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Conserved domains on  [gi|663511209|gb|AIF01812|]
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glutaryl-CoA dehydrogenase (GCDH, gcdH) [uncultured marine group II/III euryarchaeote KM3_14_H03]

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 ...
 7-386 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: 596.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209   7 DFYDIDALLTEEERMVRDMVRDWVDKEVIPNIEEACREGVFPDKWRVDLGEMGILGAPLKGYGCPGLSYIAYGLICQELE 86
Cdd:cd01151    5 DPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGYGCAGLSSVAYGLIAREVE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  87 RGDSGVRSFASVQGSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWI 166
Cdd:cd01151   85 RVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 167 TNGTTADLAVVWAKLD--GVIRGFIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRILPGVKGLKGPFSCLNN 244
Cdd:cd01151  165 TNSPIADVFVVWARNDetGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGPFKCLNN 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 245 ARYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTWIPEQISLAKM 324
Cdd:cd01151  245 ARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKR 324

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511209 325 NNVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGRHITGIQSF 386
Cdd:cd01151  325 NNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
 
Name Accession Description Interval E-value
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 7-386 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: 596.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209   7 DFYDIDALLTEEERMVRDMVRDWVDKEVIPNIEEACREGVFPDKWRVDLGEMGILGAPLKGYGCPGLSYIAYGLICQELE 86
Cdd:cd01151    5 DPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGYGCAGLSSVAYGLIAREVE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  87 RGDSGVRSFASVQGSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWI 166
Cdd:cd01151   85 RVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 167 TNGTTADLAVVWAKLD--GVIRGFIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRILPGVKGLKGPFSCLNN 244
Cdd:cd01151  165 TNSPIADVFVVWARNDetGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGPFKCLNN 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 245 ARYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTWIPEQISLAKM 324
Cdd:cd01151  245 ARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKR 324

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511209 325 NNVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGRHITGIQSF 386
Cdd:cd01151  325 NNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 12-382 4.11e-144

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: 414.24  E-value: 4.11e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  12 DALLTEEERMVRDMVRDWVDKEVIPNIEEACREGVFPDKWRVDLGEMGILGAPL-KGYGCPGLSYIAYGLICQELERGDS 90
Cdd:COG1960    2 DFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIpEEYGGLGLSLVELALVLEELARADA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  91 GVRSFASVQgSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWITNGT 170
Cdd:COG1960   82 SLALPVGVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 171 TADLAVVWAKLDG-----VIRGFIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRILPGV-KGLKGPFSCLNN 244
Cdd:COG1960  161 VADVILVLARTDPaaghrGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEgKGFKIAMSTLNA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 245 ARYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTWIPEQISLAKM 324
Cdd:COG1960  241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKL 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663511209 325 NNVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGRHITG 382
Cdd:COG1960  321 FATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
PLN02526 PLN02526
acyl-coenzyme A oxidase
 7-386 9.85e-97

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 294.45  E-value: 9.85e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209   7 DFYDIDALLTEEERMVRDMVRDWVDKEVIPNIEEACREGVFPDKWRVDLGEMGILGAPLKGYGCPGLSYIAYGLICQELE 86
Cdd:PLN02526  21 DYYQFDDLLTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIKGYGCPGLSITASAIATAEVA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  87 RGDSGVRSFASVQGSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWI 166
Cdd:PLN02526 101 RVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWI 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 167 TNGTTADLAVVWAKLDGV--IRGFIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRILPGVKGLKGPFSCLNN 244
Cdd:PLN02526 181 GNSTFADVLVIFARNTTTnqINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSFQDTNKVLAV 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 245 ARYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTWIPEQISLAKM 324
Cdd:PLN02526 261 SRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKA 340

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511209 325 NNVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGRHITGIQSF 386
Cdd:PLN02526 341 WITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIASF 402
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 16-127 1.02e-43

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


Pssm-ID: 460686 [Multi-domain]  Cd Length: 113  Bit Score: 147.61  E-value: 1.02e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209   16 TEEERMVRDMVRDWVDKEVIPNIEEACREGVFP-DKWRvDLGEMGILGAPL-KGYGCPGLSYIAYGLICQELERGDSGVR 93
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPrELWK-KLGELGLLGITIpEEYGGAGLDYLAYALVAEELARADASVA 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 663511209   94 SFASVQGSLAMYPIWDFGSEEQKNHYLPGMATGE 127
Cdd:pfam02771  80 LALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
 
