ID   3HIDH_RABIT             Reviewed;          35 AA.
AC   P32185;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   10-JUN-2026, entry version 110.
DE   RecName: Full=3-hydroxyisobutyrate dehydrogenase;
DE            Short=HIBADH;
DE            EC=1.1.1.31;
DE   Flags: Fragment;
GN   Name=HIBADH;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=2647728; DOI=10.1016/s0021-9258(18)83634-1;
RA   Rougraff P.M., Zhang B., Kuntz M.J., Harris R.A., Crabb D.W.;
RT   "Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate
RT   dehydrogenase. Evidence for its evolutionary relationship to other pyridine
RT   nucleotide-dependent dehydrogenases.";
RL   J. Biol. Chem. 264:5899-5903(1989).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-
CC         oxopropanoate + NADH + H(+); Xref=Rhea:RHEA:17681, ChEBI:CHEBI:11805,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57700,
CC         ChEBI:CHEBI:57945; EC=1.1.1.31;
CC   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC       dehydrogenase subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P32185; -.
DR   SMR; P32185; -.
DR   STRING; 9986.ENSOCUP00000046575; -.
DR   PaxDb; 9986-ENSOCUP00000046575; -.
DR   eggNOG; KOG0409; Eukaryota.
DR   InParanoid; P32185; -.
DR   UniPathway; UPA00362; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006574; P:L-valine catabolic process; ISS:UniProtKB.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR22981:SF7; 3-HYDROXYISOBUTYRATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22981; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Branched-chain amino acid catabolism;
KW   Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..>35
FT                   /note="3-hydroxyisobutyrate dehydrogenase"
FT                   /id="PRO_0000173054"
FT   BINDING         4..33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         24
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   MOD_RES         24
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L13"
FT   NON_TER         35
SQ   SEQUENCE   35 AA;  3796 MW;  C15D62589F84ED64 CRC64;
     ASKTPVGFIG LGNMGNPMAK NLMKHGYPLI IYDVF
//