3HIDH_RAT
ID 3HIDH_RAT Reviewed; 335 AA.
AC P29266; A1L107;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=3-hydroxyisobutyrate dehydrogenase, mitochondrial;
DE Short=HIBADH;
DE EC=1.1.1.31;
DE Flags: Precursor;
GN Name=Hibadh;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 60-75; 297-310 AND 321-330, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [4]
RP MUTAGENESIS.
RX PubMed=8766712; DOI=10.1016/0014-5793(96)00597-2;
RA Hawes J.W., Harper E.T., Crabb D.W., Harris R.A.;
RT "Structural and mechanistic similarities of 6-phosphogluconate and 3-
RT hydroxyisobutyrate dehydrogenases reveal a new enzyme family, the 3-
RT hydroxyacid dehydrogenases.";
RL FEBS Lett. 389:263-267(1996).
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.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- TISSUE SPECIFICITY: Higher level in kidney, liver, and heart than in
CC muscle.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC dehydrogenase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA50312.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; J04628; AAA50312.1; ALT_FRAME; mRNA.
DR EMBL; BC127442; AAI27443.1; -; mRNA.
DR PIR; A32867; A32867.
DR RefSeq; NP_071579.1; NM_022243.1.
DR AlphaFoldDB; P29266; -.
DR SMR; P29266; -.
DR IntAct; P29266; 1.
DR STRING; 10116.ENSRNOP00000011069; -.
DR iPTMnet; P29266; -.
DR PhosphoSitePlus; P29266; -.
DR PaxDb; P29266; -.
DR PRIDE; P29266; -.
DR GeneID; 63938; -.
DR KEGG; rno:63938; -.
DR UCSC; RGD:708399; rat.
DR CTD; 11112; -.
DR RGD; 708399; Hibadh.
DR VEuPathDB; HostDB:ENSRNOG00000008063; -.
DR eggNOG; KOG0409; Eukaryota.
DR HOGENOM; CLU_035117_6_0_1; -.
DR InParanoid; P29266; -.
DR OMA; WSSEVNN; -.
DR OrthoDB; 812358at2759; -.
DR PhylomeDB; P29266; -.
DR TreeFam; TF314043; -.
DR Reactome; R-RNO-70895; Branched-chain amino acid catabolism.
DR SABIO-RK; P29266; -.
DR UniPathway; UPA00362; -.
DR PRO; PR:P29266; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000008063; Expressed in kidney and 20 other tissues.
DR Genevisible; P29266; RN.
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; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
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.
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; Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 36..335
FT /note="3-hydroxyisobutyrate dehydrogenase, mitochondrial"
FT /id="PRO_0000007160"
FT ACT_SITE 208
FT /evidence="ECO:0000305"
FT BINDING 39..68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 102..103
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 59
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 59
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 75
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 75
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 94
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 120
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 140
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 148
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 148
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 237
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 237
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 241
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 241
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 296
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 320
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MOD_RES 320
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99L13"
FT MUTAGEN 68
FT /note="D->R: Decrease of activity with NAD, increase of
FT activity with NADP."
FT /evidence="ECO:0000269|PubMed:8766712"
FT MUTAGEN 208
FT /note="K->A,H,N,R: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:8766712"
FT MUTAGEN 212
FT /note="N->Q: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:8766712"
SQ SEQUENCE 335 AA; 35303 MW; D266A7838500295A CRC64;
MAASLGFRGA ASGLRYWSGR RRPVGSLAAV CSRSMASKTP VGFIGLGNMG NPMAKNLIKH
GYPLILYDVF PDVCKEFKEA GEQVASSPAD VAEKADRIIT MLPSSMNSIE VYSGANGILK
KVKKGSLLID SSTIDPSVSK ELAKEVEKMG AVFMDAPVSG GVGAARSGNL TFMVGGVENE
FAAAQELLGC MGSNVLYCGA VGSGQSAKIC NNMLLAISMI GTAEAMNLGI RSGLDPKLLA
KILNMSSGRC WSSDTYNPVP GVMDGVPSSN NYQGGFGTTL MAKDLGLAQD SATSTKTPIL
LGSVAHQIYR MMCSKGYSKK DFSSVFQYLR EEETF
