHDVHALILGRA 255
Cdd:pfam00441  82 GPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARR 148
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 8-96 1.39e-24

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: 93.88  E-value: 1.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   8 CFGLTEPDHGSDPGSMSTHAKKVDGG-YVLNGAKTWITNSPIADVAVVWA-----NLDGKINGFVVERGFDGFSTPKIEG 81
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAADGDGGgWVLNGTKWWITNAGIADLFLVLArtggdDRHGGISLFLVPKDAPGVSVRRIET 80

                          90
                  ....*....|....*
gi 1024869198  82 KFSLRASITGQIMLD 96
Cdd:pfam02770  81 KLGVRGLPTGELVFD 95
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 1-254 6.48e-23

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: 6.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHA-KKVDGGYVLNGAKTWITN--SPIADVAV--VWANLDGKING------FVV-- 67
Cdd:cd01153   113 AEGEWTGTMCLTEPDAGSDLGALRTKAvYQADGSWRINGVKRFISAgeHDMSENIVhlVLARSEGAPPGvkglslFLVpk 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  68 -----ERGfdGFSTPKIEGKFSLRASITGQIMLDDC---FVPEENRldveGLKGPFSCLNKARYGISWGAMGAAEFCWQA 139
Cdd:cd01153   193 flddgERN--GVTVARIEEKMGLHGSPTCELVFDNAkgeLIGEEGM----GLAQMFAMMNGARLGVGTQGTGLAEAAYLN 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 140 ARQYTLDRKQFGRPLAA--------------TQLIQKKLA------DMQT--EITLGLQGALQLGRLMDAGNWSPEMVSL 197
Cdd:cd01153   267 ALAYAKERKQGGDLIKAapavtiihhpdvrrSLMTQKAYAegsralDLYTatVQDLAERKATEGEDRKALSALADLLTPV 346

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1024869198 198 MKRNNCGKAIDIARQARDMHGGNGISDEYHVIRHVMNLEAVNTYEGTHDVHAL-ILGR 254
Cdd:cd01153   347 VKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALdLIGR 404
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 5-250 1.91e-21

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: 92.43  E-value: 1.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   5 WVGCFGLTEPDHGSDPGSMSTHAKKVDGG-YVLNGAKtWITNSPIADVAVVWANLDGKING------FVVER-----GFD 72
Cdd:cd01154   147 LLGGTWMTEKQGGSDLGANETTAERSGGGvYRLNGHK-WFASAPLADAALVLARPEGAPAGarglslFLVPRlledgTRN 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  73 GFSTPKIEGKFSLRASITGQIMLDDCfvpEENRL--DVEGLKGPFSCLNKARYGISWGAMGAAEFCWQAARQYTLDRKQF 150
Cdd:cd01154   226 GYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIgdEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAF 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 151 GRPLAATQLIQKKLADMQTEITLGLQGALQLGRLMD-AGNWSPE-------MVSLMKRNNCGKAIDIARQARDMHGGNGI 222
Cdd:cd01154   303 GKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDrAAADKPVeahmarlATPVAKLIACKRAAPVTSEAMEVFGGNGY 382

                         250       260
                  ....*....|....*....|....*...
gi 1024869198 223 SDEYHVIRHVMNLEAVNTYEGTHDVHAL 250
Cdd:cd01154   383 LEEWPVARLHREAQVTPIWEGTGNIQAL 410
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 2-255 9.78e-20

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 87.19  E-value: 9.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   2 TGEWVGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWANLDGKINGFVVERGFDGFSTPKIE- 80
Cdd:PRK03354  115 TGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVYTEWFVDMSKPGIKv 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  81 ---GKFSLRASITGQIMLDDCFVPEENRLDVEG-----LKGPFsclNKARYGISWGAMGAAEFCWQAARQYTLDRKQFGR 152
Cdd:PRK03354  195 tklEKLGLRMDSCCEITFDDVELDEKDMFGREGngfnrVKEEF---DHERFLVALTNYGTAMCAFEDAARYANQRVQFGE 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 153 PLAATQLIQKKLADMQTEITLGLQGALQLGRLMDAGNWSPEMVSLMKRNNCGKAIDIARQARDMHGGNGISDEYHVIRHV 232
Cdd:PRK03354  272 AIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFW 351

                         250       260
                  ....*....|....*....|...
gi 1024869198 233 MNLEAVNTYEGTHDVHALILGRA 255
Cdd:PRK03354  352 RDLRVDRVSGGSDEMQILTLGRA 374
PRK12341 PRK12341
acyl-CoA dehydrogenase;
1-171 1.02e-18