Name Accession Description Interval E-value
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 7-386 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: 596.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209   7 DFYDIDALLTEEERMVRDMVRDWVDKEVIPNIEEACREGVFPDKWRVDLGEMGILGAPLKGYGCPGLSYIAYGLICQELE 86
Cdd:cd01151    5 DPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGYGCAGLSSVAYGLIAREVE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  87 RGDSGVRSFASVQGSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWI 166
Cdd:cd01151   85 RVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 167 TNGTTADLAVVWAKLD--GVIRGFIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRILPGVKGLKGPFSCLNN 244
Cdd:cd01151  165 TNSPIADVFVVWARNDetGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGPFKCLNN 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 245 ARYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTWIPEQISLAKM 324
Cdd:cd01151  245 ARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKR 324

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511209 325 NNVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGRHITGIQSF 386
Cdd:cd01151  325 NNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 12-382 4.11e-144

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: 414.24  E-value: 4.11e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  12 DALLTEEERMVRDMVRDWVDKEVIPNIEEACREGVFPDKWRVDLGEMGILGAPL-KGYGCPGLSYIAYGLICQELERGDS 90
Cdd:COG1960    2 DFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIpEEYGGLGLSLVELALVLEELARADA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  91 GVRSFASVQgSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWITNGT 170
Cdd:COG1960   82 SLALPVGVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 171 TADLAVVWAKLDG-----VIRGFIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRILPGV-KGLKGPFSCLNN 244
Cdd:COG1960  161 VADVILVLARTDPaaghrGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEgKGFKIAMSTLNA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 245 ARYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTWIPEQISLAKM 324
Cdd:COG1960  241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKL 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663511209 325 NNVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGRHITG 382
Cdd:COG1960  321 FATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 17-380 4.01e-110

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: 327.30  E-value: 4.01e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  17 EEERMVRDMVRDWVDKEVIPNIEEACREGVFPDKWRVDLGEMGILGAPL-KGYGCPGLSYIAYGLICQELERGDSGVRSF 95
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIpEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  96 ASVQGSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWITNGTTADLA 175
Cdd:cd01158   81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 176 VVWAKLDGV-----IRGFIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRIL--PGvKGLKGPFSCLNNARYG 248
Cdd:cd01158  161 IVFAVTDPSkgyrgITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILgeEG-EGFKIAMQTLDGGRIG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 249 ISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTWIPEQISLAKMNNVD 328
Cdd:cd01158  240 IAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASE 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663511209 329 IALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGRHI 380
Cdd:cd01158  320 VAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
PLN02526 PLN02526
acyl-coenzyme A oxidase
 7-386 9.85e-97

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 294.45  E-value: 9.85e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209   7 DFYDIDALLTEEERMVRDMVRDWVDKEVIPNIEEACREGVFPDKWRVDLGEMGILGAPLKGYGCPGLSYIAYGLICQELE 86
Cdd:PLN02526  21 DYYQFDDLLTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIKGYGCPGLSITASAIATAEVA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  87 RGDSGVRSFASVQGSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWI 166
Cdd:PLN02526 101 RVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWI 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 167 TNGTTADLAVVWAKLDGV--IRGFIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRILPGVKGLKGPFSCLNN 244
Cdd:PLN02526 181 GNSTFADVLVIFARNTTTnqINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSFQDTNKVLAV 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 245 ARYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTWIPEQISLAKM 324
Cdd:PLN02526 261 SRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKA 340

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511209 325 NNVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGRHITGIQSF 386
Cdd:PLN02526 341 WITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIASF 402
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 17-378 2.28e-92

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: 280.32  E-value: 2.28e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  17 EEERMVRDMVRDWVDKEVIPNIEEACREGVFPDKWRVDLGEMGilgaplkgygcpglsyiayglicqelergdsgvrsfa 96
Cdd:cd00567    1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLL------------------------------------- 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  97 svqgslAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWITNGTTADLAV 176
Cdd:cd00567   44 ------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 177 VWAKLDG------VIRGFIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRILPGV-KGLKGPFSCLNNARYGI 249
Cdd:cd00567  118 VLARTDEegpghrGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEgGGFELAMKGLNVGRLLL 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 250 SWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGT-WIPEQISLAKMNNVD 328
Cdd:cd00567  198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPdEARLEAAMAKLFATE 277

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 663511209 329 IALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGR 378
Cdd:cd00567  278 AAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 15-378 9.31e-89

