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Conserved domains on  [gi|71982178|ref|NP_495066|]
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Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial [Caenorhabditis elegans]

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 ...
 38-308 7.52e-122

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 cd01158:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 373  Bit Score: 353.88  E-value: 7.52e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  38 ENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALI 117
Cdd:cd01158   1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 118 MHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIADFF 196
Cdd:cd01158  81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATgEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 197 LVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNASRIVI 276
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                       250       260       270
                ....*....|....*....|....*....|..
gi 71982178 277 GAQMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADF 272
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 38-308 7.52e-122

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: 353.88  E-value: 7.52e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  38 ENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALI 117
Cdd:cd01158   1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 118 MHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIADFF 196
Cdd:cd01158  81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATgEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 197 LVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNASRIVI 276
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                       250       260       270
                ....*....|....*....|....*....|..
gi 71982178 277 GAQMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADF 272
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 35-308 2.30e-106

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: 314.86  E-value: 2.30e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  35 HLNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAI 114
Cdd:COG1960   4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 115 ALIMHLQNAlVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIA 193
Cdd:COG1960  84 ALPVGVHNG-AAEALLRFGTEEQKERYLPRLASgEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 194 DFFLVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNASR 273
Cdd:COG1960 163 DVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242

                       250       260       270
                ....*....|....*....|....*....|....*
gi 71982178 274 IVIGAQMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADF 277
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 36-308 1.86e-47

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 163.89  E-value: 1.86e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178   36 LNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQ--LLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPA 113
Cdd:PLN02519  26 FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDvnLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  114 IALIMHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPI 192
Cdd:PLN02519 106 VGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISgEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  193 ADFFLVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNAS 272
Cdd:PLN02519 186 AQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLE 265

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 71982178  273 RIVIGAQMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:PLN02519 266 RLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEF 301
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 37-147 6.77e-34

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: 119.88  E-value: 6.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178    37 NENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIAL 116
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 71982178   117 IMHLQNALVAPLIEEFGNEELKEKYLKKLCK 147
Cdd:pfam02771  81 ALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 38-308 7.52e-122

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: 353.88  E-value: 7.52e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  38 ENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALI 117
Cdd:cd01158   1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 118 MHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIADFF 196
Cdd:cd01158  81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATgEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 197 LVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNASRIVI 276
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                       250       260       270
                ....*....|....*....|....*....|..
gi 71982178 277 GAQMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADF 272
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 35-308 2.30e-106

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: 314.86  E-value: 2.30e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  35 HLNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAI 114
Cdd:COG1960   4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 115 ALIMHLQNAlVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIA 193
Cdd:COG1960  84 ALPVGVHNG-AAEALLRFGTEEQKERYLPRLASgEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 194 DFFLVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNASR 273
Cdd:COG1960 163 DVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242

                       250       260       270
                ....*....|....*....|....*....|....*
gi 71982178 274 IVIGAQMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADF 277
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 35-308 7.13e-79

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: 244.63  E-value: 7.13e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  35 HLNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAI 114
Cdd:cd01156   1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 115 ALIMHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIA 193
Cdd:cd01156  81 ALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISgEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 194 DFFLVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNASR 273
Cdd:cd01156 161 DTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYER 240

                       250       260       270
                ....*....|....*....|....*....|....*
gi 71982178 274 IVIGAQMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:cd01156 241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEF 275
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 38-308 1.10e-68

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: 216.77  E-value: 1.10e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  38 ENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKafdlklMGLkidpkyggsgvsffelvlaveelskidpaiali 117
Cdd:cd00567   1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAE------LGL--------------------------------- 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 118 mhlqnALVAPLIEEFGNEELKEKYLKKLCKDS-VGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIADFF 196
Cdd:cd00567  42 -----LLGAALLLAYGTEEQKERYLPPLASGEaIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 197 LVLANADPE-KGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNASRIV 275
Cdd:cd00567 117 IVLARTDEEgPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196