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 84.39  E-value: 1.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWA-NLDGKINGFVVERGFDGFSTP-- 77
Cdd:PRK12341  114 ETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLArDPQPKDPKKAFTLWWVDSSKPgi 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  78 KIE--GKFSLRASITGQIMLDDCFVPEENRLDVEGlKGpFSCLNK----ARYGISWGAMGAAEFCWQAARQYTLDRKQFG 151
Cdd:PRK12341  194 KINplHKIGWHMLSTCEVYLDNVEVEESDLVGEEG-MG-FLNVMYnfemERLINAARSLGFAECAFEDAARYANQRIQFG 271

                         170       180
                  ....*....|....*....|
gi 1024869198 152 RPLAATQLIQKKLADMQTEI 171
Cdd:PRK12341  272 KPIGHNQLIQEKLTLMAIKI 291
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 1-147 1.63e-11

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 63.73  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHAKKV-DGGYVLNGAKTWIT----NSPIADVAVVWANLDGKING------FVVER 69
Cdd:PTZ00456  177 VSGEWSGTMCLTEPQCGTDLGQVKTKAEPSaDGSYKITGTKIFISagdhDLTENIVHIVLARLPNSLPTtkglslFLVPR 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  70 GF---DG-FSTPK------IEGKFSLRASITGQIMLDDC---FVPEENrldvEGLKGPFSCLNKARYGISWGAMGAAEFC 136
Cdd:PTZ00456  257 HVvkpDGsLETAKnvkcigLEKKMGIKGSSTCQLSFENSvgyLIGEPN----AGMKQMFTFMNTARVGTALEGVCHAELA 332

                         170
                  ....*....|.
gi 1024869198 137 WQAARQYTLDR 147
Cdd:PTZ00456  333 FQNALRYARER 343
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 1-224 9.72e-09

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 55.73  E-value: 9.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHA----KKVDGGYVL----NGAKTWITNSPIADV---AVVWANLDGKINGFVVEr 69
Cdd:PRK13026  188 ADGTEIPCFALTGPEAGSDAGAIPDTGivcrGEFEGEEVLglrlTWDKRYITLAPVATVlglAFKLRDPDGLLGDKKEL- 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  70 gfdGF-------STPKIE--------GKFSLRASITGQimldDCFVPeenrLD-VEGlkGP----------FSCLNKARy 123
Cdd:PRK13026  267 ---GItcaliptDHPGVEigrrhnplGMAFMNGTTRGK----DVFIP----LDwIIG--GPdyagrgwrmlVECLSAGR- 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 124 GISWGAMGAA--EFCWQAARQYTLDRKQFGRPLAATQLIQKKLADMqteitLGLQGALQLGRLM-----DAGNwSPEMVS 196
Cdd:PRK13026  333 GISLPALGTAsgHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARI-----AGNTYLLEAARRLtttglDLGV-KPSVVT 406

                         250       260
                  ....*....|....*....|....*....
gi 1024869198 197 -LMKRNNCGKAIDIARQARDMHGGNGISD 224
Cdd:PRK13026  407 aIAKYHMTELARDVVNDAMDIHAGKGIQL 435
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 1-218 1.22e-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: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMSTHAKKVDGGYVLNGAKTWITNSPIADVAVVWANLDG---KING---FVVERGFDGF 74
Cdd:cd01152   113 LSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPeapKHRGisiLLVDMDSPGV 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  75 STPKIegKFSLRASITGQIMLDDCFVPEENRLDVE--GLKGPFSCLNKARYGI----SWGAMGAAEFCWQAARQytldrk 148
Cdd:cd01152   193 TVRPI--RSINGGEFFNEVFLDDVRVPDANRVGEVndGWKVAMTTLNFERVSIggsaATFFELLLARLLLLTRD------ 264

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 149 qfGRPLAATQLIQKKLADMQTEITLGLQGALQLGRLMDAGNWSPEMVSLMKRNNCGKAIDIARQARDMHG 218
Cdd:cd01152   265 --GRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLG 332
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 3-247 2.07e-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: 54.64  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   3 GEWVGCFGLTEPDHGSDPGSMSTHAK--KVDGGYVLN-----GAKTWITN-SPIADVAVVWANL--DGK---INGFVVE- 68
Cdd:cd01150   132 LEIIGCFAQTELGHGSNLQGLETTATydPLTQEFVINtpdftATKWWPGNlGKTATHAVVFAQLitPGKnhgLHAFIVPi 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  69 RGFDGFST-PKIE-----GKFSLRASITGQIMLDDCFVPEENRL----DV--EGL-KGPFSCLNKaRYGISWG------- 128
Cdd:cd01150   212 RDPKTHQPlPGVTvgdigPKMGLNGVDNGFLQFRNVRIPRENLLnrfgDVspDGTyVSPFKDPNK-RYGAMLGtrsggrv 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 129 --AMGAAEFCWQA---ARQYTLDRKQFGRP---------------------LAATQLI---QKKLADMQTEITLGL-QGA 178
Cdd:cd01150   291 glIYDAAMSLKKAatiAIRYSAVRRQFGPKpsdpevqildyqlqqyrlfpqLAAAYAFhfaAKSLVEMYHEIIKELlQGN 370