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: 272.75  E-value: 9.31e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  15 LTEEERMVRDMVRDWVDKEVIPNIEEACREGVFP-DKWRvDLGEMGILG--APLKgYGCPGLSYIAYGLICQELERGDSG 91
Cdd:cd01156    2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPrDLWR-KMGKLGLLGitAPEE-YGGSGMGYLAHVIIMEEISRASGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  92 VRSFASVQGSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWITNGTT 171
Cdd:cd01156   80 VALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 172 ADLAVVWAKLDGV-----IRGFIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRILPGV-KGLKGPFSCLNNA 245
Cdd:cd01156  160 ADTLVVYAKTDPSagahgITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGEnKGVYVLMSGLDYE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 246 RYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTWIPEQISLAKMN 325
Cdd:cd01156  240 RLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILY 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663511209 326 NVDIALEIARMSRDIHGANGILDEYPVMRHmanLESVKTYE---GTHDIHNLILGR 378
Cdd:cd01156  320 AAEKATQVALDAIQILGGNGYINDYPTGRL---LRDAKLYEigaGTSEIRRMVIGR 372
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 15-384 8.18e-69

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: 222.34  E-value: 8.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  15 LTEEERMVRDMVRDWVDKEVIPNIEEAcrEGVFPDKWRVDLGEMGILGAPL-KGYGCPGLSYIAYGLICQELERgDSGVR 93
Cdd:cd01161   27 QTEELNMLVGPVEKFFEEVNDPAKNDQ--LEKIPRKTLTQLKELGLFGLQVpEEYGGLGLNNTQYARLAEIVGM-DLGFS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  94 SFASVQGSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAE--DKGDHYLLNGAKMWITNGTT 171
Cdd:cd01161  104 VTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVlsEDGKHYVLNGSKIWITNGGI 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 172 ADLAVVWAKLDGV---------IRGFIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRILPGV-KGLKGPFSC 241
Cdd:cd01161  184 ADIFTVFAKTEVKdatgsvkdkITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVgDGFKVAMNI 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 242 LNNARYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTWIPEQISl 321
Cdd:cd01161  264 LNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQIE- 342

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663511209 322 AKMNNVdIALEIARMSRD----IHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGrhITGIQ 384
Cdd:cd01161  343 AAISKV-FASEAAWLVVDeaiqIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIA--LTGLQ 406
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 17-380 1.20e-68

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: 220.83  E-value: 1.20e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  17 EEERMVRDMVRDWVDKEVIPNIEEACREGVFPDK-WRvDLGEMGILGAPL-KGYGCPGLSYIAYGLICQELERGDSGVRS 94
Cdd:cd01160    1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREvWR-KAGEQGLLGVGFpEEYGGIGGDLLSAAVLWEELARAGGSGPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  95 FaSVQGSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWITNGTTADL 174
Cdd:cd01160   80 L-SLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 175 AVVWAKLDGVIRG------FIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRILPGV-KGLKGPFSCLNNARY 247
Cdd:cd01160  159 VIVVARTGGEARGaggislFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEEnKGFYYLMQNLPQERL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 248 GISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTWIPEQISLAKMNNV 327
Cdd:cd01160  239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWAT 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663511209 328 DIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGRHI 380
Cdd:cd01160  319 ELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 15-382 3.32e-66

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: 214.61  E-value: 3.32e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  15 LTEEERMVRDMVRDWVDKEVIPNIEEACREGVFPDKWRVDLGEMGILGAPLKG-YGCPGLSYIAYGLICQELERGDSGVR 93
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDdVGGSGLSRLDASIIFEALSTGCVSTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  94 SFASVQgSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWITNGTTAD 173
Cdd:cd01162   81 AYISIH-NMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 174 LAVVWAKLDGV----IRGFIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIP-KDRILPGVKGLKGPFSCLNNARYG 248
Cdd:cd01162  160 VYVVMARTGGEgpkgISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPvENRLGGEGQGFGIAMAGLNGGRLN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 249 ISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTwiPEQISL---AKMN 325
Cdd:cd01162  240 IASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGD--PDAVKLcamAKRF 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663511209 326 NVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGRHITG 382
Cdd:cd01162  318 ATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 15-382 7.36e-62

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: 203.59  E-value: 7.36e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  15 LTEEERMVRDMVRDWVDKEVIPNIEEACREGVFPDKWRVDLGEMGILGAPL-KGYGCPGLSYIAYGLICQELERGDSGVR 93
Cdd:cd01157    1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIpEDCGGLGLGTFDTCLITEELAYGCTGVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  94 SfASVQGSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWITNGTTAD 173
Cdd:cd01157   81 T-AIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKAN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 174 LAVVWAKLD--------GVIRGFIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRILPGV-KGLKGPFSCLNN 244
Cdd:cd01157  160 WYFLLARSDpdpkcpasKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEgAGFKIAMGAFDK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 245 ARYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTWIPEQISLAKM 324
Cdd:cd01157  240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKA 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663511209 325 NNVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGRHITG 382
Cdd:cd01157  320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 12-380 3.84e-58

