3HIDH_MESAU
ID 3HIDH_MESAU Reviewed; 130 AA.
AC P86199;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=3-hydroxyisobutyrate dehydrogenase, mitochondrial {ECO:0000250|UniProtKB:P29266};
DE Short=HIBADH {ECO:0000250|UniProtKB:P29266};
DE EC=1.1.1.31;
DE Flags: Fragments;
GN Name=HIBADH {ECO:0000250|UniProtKB:P29266};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-
CC oxopropanoate + H(+) + NADH; 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 Evidence={ECO:0000250|UniProtKB:P29266};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P29266}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P29266}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC dehydrogenase subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P86199; -.
DR SMR; P86199; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0006574; P:valine catabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.1040.10; -; 2.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Acetylation; Branched-chain amino acid catabolism; Mitochondrion; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN <1..130
FT /note="3-hydroxyisobutyrate dehydrogenase, mitochondrial"
FT /id="PRO_0000394394"
FT BINDING 1..>17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
FT BINDING 25..26
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
FT BINDING 30
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 47
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 47
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 101
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT NON_CONS 17..18
FT /evidence="ECO:0000305"
FT NON_CONS 43..44
FT /evidence="ECO:0000305"
FT NON_CONS 65..66
FT /evidence="ECO:0000305"
FT NON_CONS 88..89
FT /evidence="ECO:0000305"
FT NON_CONS 115..116
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 130 AA; 13777 MW; B800F8CCA17A71EE CRC64;
TPVGFIGLGN MGNPMAKADR IITMLPSSMN SIEVYSGANG ILKEVEKMGA VFMDAPVSGG
VGAARICNNM LLAISMIGTA EAMNLGIRDL GLAQDSATST KTPILLGSVA HQIYRDFSSV
FQYLREEETF