                       250       260       270
                ....*....|....*....|....*....|...
gi 71982178 276 IGAQMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEF 229
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 36-308 5.76e-62

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: 200.75  E-value: 5.76e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  36 LNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIA 115
Cdd:cd01162   1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 116 LIMHLQNaLVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIAD 194
Cdd:cd01162  81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTmEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 195 FFLVLANADpEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNASRI 274
Cdd:cd01162 160 VYVVMARTG-GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRL 238

                       250       260       270
                ....*....|....*....|....*....|....
gi 71982178 275 VIGAQMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:cd01162 239 NIASCSLGAAQAALDLARAYLEERKQFGKPLADF 272
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 32-308 1.58e-56

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: 187.18  E-value: 1.58e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  32 PLQH---LNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDpKYGGSGVSFFELVLAVEELS 108
Cdd:cd01151   6 PLNLddlLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIAREVE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 109 KIDPAIALIMHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGI 187
Cdd:cd01151  85 RVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASgELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWI 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 188 SNAPIADFFLVLANADPEKGYRGvtcFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEyGKGYKYAIE 267
Cdd:cd01151 165 TNSPIADVFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPG-AEGLRGPFK 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71982178 268 VLNASRIVIGAQMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:cd01151 241 CLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAF 281
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 20-308 2.56e-56

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: 187.29  E-value: 2.56e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  20 GSISAQQqprVFPL-----QHLNENEKKLVEKVKNFAQSSVKPlvREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSG 94
Cdd:cd01161   9 GDIVTKQ---VFPYpsvltEEQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  95 VSFFELVLAVEELSkIDPAIALIMHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKK 173
Cdd:cd01161  84 LNNTQYARLAEIVG-MDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASgEWIAAFALTEPSSGSDAASIRTTAVL 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 174 --DGDHFILNGSKWGISNAPIADFFLVLAN-----ADPEKGyRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNS 246
Cdd:cd01161 163 seDGKHYVLNGSKIWITNGGIADIFTVFAKtevkdATGSVK-DKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFED 241

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71982178 247 VRVPKTSIVGEYGKGYKYAIEVLNASRIVIGAQMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:cd01161 242 VKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEF 303
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 47-307 5.43e-54

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: 180.00  E-value: 5.43e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  47 VKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKID-PAIALIMHlqNALV 125
Cdd:cd01160  10 VRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGgSGPGLSLH--TDIV 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 126 APLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIADFFLVLANADP 204
Cdd:cd01160  88 SPYITRAGSPEQKERVLPQMVAgKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGG 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 205 E-KGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNASRIVIGAQMVGL 283
Cdd:cd01160 168 EaRGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAA 247

                       250       260
                ....*....|....*....|....
gi 71982178 284 AQGCFDQTIPYLQERKQFGSRLID 307
Cdd:cd01160 248 AEFMLEETRNYVKQRKAFGKTLAQ 271
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 36-302 5.71e-49

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: 167.38  E-value: 5.71e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  36 LNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIA 115
Cdd:cd01157   1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 116 LIMHLQNALVAPLIEEfGNEELKEKYLKKLCKDS-VGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIAD 194
Cdd:cd01157  81 TAIEANSLGQMPVIIS-GNDEQKKKYLGRMTEEPlMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKAN 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 195 FFLVLANADPEK---GYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNA 271
Cdd:cd01157 160 WYFLLARSDPDPkcpASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDK 239

                       250       260       270
                ....*....|....*....|....*....|.
gi 71982178 272 SRIVIGAQMVGLAQGCFDQTIPYLQERKQFG 302
Cdd:cd01157 240 TRPPVAAGAVGLAQRALDEATKYALERKTFG 270
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 36-308 1.86e-47