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 194.71  E-value: 3.84e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  12 DALLTEEERMVRDMVRDWVDKEVIPNIEEACREGVFP---DKWRVdLGEMGILG--APLKgYGCPGLSYIAYGLICQELE 86
Cdd:PLN02519  23 SLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdvNLWKL-MGDFNLHGitAPEE-YGGLGLGYLYHCIAMEEIS 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  87 RGDSGVRSFASVQGSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWI 166
Cdd:PLN02519 101 RASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWC 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 167 TNGTTADLAVVWAKLDGV-----IRGFIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRILPGV-KGLKGPFS 240
Cdd:PLN02519 181 TNGPVAQTLVVYAKTDVAagskgITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEgKGVYVMMS 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 241 CLNNARYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTWIPEQIS 320
Cdd:PLN02519 261 GLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCA 340

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663511209 321 LAKMNNVDIALEIARMSRDIHGANGILDEYPVMRHmanLESVKTYE---GTHDIHNLILGRHI 380
Cdd:PLN02519 341 GVILCAAERATQVALQAIQCLGGNGYINEYPTGRL---LRDAKLYEigaGTSEIRRMLIGREL 400
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 1-354 5.21e-44

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 157.41  E-value: 5.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209   1 MAYEALDFYDIDALlTEEERMVRDMVRDWVDKEVIPNIEEACREGVFPDKWRVDLGEMGILGAPL-KGYGCPGLSYIAYG 79
Cdd:PTZ00461  24 MTSASRAFMDLYNP-TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVpEADGGAGMDAVAAV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  80 LICQELERGDSGvrsFASVQGSLAMYPIWDF---GSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGD- 155
Cdd:PTZ00461 103 IIHHELSKYDPG---FCLAYLAHSMLFVNNFyysASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNg 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 156 HYLLNGAKMWITNGTTADLAVVWAKLDGVIRGFIVEKDDPGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRILPGV-KG 234
Cdd:PTZ00461 180 NYVLNGSKIWITNGTVADVFLIYAKVDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEgKG 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 235 LKGPFSCLNNARYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAY------HLGNK 308
Cdd:PTZ00461 260 MVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYsvshnvHPGNK 339

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 663511209 309 KDDGTwipeqiSLAKMNNVDIALEIARMSRDIHGANGILDEYPVMR 354
Cdd:PTZ00461 340 NRLGS------DAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVER 379
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 16-127 1.02e-43

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


Pssm-ID: 460686 [Multi-domain]  Cd Length: 113  Bit Score: 147.61  E-value: 1.02e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209   16 TEEERMVRDMVRDWVDKEVIPNIEEACREGVFP-DKWRvDLGEMGILGAPL-KGYGCPGLSYIAYGLICQELERGDSGVR 93
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPrELWK-KLGELGLLGITIpEEYGGAGLDYLAYALVAEELARADASVA 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 663511209   94 SFASVQGSLAMYPIWDFGSEEQKNHYLPGMATGE 127
Cdd:pfam02771  80 LALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 233-380 1.04e-33

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: 122.75  E-value: 1.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  233 KGLKGPFSCLNNARYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDG 312
Cdd:pfam00441   2 RGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663511209  313 TWIPEQISLAKMNNVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGRHI 380
Cdd:pfam00441  82 GPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
PRK12341 PRK12341
acyl-CoA dehydrogenase;
11-380 8.03e-33

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 126.77  E-value: 8.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  11 IDALLTEEERMVRDMVRDWVDKEVIPNIEEACRE-GVFPDKWRVDLGEMGI--LGAPLKGYGCPgLSYIAYGLICQELER 87
Cdd:PRK12341   1 MDFSLTEEQELLLASIRELITRNFPEEYFRTCDEnGTYPREFMRALADNGIsmLGVPEEFGGTP-ADYVTQMLVLEEVSK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  88 gdSGVRSFASVQGsLAMYPIWDFGSEEQ-KNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWI 166
Cdd:PRK12341  80 --CGAPAFLITNG-QCIHSMRRFGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 167 TNGTTADLAVVWAKLDG------VIRGFIVEKDDPGFSApEMTGKHSLKASVTSELVFQDCQI-PKDRIlpGVKGlKGPF 239
Cdd:PRK12341 157 TGAKEYPYMLVLARDPQpkdpkkAFTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVeESDLV--GEEG-MGFL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 240 SCLNN---ARYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGtwIP 316
Cdd:PRK12341 233 NVMYNfemERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNG--QS 310

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511209 317 EQIS--LAKMNNVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGRHI 380
Cdd:PRK12341 311 LRTSaaLAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQI 376
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 22-382 2.87e-30

