ID   HIBCH_XENLA             Reviewed;         385 AA.
AC   A2VDC2;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=3-hydroxyisobutyryl-CoA hydrolase, mitochondrial;
DE            EC=3.1.2.4;
DE   AltName: Full=3-hydroxyisobutyryl-coenzyme A hydrolase;
DE            Short=HIB-CoA hydrolase;
DE            Short=HIBYL-CoA-H;
DE   Flags: Precursor;
GN   Name=hibch;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline
CC       catabolite. Has high activity toward isobutyryl-CoA. Could be an
CC       isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also
CC       hydrolyzes 3-hydroxypropanoyl-CoA (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-2-methylpropanoyl-CoA + H2O = 3-hydroxy-2-
CC         methylpropanoate + CoA + H(+); Xref=Rhea:RHEA:20888,
CC         ChEBI:CHEBI:11805, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57340; EC=3.1.2.4;
CC   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; BC129743; AAI29744.1; -; mRNA.
DR   RefSeq; NP_001091374.1; NM_001097905.1.
DR   AlphaFoldDB; A2VDC2; -.
DR   SMR; A2VDC2; -.
DR   GeneID; 100037216; -.
DR   KEGG; xla:100037216; -.
DR   CTD; 100037216; -.
DR   Xenbase; XB-GENE-947701; hibch.L.
DR   UniPathway; UPA00362; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 100037216; Expressed in heart and 19 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006574; P:valine catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR045004; ECH_dom.
DR   InterPro; IPR032259; HIBYL-CoA-H.
DR   PANTHER; PTHR43176; PTHR43176; 1.
DR   Pfam; PF16113; ECH_2; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
PE   2: Evidence at transcript level;
KW   Branched-chain amino acid catabolism; Hydrolase; Mitochondrion;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..385
FT                   /note="3-hydroxyisobutyryl-CoA hydrolase, mitochondrial"
FT                   /id="PRO_0000353183"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   385 AA;  42367 MW;  1BE261806F682E85 CRC64;
     MSFGRLESQL RLKVFGRLQV IRQHLRMSNH TVKDGGCLLT KAGCAGVITL NRPKALNALN
     LGMIRQIYPQ LKLWEEDPET YLVIIKGAGG KAFCAGGDIR AVTDAGKVGD RLAQDFFREE
     YILNNAIGTC KKPYVAVIDG ITMGGGVGLS VHGHFRVASE KTLFAMPETA IGLFPDVGGG
     YFLPRLTGKL GLYLALTGFR LKGSDVQKAG IATHFVESEK LSSLEQDLVA MKSPSKENVA
     DVLDSYQKKS YAAQDKPFVL AENMDKINSL FSGNTVEEIM ENLKCDGSSF AMKQLQTLST
     MSPTSLKITF RQLKEGASMS LQEVLTMEYR LSQACMNGHD FYEGVRAVLI DKDQKAKWKP
     ESLEEVTEDY IDSCFTSLGS RDLKL