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 163.89  E-value: 1.86e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178   36 LNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQ--LLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPA 113
Cdd:PLN02519  26 FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDvnLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  114 IALIMHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPI 192
Cdd:PLN02519 106 VGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISgEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  193 ADFFLVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNAS 272
Cdd:PLN02519 186 AQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLE 265

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 71982178  273 RIVIGAQMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:PLN02519 266 RLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEF 301
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 41-308 3.12e-45

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 158.18  E-value: 3.12e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178   41 KKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALIMHL 120
Cdd:PTZ00461  42 AALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLA 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  121 QNALVAPLIEEFGNEELKEKYLKK-LCKDSVGAFALSEVVSGSDAFAMQTVAKKDGD-HFILNGSKWGISNAPIADFFLV 198
Cdd:PTZ00461 122 HSMLFVNNFYYSASPAQRARWLPKvLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVADVFLI 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  199 LANADPEkgyrgVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNASRIVIGA 278
Cdd:PTZ00461 202 YAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAA 276

                        250       260       270
                 ....*....|....*....|....*....|
gi 71982178  279 QMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:PTZ00461 277 MAVGIAERSVELMTSYASERKAFGKPISNF 306
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 37-147 6.77e-34

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: 119.88  E-value: 6.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178    37 NENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIAL 116
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 71982178   117 IMHLQNALVAPLIEEFGNEELKEKYLKKLCK 147
Cdd:pfam02771  81 ALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
PLN02526 PLN02526
acyl-coenzyme A oxidase
 36-308 2.26e-31

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 121.11  E-value: 2.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178   36 LNENEKKLVEKVKNFAQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDpKYGGSGVSFFELVLAVEELSKIDPAIA 115
Cdd:PLN02526  29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK-GYGCPGLSITASAIATAEVARVDASCS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  116 LIMHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIAD 194
Cdd:PLN02526 108 TFILVHSSLAMLTIALCGSEAQKQKYLPSLAQlDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  195 FFLVLA-NADPEKgyrgVTCFIVDRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVP-KTSIVGEygKGYKYAIEVLNAS 272
Cdd:PLN02526 188 VLVIFArNTTTNQ----INGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPdEDRLPGV--NSFQDTNKVLAVS 261

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 71982178  273 RIVIGAQMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:PLN02526 262 RVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAF 297
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 152-236 9.47e-28

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: 103.51  E-value: 9.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178   152 AFALSEVVSGSDAFAMQTVA-KKDGDHFILNGSKWGISNAPIADFFLVLANADPEKGYRGVTCFIVDRDHEGVVLGEQDD 230
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80


                  ....*.
gi 71982178   231 NLGMRA 236
Cdd:pfam02770  81 KLGVRG 86
PRK12341 PRK12341
acyl-CoA dehydrogenase;
59-302 4.35e-27

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 109.05  E-value: 4.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178   59 VREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALImhlQNALVAPLIEEFGNEELK 138
Cdd:PRK12341  29 FRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGAPAFLI---TNGQCIHSMRRFGSAEQL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  139 EKYLKKLCKDSVGAFAL--SEVVSGSDAFAMQTVA-KKDGDhFILNGSKWGISNAPIADFFLVLA-NADPEKGYRGVTCF 214
Cdd:PRK12341 106 RKTAESTLETGDPAYALalTEPGAGSDNNSATTTYtRKNGK-VYLNGQKTFITGAKEYPYMLVLArDPQPKDPKKAFTLW 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  215 IVDRDHEGVVLgEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNASRIVIGAQMVGLAQGCFDQTIPY 294
Cdd:PRK12341 185 WVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARY 263


                 ....*...
gi 71982178  295 LQERKQFG 302
Cdd:PRK12341 264 ANQRIQFG 271
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 45-308 1.68e-25