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: 120.19  E-value: 2.87e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  22 VRDMVRDWVDKEVIPNIEEACREG-VFPDKwRV--------------DLGEMGiLGAPLKgYGCPGLSYIAYGLICQELE 86
Cdd:cd01153    1 VLEEVARLAENVLAPLNADGDREGpVFDDG-RVvvpppfkealdafaEAGWMA-LGVPEE-YGGQGLPITVYSALAEIFS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  87 RGDSGVRSFASVQGslAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGD-HYLLNGAKMW 165
Cdd:cd01153   78 RGDAPLMYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRF 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 166 ITNG--TTADLAV--VWAKLDGVIRG------FIVEK--DDPGFSAPEMTG---KHSLKASVTSELVFQDCQIPkdriLP 230
Cdd:cd01153  156 ISAGehDMSENIVhlVLARSEGAPPGvkglslFLVPKflDDGERNGVTVARieeKMGLHGSPTCELVFDNAKGE----LI 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 231 GVK--GLKGPFSCLNNARYGISWGAVGAAQSCFDSAKEYALSRIQFG-------------HPIASFQLIQNKLSWM---- 291
Cdd:cd01153  232 GEEgmGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGdlikaapavtiihHPDVRRSLMTQKAYAEgsra 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 292 --LREITKAQLLAYHLGNKKDDGTWipEQIS-----LAKMNNVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKT 364
Cdd:cd01153  312 ldLYTATVQDLAERKATEGEDRKAL--SALAdlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTI 389

                        410
                 ....*....|....*...
gi 663511209 365 YEGTHDIHNLILGRHITG 382
Cdd:cd01153  390 YEGTTGIQALDLIGRKIV 407
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 16-382 8.81e-29

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: 115.52  E-value: 8.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  16 TEEERMvRDMVRDWVDKEVIPNIEEACREGVFPD-----KWRVDLGEMGiLGAPL--KGYGCPGLSYIAYGLICQELERG 88
Cdd:cd01152    1 PSEEAF-RAEVRAWLAAHLPPELREESALGYREGredrrRWQRALAAAG-WAAPGwpKEYGGRGASLMEQLIFREEMAAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  89 DSGVRSFASVQGSLAmyP-IWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWIT 167
Cdd:cd01152   79 GAPVPFNQIGIDLAG--PtILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 168 NGTTADLAVVWAKLDGVI---RG---FIVEKDDPGFSA-P--EMTGKHSlkasvTSELVFQDCQIPKDRILPGV-KGLKG 237
Cdd:cd01152  157 GAHYADWAWLLVRTDPEApkhRGisiLLVDMDSPGVTVrPirSINGGEF-----FNEVFLDDVRVPDANRVGEVnDGWKV 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 238 PFSCLNNARygiswGAVGAAQSCF-DSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTWIP 316
Cdd:cd01152  232 AMTTLNFER-----VSIGGSAATFfELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG 306

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511209 317 EQISLAKMNNVDIALEIARMSRDIHGANGILDEYP--------VMRHManLESVKT--YEGTHDIHNLILGRHITG 382
Cdd:cd01152  307 AEASIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWEADY--LRSRATtiYGGTSEIQRNIIAERLLG 380
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 11-378 3.38e-28

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 113.77  E-value: 3.38e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  11 IDALLTEEERMVRDMVRDWVDKEVIPNIEEAC-REGVFPDKWRVDLGEMGI--LGAPlKGYGCPGLSYIAYGLICQELer 87
Cdd:PRK03354   1 MDFNLNDEQELFVAGIRELMASENWEAYFAECdRDSVYPERFVKALADMGIdsLLIP-EEHGGLDAGFVTLAAVWMEL-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  88 GDSGVRSFASVQGSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRAEDKGDHYLLNGAKMWIT 167
Cdd:PRK03354  78 GRLGAPTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFIT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 168 NGTTADLAVVWAKLD-----GVIRGFIVEKDDPGFSAPEMTgKHSLKASVTSELVFQDCQIPKDRIL----PGVKGLKGP 238
Cdd:PRK03354 158 SSAYTPYIVVMARDGaspdkPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFgregNGFNRVKEE 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 239 FsclNNARYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLLAYHLGNKKDDGTWIPEQ 318
Cdd:PRK03354 237 F---DHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGD 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 319 ISLAKMNNVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNLILGR 378
Cdd:PRK03354 314 AAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGR 373
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 131-218 2.84e-23

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: 92.73  E-value: 2.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  131 CFGLTEPDYGSNPGDMITRA-EDKGDHYLLNGAKMWITNGTTADLAVVWAKL-----DGVIRGFIVEKDDPGFSAPEMTG 204
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTggddrHGGISLFLVPKDAPGVSVRRIET 80

