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Database: UniProt
Entry: A0A085NR07_9BILA
LinkDB: A0A085NR07_9BILA
Original site: A0A085NR07_9BILA 
ID   A0A085NR07_9BILA        Unreviewed;       412 AA.
AC   A0A085NR07;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00039850};
DE            EC=1.3.8.5 {ECO:0000256|ARBA:ARBA00039036};
DE   AltName: Full=2-methyl branched chain acyl-CoA dehydrogenase {ECO:0000256|ARBA:ARBA00042821};
DE   AltName: Full=2-methylbutyryl-coenzyme A dehydrogenase {ECO:0000256|ARBA:ARBA00041537};
GN   ORFNames=M514_08156 {ECO:0000313|EMBL:KFD71903.1};
OS   Trichuris suis (pig whipworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD71903.1};
RN   [1] {ECO:0000313|EMBL:KFD71903.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD71903.1};
RX   PubMed=24929829; DOI=10.1038/ng.3012;
RA   Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA   Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA   Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT   "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL   Nat. Genet. 46:701-706(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = ethylacryloyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:65296, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:156439, ChEBI:CHEBI:156440;
CC         Evidence={ECO:0000256|ARBA:ARBA00036907};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65297;
CC         Evidence={ECO:0000256|ARBA:ARBA00036907};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-
CC         transfer flavoprotein]; Xref=Rhea:RHEA:48256, Rhea:RHEA-COMP:10685,
CC         Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57337,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:88166;
CC         Evidence={ECO:0000256|ARBA:ARBA00036507};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48257;
CC         Evidence={ECO:0000256|ARBA:ARBA00036507};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-
CC         transfer flavoprotein]; Xref=Rhea:RHEA:43780, Rhea:RHEA-COMP:10685,
CC         Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57336,
CC         ChEBI:CHEBI:57337, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00036426};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43781;
CC         Evidence={ECO:0000256|ARBA:ARBA00036426};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methylpropanoyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E)-2-methylpropenoyl-CoA + reduced [electron-
CC         transfer flavoprotein]; Xref=Rhea:RHEA:44180, Rhea:RHEA-COMP:10685,
CC         Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57338,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:62500;
CC         Evidence={ECO:0000256|ARBA:ARBA00036504};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44181;
CC         Evidence={ECO:0000256|ARBA:ARBA00036504};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer
CC         flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC         Evidence={ECO:0000256|ARBA:ARBA00001483};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465;
CC         Evidence={ECO:0000256|ARBA:ARBA00001483};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxidized [electron-transfer flavoprotein] + valproyl-
CC         CoA = (2E)-2-propylpent-2-enoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:65344, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:156457, ChEBI:CHEBI:156458;
CC         Evidence={ECO:0000256|ARBA:ARBA00035997};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65345;
CC         Evidence={ECO:0000256|ARBA:ARBA00035997};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=butanoyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:24004, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332, ChEBI:CHEBI:57371,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307;
CC         Evidence={ECO:0000256|ARBA:ARBA00036579};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24005;
CC         Evidence={ECO:0000256|ARBA:ARBA00036579};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- PATHWAY: Amino-acid degradation; L-isoleucine degradation.
CC       {ECO:0000256|ARBA:ARBA00037895}.
CC   -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005198}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; KL367480; KFD71903.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A085NR07; -.
DR   Proteomes; UP000030758; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01158; SCAD_SBCAD; 1.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF1; SHORT/BRANCHED CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   PIRSF; PIRSF016578; HsaA; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN          39..147
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          152..247
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          259..405
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   412 AA;  45454 MW;  2BD184CEB725B8D8 CRC64;
     MWKGLRLPQL CFASARSAAL KNEMTKSLHT PALTDLSTDE EIMKSSSAKF AKEMVGPLVS
     RMDEESCLDS TVLRGLFLNG FMGIEIPSEY GGSEAPFFSV VQVVEELAKV DASVAIVCDV
     QNTLINSMLL AYGEEEQKKR YLPALCKNLI GAFCLSESTS GSDAFALKTT AERSGSDYIL
     KGEKLWITNA EHAGVFLVFA NVDPSKGYKG ITCFIVDRQL PGVSVARKED KLGIRASSTC
     PVYFEEVRIP ANCVLGEVGQ GYRYAMEALN EGRIGIAAQM IGISQGCIDR TIPYLKERKQ
     FGRRIFDFQG MRHQLAEVCT KLEAARLLTY NAARLKETGL PFMKEAAMAK LYSSQIAGEA
     TSKCVEWLGG NGFIKEYAVE KYYRDCKIGA IYEGTSNIQM NTIAKLIEKE YD
//
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