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: 104.78  E-value: 1.68e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  45 EKVKNFAQSSVKPLVREMDR------DARIN-----KQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPA 113
Cdd:cd01153   3 EEVARLAENVLAPLNADGDRegpvfdDGRVVvpppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 114 IALIMHLQNAlvAPLIEEFGNEELKEKYLKKLC-KDSVGAFALSEVVSGSDAFAMQTVAKKDGD-HFILNGSKWGISNA- 190
Cdd:cd01153  83 LMYASGTQGA--AATLLAHGTEAQREKWIPRLAeGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGe 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 191 -----PIadFFLVLANA-DPEKGYRGVTCFIV-----DRDHEGVVLGEQDDNLGMRAGTIAQVHLNSVRVPktsIVGEYG 259
Cdd:cd01153 161 hdmseNI--VHLVLARSeGAPPGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEG 235

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 71982178 260 KGYKYAIEVLNASRIVIGAQMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:cd01153 236 MGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAA 284
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 88-278 3.10e-25

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: 103.97  E-value: 3.10e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  88 PK-YGGSGVSFFELVLAVEELSKIDPAIALIMHLQNaLVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAF 165
Cdd:cd01152  55 PKeYGGRGASLMEQLIFREEMAAAGAPVPFNQIGID-LAGPTILAYGTDEQKRRFLPPILSgEEIWCQGFSEPGAGSDLA 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 166 AMQTVAKKDGDHFILNGSKWGISNAPIADFFLVLANADPE-KGYRGVTCFIVDRDHEGVV-------LGEQDDNlgmrag 237
Cdd:cd01152 134 GLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEaPKHRGISILLVDMDSPGVTvrpirsiNGGEFFN------ 207

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 71982178 238 tiaQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNASRIVIGA 278
Cdd:cd01152 208 ---EVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGG 245
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 41-305 2.27e-22

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: 95.92  E-value: 2.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  41 KKLVEKVKNFAQSSVKPLVREMDRDARINK-----------QLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSK 109
Cdd:cd01155   4 QELRARVKAFMEEHVYPAEQEFLEYYAEGGdrwwtpppiieKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 110 idpaialimhlqnALVAP--------------LIEEFGNEELKEKYLKKLCKDSV-GAFALSEV-VSGSDAFAMQTVAKK 173
Cdd:cd01155  84 -------------SFFAPevfncqapdtgnmeVLHRYGSEEQKKQWLEPLLDGKIrSAFAMTEPdVASSDATNIECSIER 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 174 DGDHFILNGSKWGISNA--PIADFFLVLANADP--EKGYRGVTCFIVDRDHEGV-------VLGEQDDNLGMragtiAQV 242
Cdd:cd01155 151 DGDDYVINGRKWWSSGAgdPRCKIAIVMGRTDPdgAPRHRQQSMILVPMDTPGVtiirplsVFGYDDAPHGH-----AEI 225

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71982178 243 HLNSVRVPKTSIVGEYGKGYKYAIEVLNASRIVIGAQMVGLAQGCFDQTIPYLQERKQFGSRL 305
Cdd:cd01155 226 TFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKL 288
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 126-307 3.50e-22

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: 95.52  E-value: 3.50e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 126 APLIEEFGNEELKEKYLKKLCKDS----VGAFALSEVVSGSDAFAMQTVAKKD-GDHFILNGSKWGISnAPIADFFLVLA 200
Cdd:cd01154 120 VYALRKYGPEELKQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSgGGVYRLNGHKWFAS-APLADAALVLA 198

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 201 N-ADPEKGYRGVTCFIVDRDHE-----GVVLGEQDDNLGMRAGTIAQVHLNSVrvpKTSIVGEYGKGYKYAIEVLNASRI 274
Cdd:cd01154 199 RpEGAPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRL 275

                       170       180       190
                ....*....|....*....|....*....|...
gi 71982178 275 VIGAQMVGLAQGCFDQTIPYLQERKQFGSRLID 307
Cdd:cd01154 276 DNAVAALGIMRRALSEAYHYARHRRAFGKPLID 308
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 36-302 4.05e-16