                          90
                  ....*....|....
gi 663511209  205 KHSLKASVTSELVF 218
Cdd:pfam02770  81 KLGVRGLPTGELVF 94
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 103-374 7.18e-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: 93.59  E-value: 7.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 103 AMYPIWDFGSEEQKnHYLPGMATGE----LIGCFGLTEPDYGSNPGDMITRAE-DKGDHYLLNGAKmWITNGTTADLAVV 177
Cdd:cd01154  119 AVYALRKYGPEELK-QYLPGLLSDRyktgLLGGTWMTEKQGGSDLGANETTAErSGGGVYRLNGHK-WFASAPLADAALV 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 178 WAKLDGVIRG------FIVEKDDP-----GFSAPEMTGKHSLKASVTSELVFQDCQipKDRILPGVKGLKGPFSCLNNAR 246
Cdd:cd01154  197 LARPEGAPAGarglslFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDAE--AYLIGDEGKGIYYILEMLNISR 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 247 YGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQLL------AYHLGNKKDDGTWIPEQI- 319
Cdd:cd01154  275 LDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALtfraarAFDRAAADKPVEAHMARLa 354

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663511209 320 -SLAKMNNVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHNL 374
Cdd:cd01154  355 tPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 22-378 8.85e-18

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: 83.98  E-value: 8.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  22 VRDMVRDWVDKEVIPNIEEACRE-GVFPDKWRV------DLGEM----GILGAPL-KGYGCPGLSYIAYGLICQELERGD 89
Cdd:cd01155    6 LRARVKAFMEEHVYPAEQEFLEYyAEGGDRWWTpppiieKLKAKakaeGLWNLFLpEVSGLSGLTNLEYAYLAEETGRSF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  90 SGVRSF---ASVQGSlaMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPG-DMITRAEDKGDHYLLNGAKMW 165
Cdd:cd01155   86 FAPEVFncqAPDTGN--MEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASSDAtNIECSIERDGDDYVINGRKWW 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 166 ITNGTTAD--LAVVWAKLDGVIRG-------FIVEKDDPGFSAPEMT---------GKHslkasvtSELVFQDCQIPKDR 227
Cdd:cd01155  164 SSGAGDPRckIAIVMGRTDPDGAPrhrqqsmILVPMDTPGVTIIRPLsvfgyddapHGH-------AEITFDNVRVPASN 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 228 ILPG-------VKGLKGPfsclnnARYGISWGAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLSWMLREITKAQL 300
Cdd:cd01155  237 LILGegrgfeiAQGRLGP------GRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARL 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 301 L----AYHL---GNKKDDGtwipeQISLAKMNNVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGTHDIHN 373
Cdd:cd01155  311 LvlkaAHMIdtvGNKAARK-----EIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHL 385


                 ....*
gi 663511209 374 LILGR 378
Cdd:cd01155  386 RSIAR 390
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 110-346 4.91e-16

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 79.86  E-value: 4.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 110 FGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDM-----ITRAEDKGDHYL---LNGAKMWITNGTTAD---LAVvw 178
Cdd:PRK09463 175 YGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIpdtgvVCKGEWQGEEVLgmrLTWNKRYITLAPIATvlgLAF-- 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 179 aKL---DGVIrGfivEKDDPGF-------SAPEM-TGKHSLKASVtselVFQ-------DCQIPKDRILPGVKGL-KG-- 237
Cdd:PRK09463 253 -KLydpDGLL-G---DKEDLGItcaliptDTPGVeIGRRHFPLNV----PFQngptrgkDVFIPLDYIIGGPKMAgQGwr 323

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 238 -PFSCLNNARyGISW--GAVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQNKLS------WMLREITKAQLLAYHLGNK 308
Cdd:PRK09463 324 mLMECLSVGR-GISLpsNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLAriagnaYLMDAARTLTTAAVDLGEK 402

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 663511209 309 kddgtwiPEQIS-LAKMNNVDIALEIARMSRDIHGANGI 346
Cdd:PRK09463 403 -------PSVLSaIAKYHLTERGRQVINDAMDIHGGKGI 434
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 100-348 1.44e-15

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 78.46  E-value: 1.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 100 GSLAMYpiwdFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDM-----ITRAEDKGDHYL---LNGAKMWITNGTT 171
Cdd:PRK13026 168 GELLTH----YGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIpdtgiVCRGEFEGEEVLglrLTWDKRYITLAPV 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 172 AD---LAVVWAKLDGVIRG--------FIVEKDDPG---------FSAPEMTGkhslkaSVTSELVFqdcqIPKDRILPG 231
Cdd:PRK13026 244 ATvlgLAFKLRDPDGLLGDkkelgitcALIPTDHPGveigrrhnpLGMAFMNG------TTRGKDVF----IPLDWIIGG 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 232 V----KGLKGPFSCLNNARyGISWGAVGAA--QSCFDSAKEYALSRIQFGHPIASFQLIQNKL------SWML---REIT 296
Cdd:PRK13026 314 PdyagRGWRMLVECLSAGR-GISLPALGTAsgHMATRTTGAYAYVRRQFGMPIGQFEGVQEALariagnTYLLeaaRRLT 392

