ID A0A0V0RIB8_9BILA Unreviewed; 879 AA.
AC A0A0V0RIB8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
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};
DE Flags: Fragment;
GN Name=ACADSB {ECO:0000313|EMBL:KRX14230.1};
GN ORFNames=T07_4556 {ECO:0000313|EMBL:KRX14230.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX14230.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX14230.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX14230.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
CC -!- SIMILARITY: Belongs to the lin-54 family.
CC {ECO:0000256|ARBA:ARBA00007267}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX14230.1}.
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DR EMBL; JYDL01000167; KRX14230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0RIB8; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016814; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 InterPro; IPR013158; APOBEC_N.
DR InterPro; IPR005172; CRC.
DR InterPro; IPR033467; Tesmin/TSO1-like_CXC.
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 Pfam; PF08210; APOBEC_N; 1.
DR SMART; SM01114; CXC; 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.
DR PROSITE; PS51634; CRC; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630}.
FT DOMAIN 426..514
FT /note="CRC"
FT /evidence="ECO:0000259|PROSITE:PS51634"
FT REGION 800..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX14230.1"
SQ SEQUENCE 879 AA; 99496 MW; B0FE50BCA9896407 CRC64;
LDCLLNKSFH NAQICLMMSK TTLKMAKLLK PLLSFSFPKP AIKIFKRNLA ALTDLYPEEM
ALKDSVAKFC KEVVQPHVTK MDREATMEQT IIEGLFKNGF MGIGIPGEYG GHDASFFMTL
LVIEELSKVG AFCLSEVQSG SDAFALKTFA KQDGTDFVIN GTKMWITNAE HANIFLVMAT
TDPSKVIYMG YKGISCFAVE RALAGVSVAK KEDKLGIRAS STCPVHFDNV RVPMSAVVGT
IGQGYKYAIE ILNEGRIGIA AQMIGIAQGC LDRTIPYLKE RKQFGRHIFD FQAMQHQVAD
MFTELEAARL LTYNAGRLLE TGQTVVKQAA MAKLYSSQMA SKVTSRCIEW MGGVGFIKDY
PVEKYYRDCK IDESCSCFLV QKFCDEQCES TRYRCDCLNQ VVVKCNCEIP ELSRVFPNLS
GGNNKQQPSC RICINPDRCD CARIKEACTK LCACKQLCKN NETKKILPIC KPTAGCLCCK
TKKQCMKRDC TCRAMYEFCS AKCKCQGDCS NGPSKFTISR QGQQCFLEQK HESSVILVTL
IGEDYVYRVE FCHESKSSRH CEEQLAIALH ELIVKYKINL YEILIYSSRS PCFHQDCEPR
CDVIDECSSN KACSKLLALL LTKVRKELKK ADIRMTVRFL FPHLHRGDLY TKQGILCMLQ
HGIKVEPLLM RDWSAIMDWA PQNEYKGDYL GLWNEHNLDQ AVAKSQSFVN ECRRALSMPM
KFWVAEIHEI VRNTILQFSE IRSKLQELAD SLKCLDLTAT PHKIRSTPNK RRSFIDILEL
RDKLHFKDYL HSSHAKVERE LHHQHQHQHK ARPVGSNISL SNEENSGANN AQLMVASLCG
RSYDDSETNE IAQRIRRATS NITVEIDSLL DYLNLKSNA
//