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 77.95  E-value: 4.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178   36 LNENEKKLVEKVKNF-AQSSVKPLVREMDRDARINKQLLKKAFDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAI 114
Cdd:PRK03354   5 LNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  115 ALIMHLQNALVAPLIEefGNEELKEKYLKKL-CKDSVGAFALSEVVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIA 193
Cdd:PRK03354  85 YVLYQLPGGFNTFLRE--GTQEQIDKIMAFRgTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  194 DFFLVLA--NADPEKGYrgVTCFIVDRDHEGVVLgEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNA 271
Cdd:PRK03354 163 PYIVVMArdGASPDKPV--YTEWFVDMSKPGIKV-TKLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDH 239

                        250       260       270
                 ....*....|....*....|....*....|.
gi 71982178  272 SRIVIGAQMVGLAQGCFDQTIPYLQERKQFG 302
Cdd:PRK03354 240 ERFLVALTNYGTAMCAFEDAARYANQRVQFG 270
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 71-302 8.54e-16

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 77.69  E-value: 8.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178   71 QLLKKAfdlKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALIMHLQNALvAP--LIEEFGNEELKEKYLKKLCK- 147
Cdd:PRK13026 115 DYLKKE---GFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSL-GPgeLLTHYGTQEQKDYWLPRLADg 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  148 DSVGAFALSEVVSGSDAFAMQTVA-----KKDGDHFI---LNGSKWGISNAPIADfflVLANA----DPE-----KGYRG 210
Cdd:PRK13026 191 TEIPCFALTGPEAGSDAGAIPDTGivcrgEFEGEEVLglrLTWDKRYITLAPVAT---VLGLAfklrDPDgllgdKKELG 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  211 VTCFIVDRDHEGVVLGEQDDNLGMR--AGTIAQvhlNSVRVPKTSIVG--EY-GKGYKYAIEVLNASR-IVIGAQMVGLA 284
Cdd:PRK13026 268 ITCALIPTDHPGVEIGRRHNPLGMAfmNGTTRG---KDVFIPLDWIIGgpDYaGRGWRMLVECLSAGRgISLPALGTASG 344

                        250
                 ....*....|....*...
gi 71982178  285 QGCFDQTIPYLQERKQFG 302
Cdd:PRK13026 345 HMATRTTGAYAYVRRQFG 362
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 50-299 3.99e-15

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: 75.05  E-value: 3.99e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  50 FAQSSVKplvREMDRD-ARINKQLLKkafDLKLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALIMHLQNALVAPL 128
Cdd:cd01163  10 IAEGAAE---RDRQRGlPYEEVALLR---QSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVEAL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 129 IeEFGNEELKEKYLKKLCK-DSVGAfALSEvVSGSDAFAMQTVAKKDGDHFILNGSKWGISNAPIADFFLVLANADPEKg 207
Cdd:cd01163  84 L-LAGPEQFRKRWFGRVLNgWIFGN-AVSE-RGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGK- 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 208 yrgVTCFIVDRDHEGVVLGEQDDNLGMR---AGTiaqVHLNSVRVPKTSIVGeYGKGYKYAIEVLNASRIVIGAQMVGLA 284
Cdd:cd01163 160 ---LVFAAVPTDRPGITVVDDWDGFGQRltaSGT---VTFDNVRVEPDEVLP-RPNAPDRGTLLTAIYQLVLAAVLAGIA 232

                       250
                ....*....|....*
gi 71982178 285 QGCFDQTIPYLQERK 299
Cdd:cd01163 233 RAALDDAVAYVRSRT 247
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 259-308 3.49e-13

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: 65.74  E-value: 3.49e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 71982178   259 GKGYKYAIEVLNASRIVIGAQMVGLAQGCFDQTIPYLQERKQFGSRLIDF 308
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDF 50
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 1-298 1.66e-10