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663511209 297 KAQLlayHLGNKkddgtwiPEQIS-LAKMNNVDIALEIARMSRDIHGANGILD 348
Cdd:PRK13026 393 TTGL---DLGVK-------PSVVTaIAKYHMTELARDVVNDAMDIHAGKGIQL 435
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 68-271 4.67e-14

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 73.75  E-value: 4.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  68 YGCPGLSYiAYGLICQELergdsgvrsFASVQGSLAMYP---------IWDFGSEEQKNHYLPGMATGELIGCFGLTEPD 138
Cdd:PTZ00456 122 YGGQALPL-SVGFITREL---------MATANWGFSMYPglsigaantLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQ 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 139 YGSNPGDMITRAEDKGD-HYLLNGAKMWITNG----TTADLAVVWAKLDGVIRG------FIV----EKDDPGFSAPE-- 201
Cdd:PTZ00456 192 CGTDLGQVKTKAEPSADgSYKITGTKIFISAGdhdlTENIVHIVLARLPNSLPTtkglslFLVprhvVKPDGSLETAKnv 271

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511209 202 ----MTGKHSLKASVTSELVFQDCQipkdRILPGV--KGLKGPFSCLNNARYGISWGAVGAAQSCFDSAKEYALSR 271
Cdd:PTZ00456 272 kcigLEKKMGIKGSSTCQLSFENSV----GYLIGEpnAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARER 343
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
248-368 1.09e-11

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 61.98  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  248 GISWGAVGAAQSCFDSAKEYALSRIQ--FGHPIASFQLIQNKLSWMLREITKAQLLAYHLG----NKKDDGTWIPE---- 317
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVTPalra 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 663511209  318 QISLAKMNNVDIALEIARMSRDIHGANGILDEYPVMRHMANLESVKTYEGT 368
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAV 131
PLN02876 PLN02876
acyl-CoA dehydrogenase
 72-372 6.57e-11

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 64.05  E-value: 6.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  72 GLSYIAYGLICQELERGDSGVRSF---ASVQGSlaMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMIT 148
Cdd:PLN02876 493 GLSNLEYGYLCEIMGRSVWAPQVFncgAPDTGN--MEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQVASSDATNIE 570

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 149 -RAEDKGDHYLLNGAKMWiTNGTT---ADLAVVWAKLD---------GVIrgfIVEKDDPGFSA--PEMTGKHSLKASVT 213
Cdd:PLN02876 571 cSIRRQGDSYVINGTKWW-TSGAMdprCRVLIVMGKTDfnapkhkqqSMI---LVDIQTPGVQIkrPLLVFGFDDAPHGH 646

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 214 SELVFQDCQIPKDRILPG-------VKGLKGPFSCLNNARYgiswgaVGAAQSCFDSAKEYALSRIQFGHPIASFQLIQN 286
Cdd:PLN02876 647 AEISFENVRVPAKNILLGegrgfeiAQGRLGPGRLHHCMRL------IGAAERGMQLMVQRALSRKAFGKLIAQHGSFLS 720

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 287 KLSWMLREITKAQLL----AYHL---GNKKDDGTwipeqISLAKMNNVDIALEIARMSRDIHGANGILDEYPVMRHMANL 359
Cdd:PLN02876 721 DLAKCRVELEQTRLLvleaADQLdrlGNKKARGI-----IAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATA 795

                        330
                 ....*....|...
gi 663511209 360 ESVKTYEGTHDIH 372
Cdd:PLN02876 796 RTLRIADGPDEVH 808
PLN02636 PLN02636
acyl-coenzyme A oxidase
 98-304 6.82e-10

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 60.64  E-value: 6.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  98 VQGSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRA--EDKGDHYLLN----GA-KMWITNGT 170
Cdd:PLN02636 143 VQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFVINtpndGAiKWWIGNAA 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 171 T-ADLAVVWAKL-----------DGVIRGFIVEKDD-------PGFSAPEMTGKHSLKASVTSELVFQDCQIPKDRI--- 228
Cdd:PLN02636 223 VhGKFATVFARLklpthdskgvsDMGVHAFIVPIRDmkthqvlPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLlnr 302

