3HIDH_BOVIN
ID 3HIDH_BOVIN Reviewed; 336 AA.
AC Q2HJD7;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=3-hydroxyisobutyrate dehydrogenase, mitochondrial;
DE Short=HIBADH;
DE EC=1.1.1.31;
DE Flags: Precursor;
GN Name=HIBADH;
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=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC dehydrogenase subfamily. {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; BC105543; AAI05544.1; -; mRNA.
DR RefSeq; NP_001039571.1; NM_001046106.1.
DR AlphaFoldDB; Q2HJD7; -.
DR SMR; Q2HJD7; -.
DR STRING; 9913.ENSBTAP00000001374; -.
DR PaxDb; Q2HJD7; -.
DR PeptideAtlas; Q2HJD7; -.
DR PRIDE; Q2HJD7; -.
DR Ensembl; ENSBTAT00000001374; ENSBTAP00000001374; ENSBTAG00000001036.
DR GeneID; 512002; -.
DR KEGG; bta:512002; -.
DR CTD; 11112; -.
DR VEuPathDB; HostDB:ENSBTAG00000001036; -.
DR VGNC; VGNC:29844; HIBADH.
DR eggNOG; KOG0409; Eukaryota.
DR GeneTree; ENSGT00940000155255; -.
DR HOGENOM; CLU_035117_6_0_1; -.
DR InParanoid; Q2HJD7; -.
DR OMA; WSSEVNN; -.
DR OrthoDB; 812358at2759; -.
DR TreeFam; TF314043; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000001036; Expressed in liver and 103 other tissues.
DR ExpressionAtlas; Q2HJD7; baseline.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0006574; P:valine catabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR011548; HIBADH.
DR InterPro; IPR015815; HIBADH-related.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029154; NADP-bd.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000103; HIBADH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01692; HIBADH; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Branched-chain amino acid catabolism; Mitochondrion; NAD;
KW Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 37..336
FT /note="3-hydroxyisobutyrate dehydrogenase, mitochondrial"
FT /id="PRO_0000290342"
FT ACT_SITE 209
FT /evidence="ECO:0000250"
FT BINDING 40..69
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 103..104
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 60
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 60
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 76
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 76
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 95
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 121
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 141
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 145
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 149
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 149
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 238
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 238
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 242
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 242
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 297
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 321
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 321
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
SQ SEQUENCE 336 AA; 35410 MW; 11AB54F01BA8D5B8 CRC64;
MAASLRLRGA ASGLRYWSRR QPPAVASLAA VCSRSMASKT PVGFIGVGNM GNPMAKNLMK
HGYPLIIYDV FPDACKEFLD AGEQVVSSPA DVAEKADRII TMLPTSINAI EAYSGANGIL
KKVKKGSLLI DSSTIDPMVS KELAKEVEKM GAVFMDAPVS GGVGAARSGN LTFMVGGVEE
EFAAAQELLG CMGSNVVYCG AVGTGQAAKI CNNLLLAISM IGTAEAMNLG IRLGLDPKLL
AKILNMSSGR CWSSDTYNPV PGVMDGVPSA NNYQGGFGTT LMAKDLGLAQ DSATSTKSPI
LLGSQAHQIY RMMCAKGYSK KDFSSVFQFL REEETF