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 61.81  E-value: 1.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178    1 MFKVPRKLPISAISTFSTTGSISAQQQPRVFPLQHLNEN--------EK------------KLVEKVKNFAQSSVKPLVR 60
Cdd:PTZ00456   1 MFRRVCSSAAASHAAAVSASARSLQYQPRIRDVQFLVEEvfnmydhyEKlgktdvtkelmdSLLEEASKLATQTLLPLYE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178   61 EMDRDARI---NKQL-----LKKAFD-LK---LMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIA----LIMHLQNAL 124
Cdd:PTZ00456  81 SSDSEGCVllkDGNVttpkgFKEAYQaLKaggWTGISEPEEYGGQALPLSVGFITRELMATANWGFSmypgLSIGAANTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  125 VAplieeFGNEELKEKYLKKLCKDS-VGAFALSEVVSGSDAFAMQTVAKKDGD-HFILNGSKWGISnAPIADF-----FL 197
Cdd:PTZ00456 161 MA-----WGSEEQKEQYLTKLVSGEwSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFIS-AGDHDLtenivHI 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  198 VLA---NADPekGYRGVTCFIVDR----------DHEGVVLGEQDDNLGMRAGTIAQVHL-NSVrvpkTSIVGEYGKGYK 263
Cdd:PTZ00456 235 VLArlpNSLP--TTKGLSLFLVPRhvvkpdgsleTAKNVKCIGLEKKMGIKGSSTCQLSFeNSV----GYLIGEPNAGMK 308

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 71982178  264 YAIEVLNASRIVIGAQMVGLAQGCFDQTIPYLQER 298
Cdd:PTZ00456 309 QMFTFMNTARVGTALEGVCHAELAFQNALRYARER 343
PLN02876 PLN02876
acyl-CoA dehydrogenase
 132-305 2.47e-08

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 55.19  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  132 FGNEELKEKYLKKLCKDSV-GAFALSEV-VSGSDAFAMQTVAKKDGDHFILNGSKWGISNA--PIADFFLVLANADPEKG 207
Cdd:PLN02876 532 YGNKEQQLEWLIPLLEGKIrSGFAMTEPqVASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTDFNAP 611

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  208 -YRGVTCFIVDRDHEGV-------VLGEQDDNLGMragtiAQVHLNSVRVPKTSIVGEYGKGYKYAIEVLNASRIVIGAQ 279
Cdd:PLN02876 612 kHKQQSMILVDIQTPGVqikrpllVFGFDDAPHGH-----AEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMR 686

                        170       180
                 ....*....|....*....|....*.
gi 71982178  280 MVGLAQGCFDQTIPYLQERKQFGSRL 305
Cdd:PLN02876 687 LIGAAERGMQLMVQRALSRKAFGKLI 712
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 80-302 2.37e-07

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 52.13  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178   80 KLMGLKIDPKYGGSGVSFFELVLAVEELSKIDPAIALIMHLQNAL-VAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSE 157
Cdd:PRK09463 122 GFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLgPGELLLHYGTDEQKDHYLPRLARgEEIPCFALTS 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  158 VVSGSDAFAMQ---TVAKkdGDH-------FILNGSKWGISNAPIADfflVLANA----DPE-----KGYRGVTCFIVDR 218
Cdd:PRK09463 202 PEAGSDAGSIPdtgVVCK--GEWqgeevlgMRLTWNKRYITLAPIAT---VLGLAfklyDPDgllgdKEDLGITCALIPT 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  219 DHEGVVLGEQDDNLGmragtiaQVHLNS------VRVPKTSIVG--EY-GKGYKYAIEVLNASR-IVIGAQMVGLAQGCF 288
Cdd:PRK09463 277 DTPGVEIGRRHFPLN-------VPFQNGptrgkdVFIPLDYIIGgpKMaGQGWRMLMECLSVGRgISLPSNSTGGAKLAA 349

                        250
                 ....*....|....
gi 71982178  289 DQTIPYLQERKQFG 302
Cdd:PRK09463 350 LATGAYARIRRQFK 363
PLN02636 PLN02636
acyl-coenzyme A oxidase
 104-302 9.44e-07