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 229 -------------LPGV-KGLKGPFSCLNNARYGISWGAVGAAQSCFDSAKEYALSRIQFGHP------IASFQLIQNKL 288
Cdd:PLN02636 303 fgdvsrdgkytssLPTInKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQHKL 382

                        250
                 ....*....|....*.
gi 663511209 289 SWMLreitkAQLLAYH 304
Cdd:PLN02636 383 MPML-----ASTYAFH 393
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 85-288 7.05e-10

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


Pssm-ID: 173839 [Multi-domain]  Cd Length: 610  Bit Score: 60.81  E-value: 7.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  85 LERGDSGVRSFASVQGSLAMYPIWDFGSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRA--EDKGDHYLLN-- 160
Cdd:cd01150   91 LGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQEFVINtp 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 161 ---GAKMWITN-GTTADLAVVWAKL--DGVIRG---FIVEKDD-------PGFSAPEMTGKHSLKASVTSELVFQDCQIP 224
Cdd:cd01150  171 dftATKWWPGNlGKTATHAVVFAQLitPGKNHGlhaFIVPIRDpkthqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIP 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 225 KDRIL--------------PG---VKGLKGPFSCLNNARYGISWGAVGAAQSCFDSAKEYALSRIQFGH-------PIAS 280
Cdd:cd01150  251 RENLLnrfgdvspdgtyvsPFkdpNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPkpsdpevQILD 330


                 ....*...
gi 663511209 281 FQLIQNKL 288
Cdd:cd01150  331 YQLQQYRL 338
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 92-382 7.77e-09

Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.


Pssm-ID: 173852 [Multi-domain]  Cd Length: 377  Bit Score: 56.95  E-value: 7.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  92 VRSFASVQGSLAMYP---------IWDFGSEEQKNHYLPGMATGELIGCfGLTEPDyGSNPGDMITRAEDKGDHYLLNGA 162
Cdd:cd01163   59 VRELAAADSNIAQALrahfgfveaLLLAGPEQFRKRWFGRVLNGWIFGN-AVSERG-SVRPGTFLTATVRDGGGYVLNGK 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 163 KMWITNGTTADLAVVWAKLD-GVIRGFIVEKDDPGFSAPE--------MTGKHSlkasvtseLVFQDCQIPKDRILPGVK 233
Cdd:cd01163  137 KFYSTGALFSDWVTVSALDEeGKLVFAAVPTDRPGITVVDdwdgfgqrLTASGT--------VTFDNVRVEPDEVLPRPN 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 234 GLKGPfsCLNNARYGISWGAV--GAAQSCFDSAKEYALSRIQ-FGHPIAS-----FQLIQ-----NKLSWMLREITK--A 298
Cdd:cd01163  209 APDRG--TLLTAIYQLVLAAVlaGIARAALDDAVAYVRSRTRpWIHSGAEsarddPYVQQvvgdlAARLHAAEALVLqaA 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 299 QLL----AYHLGNKKDDGTWIPEQISLAKMNNVDIALEIARMSRDIHGANGILDEYPVMRHMANLEsvktyegTHDIHN- 373
Cdd:cd01163  287 RALdaaaAAGTALTAEARGEAALAVAAAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR-------THTLHNp 359


                 ....*....
gi 663511209 374 LILGRHITG 382
Cdd:cd01163  360 VIYKERAVG 368
PLN02443 PLN02443
acyl-coenzyme A oxidase
 111-229 2.41e-05

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 46.37  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209 111 GSEEQKNHYLPGMATGELIGCFGLTEPDYGSNPGDMITRA--EDKGDHYLLN-----GAKMWITN-GTTADLAVVWAKL- 181
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTAtfDPKTDEFVIHsptltSSKWWPGGlGKVSTHAVVYARLi 193

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511209 182 ----DGVIRGFIVE---KDD----PGFSAPEMTGKHSLKASVTSE---LVFQDCQIPKDRIL 229
Cdd:PLN02443 194 tngkDHGIHGFIVQlrsLDDhsplPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQML 255
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 68-198 4.70e-04

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 42.18  E-value: 4.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511209  68 YGCPGLSYIAYGLICQELerGDSGV-RSFASVQGS-LAMYPIWDFGSEEQKNHYLPGMATGELIGCFGlTEPDYGSNPGD 145
Cdd:PTZ00457  74 YGGLGLGHTAHALIYEEV--GTNCDsKLLSTIQHSgFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISM 150

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511209 146 MITRAEDKGD-HYLLNGAKMWItNGTTADLAVVWAKL-------DG---VIRG--FIVEKDDPGFS 198
Cdd:PTZ00457 151 NTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKTltqtaaeEGateVSRNsfFICAKDAKGVS 215
 
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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