IVD_BOVIN
ID IVD_BOVIN Reviewed; 426 AA.
AC Q3SZI8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Isovaleryl-CoA dehydrogenase, mitochondrial;
DE Short=IVD;
DE EC=1.3.8.4 {ECO:0000250|UniProtKB:P26440};
DE AltName: Full=Butyryl-CoA dehydrogenase;
DE EC=1.3.8.1 {ECO:0000250|UniProtKB:P26440};
DE Flags: Precursor;
GN Name=IVD;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of isovaleryl-CoA/3-methylbutanoyl-
CC CoA to 3-methylbut-2-enoyl-CoA as an intermediate step in the leucine
CC (Leu) catabolic pathway. To a lesser extent, is also able to catalyze
CC the oxidation of other saturated short-chain acyl-CoA thioesters as
CC pentanoyl-CoA, hexenoyl-CoA and butenoyl-CoA.
CC {ECO:0000250|UniProtKB:P26440}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = 3-methyl-(2E)-butenoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:12276, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57344,
CC ChEBI:CHEBI:57345, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.4;
CC Evidence={ECO:0000250|UniProtKB:P26440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] + pentanoyl-
CC CoA = (2E)-pentenoyl-CoA + reduced [electron-transfer flavoprotein];
CC Xref=Rhea:RHEA:43456, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57389, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:86160;
CC Evidence={ECO:0000250|UniProtKB:P26440};
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:0000250|UniProtKB:P26440};
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; EC=1.3.8.1;
CC Evidence={ECO:0000250|UniProtKB:P26440};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P26440};
CC -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-
CC 3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 1/3.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P26440}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P12007}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; BC102836; AAI02837.1; -; mRNA.
DR RefSeq; NP_001029554.1; NM_001034382.2.
DR AlphaFoldDB; Q3SZI8; -.
DR SMR; Q3SZI8; -.
DR IntAct; Q3SZI8; 1.
DR STRING; 9913.ENSBTAP00000005782; -.
DR PaxDb; Q3SZI8; -.
DR PeptideAtlas; Q3SZI8; -.
DR PRIDE; Q3SZI8; -.
DR GeneID; 510440; -.
DR KEGG; bta:510440; -.
DR CTD; 3712; -.
DR eggNOG; KOG0141; Eukaryota.
DR HOGENOM; CLU_018204_0_1_1; -.
DR InParanoid; Q3SZI8; -.
DR OrthoDB; 589058at2759; -.
DR TreeFam; TF105050; -.
DR UniPathway; UPA00363; UER00860.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0008470; F:isovaleryl-CoA dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; ISS:UniProtKB.
DR GO; GO:0006552; P:leucine catabolic process; ISS:UniProtKB.
DR CDD; cd01156; IVD; 1.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 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.
DR InterPro; IPR034183; IVD.
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 SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; FAD; Flavoprotein; Mitochondrion; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT CHAIN 33..426
FT /note="Isovaleryl-CoA dehydrogenase, mitochondrial"
FT /id="PRO_0000281993"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 165..174
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 198..200
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 222..223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 284..287
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 312
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 380..384
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 407..408
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 409..411
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT MOD_RES 58
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9JHI5"
FT MOD_RES 58
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9JHI5"
FT MOD_RES 78
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT MOD_RES 78
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9JHI5"
FT MOD_RES 241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHI5"
FT MOD_RES 318
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHI5"
SQ SEQUENCE 426 AA; 46498 MW; 77C268E25568ACCA CRC64;
MATAAWLLGR RVASWRMRPP LQSLAGLITQ RTNSLLPVDD AVNGLNEEQK QLRQTVAKFL
QEHLAPQAQE IDQSNEFKNL REFWKQLGNL GVLGITAPVQ YGGSGLGFLE NVLVMEEISR
VSGAVGLSYG AHSNLCINQI VRNGNETQKE KYLPKLISGE YIGALAMSEP NAGSDVVSMK
LKAEKKGDHY VLNGNKFWIT NGPDADVLVV YAKTDVTAVP ASRGITAFIV EKGMPGFSTS
KKLDKLGMRG SNTCELVFED CEVPAANILG HLGKGVYVLM SGLDLERLVL AGGPLGIMQA
VLDHTIPYLH MREAFGQKIG HFQLMQGKMA DMYTRLMACR QYVYNVAKAC DEGHCTTKDC
AGVILYSAEC ATQVALDGIQ CLGGNGYIND FPMGRFLRDA KLYEIGAGTS EVRRLVIGRA
FNADFH