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 50.24  E-value: 9.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  104 VEELSKIDPAIALIMHLQNALVAPLIEEFGNEELKEKYLKKLCK-DSVGAFALSEVVSGSDAFAMQTVAKKD--GDHFIL 180
Cdd:PLN02636 127 TEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNlDYPGCFAMTELHHGSNVQGLQTTATFDplTDEFVI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  181 N-----GSKWGISNAPI----ADFF--LVLANADpEKGYR--GVTCFIVD----RDHE---GVVLGEQDDNLGMRAGTIA 240
Cdd:PLN02636 207 NtpndgAIKWWIGNAAVhgkfATVFarLKLPTHD-SKGVSdmGVHAFIVPirdmKTHQvlpGVEIRDCGHKVGLNGVDNG 285

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71982178  241 QVHLNSVRVPKTSIVGEYGK-----GYKYAIEVLN-----------ASRIVIGAQMVGLAQGCFDQTIPYLQERKQFG 302
Cdd:PLN02636 286 ALRFRSVRIPRDNLLNRFGDvsrdgKYTSSLPTINkrfaatlgelvGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFG 363
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 97-304 1.77e-06

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: 49.25  E-value: 1.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  97 FFELVLAVEELSKIDP--AIALI-------------MHLQNALVAPLIEEFGNEELKEKYLKK-LCKDSVGAFALSEVVS 160
Cdd:cd01150  66 AKTDVERMGELMADDPekMLALTnslggydlslgakLGLHLGLFGNAIKNLGTDEHQDYWLQGaNNLEIIGCFAQTELGH 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 161 GSDAFAMQTVAKKD--GDHFILN-----GSKWGISN-APIADFFLVLANADPEKGYRGVTCFIVD-RDHE------GVVL 225
Cdd:cd01150 146 GSNLQGLETTATYDplTQEFVINtpdftATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAFIVPiRDPKthqplpGVTV 225

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178 226 GEQDDNLGMRAGTIAQVHLNSVRVPKTSIVGEYG----------------KGYKYAIEVLNASRI-VIGAQMVGLAQGCf 288
Cdd:cd01150 226 GDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGdvspdgtyvspfkdpnKRYGAMLGTRSGGRVgLIYDAAMSLKKAA- 304

                       250
                ....*....|....*...
gi 71982178 289 dqTIP--YLQERKQFGSR 304
Cdd:cd01150 305 --TIAirYSAVRRQFGPK 320
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 60-283 2.04e-06

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 49.11  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178   60 REMDRDARINKQLL-----KKAFDL-KLMGLKIDPKYGGSGVSFFELVLAVEEL--SKIDPAIALIMHlqNALVAPLIEE 131
Cdd:PTZ00457  38 RKLDGDEAENLQSLleqirSNDKILgNLYGARIATEYGGLGLGHTAHALIYEEVgtNCDSKLLSTIQH--SGFCTYLLST 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  132 FGNEELKEKYLKKLCKDSVGAFALSEVVSGSDaFAMQTV--AKKDGDHFILNGSKwGISNAPIADFFLVLANA----DPE 205
Cdd:PTZ00457 116 VGSKELKGKYLTAMSDGTIMMGWATEEGCGSD-ISMNTTkaSLTDDGSYVLTGQK-RCEFAASATHFLVLAKTltqtAAE 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982178  206 KGYRGV---TCFIVDRDHEGV-VLGEQddnlgmragtiaqvhLNSVRVPKTSIVGEYGKGYKYAIEVLNASRIVIGAQMV 281
Cdd:PTZ00457 194 EGATEVsrnSFFICAKDAKGVsVNGDS---------------VVFENTPAADVVGVVGEGFKDAMITLFTEQYLYAASLL 258


                 ..
gi 71982178  282 GL 283
Cdd:PTZ00457 259 GI 260
 
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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