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024869198 179 LQLGRLMDAgnwspeMVSLMKRNN---CGKAIDIARQArdmHGGNGISDE--YHVIRhVMNlEAVNTYEGTHDV 247
Cdd:cd01150   371 SELLAELHA------LSAGLKAVAtwtAAQGIQECREA---CGGHGYLAMnrLPTLR-DDN-DPFCTYEGDNTV 433
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 3-256 3.80e-08

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: 53.55  E-value: 3.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   3 GEWVGCFGLTEPD-HGSDPGSMSTHAKKVDGGYVLNGAKTWITNSpiadvavvwANLDGKINGFVVERGFDGFS------ 75
Cdd:cd01155   123 GKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGA---------GDPRCKIAIVMGRTDPDGAPrhrqqs 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  76 -------TPKIEGKFSLraSITGQ---------IMLDDCFVPEENRLDVEGlKGpfsclnkarYGISWG----------- 128
Cdd:cd01155   194 milvpmdTPGVTIIRPL--SVFGYddaphghaeITFDNVRVPASNLILGEG-RG---------FEIAQGrlgpgrihhcm 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 129 -AMGAAEFCWQAARQYTLDRKQFGRPLAATQLIQKKLADMQTEITLGLQGALQLGRLMDA-GNWSPE-MVSLMKRNNCGK 205
Cdd:cd01155   262 rLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTvGNKAARkEIAMIKVAAPRM 341

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1024869198 206 AIDIARQARDMHGGNGISDEYHVIRHVMNLEAVNTYEGTHDVHALILGRAQ 256
Cdd:cd01155   342 ALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARME 392
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 1-167 1.71e-05

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 45.58  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198   1 ATGEWVGCFGLTEPDHGSDPGSMsthakkVDGGYV--------------LNGAKTWITNSPIADV--------------- 51
Cdd:PRK09463  189 ARGEEIPCFALTSPEAGSDAGSI------PDTGVVckgewqgeevlgmrLTWNKRYITLAPIATVlglafklydpdgllg 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  52 ---------AVVWANLDGkingfvVERG------FDGFSTPKIEGKfslrasitgqimldDCFVP-------EEN----- 104
Cdd:PRK09463  263 dkedlgitcALIPTDTPG------VEIGrrhfplNVPFQNGPTRGK--------------DVFIPldyiiggPKMagqgw 322

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024869198 105 RLDVEglkgpfsCLNKARyGISWGAM--GAAEFCWQAARQYTLDRKQFGRPLAATQLIQKKLADM 167
Cdd:PRK09463  323 RMLME-------CLSVGR-GISLPSNstGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARI 379
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 10-250 1.78e-03

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 39.35  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  10 GLTEPDHGSDPGSMSTHAKKVDGG-YVLNGAKtWITNSPIADVAVVWANLDGKINGFVVERGF-----DGFSTPKIEGKF 83
Cdd:PRK11561  183 GMTEKQGGSDVLSNTTRAERLADGsYRLVGHK-WFFSVPQSDAHLVLAQAKGGLSCFFVPRFLpdgqrNAIRLERLKDKL 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198  84 SLRASITGQIMLDDC---FVPEENrldvEGLKGPFSCLNKARYGISWGAMGAAEFCWQAARQYTLDRKQFGRPLAATQLI 160
Cdd:PRK11561  262 GNRSNASSEVEFQDAigwLLGEEG----EGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLM 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024869198 161 QKKLADMqteiTLGLQGA----LQLGRLMDAGN------WSPEMVSLMKRNNCGKAIDIARQARDMHGGNGISDEYHVIR 230
Cdd:PRK11561  338 RQVLSRM----ALQLEGQtallFRLARAWDRRAdakealWARLFTPAAKFVICKRGIPFVAEAMEVLGGIGYCEESELPR 413

                         250       260
                  ....*....|....*....|
gi 1024869198 231 HVMNLEAVNTYEGTHDVHAL 250
Cdd:PRK11561  414 LYREMPVNSIWEGSGNIMCL 433
 
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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