ID   HIBCH_CHICK             Reviewed;         385 AA.
AC   Q5ZJ60;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
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; ORFNames=RCJMB04_20j11;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ720574; CAG32233.1; -; mRNA.
DR   RefSeq; NP_001026414.1; NM_001031243.1.
DR   AlphaFoldDB; Q5ZJ60; -.
DR   SMR; Q5ZJ60; -.
DR   STRING; 9031.ENSGALP00000003623; -.
DR   PaxDb; Q5ZJ60; -.
DR   GeneID; 423979; -.
DR   KEGG; gga:423979; -.
DR   CTD; 26275; -.
DR   VEuPathDB; HostDB:geneid_423979; -.
DR   eggNOG; KOG1684; Eukaryota.
DR   InParanoid; Q5ZJ60; -.
DR   OrthoDB; 1369862at2759; -.
DR   PhylomeDB; Q5ZJ60; -.
DR   UniPathway; UPA00362; -.
DR   PRO; PR:Q5ZJ60; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IBA:GO_Central.
DR   GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
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_0000284932"
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;  42829 MW;  C9737F7C2F3DE7DA CRC64;
     MAARVLMAPR RLKPFNRLQV ILQHLKTCKH TDSAADVLLQ KQGGAGIITL NRPKVLNALS
     FKMIQQIYPQ IKAWEQDPET FLIIIKGTGE KAFCAGGDVR AIADAGKAGD TMTRDYFREE
     YRLDNAIGTC KKPYVALIDG ITMGGGVGLS VHGHFRVATE KTVFAMPETA IGLFPDVGGG
     YFLPRLSGKI GHLLALTGFR LKGRDVLKAG IATHFVESGK LPELEKDLIA LKSPSKENIA
     DLLNSYHMQT KIDQEKEFVL DEHMERINSI FSANSMEEIV QKLKQDGSPF ATKQLEAINK
     MSPTSLKLTL RQLREGATMS LQDVFTMEYR LSQACMRGHD FYEGVRAVLI DKDQSPRWKP
     AALEEVSDEF VDNCFKPLGN NDLKL