ID   3HIDH_MOUSE             Reviewed;         335 AA.
AC   Q99L13; Q8BJY2;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 167.
DE   RecName: Full=3-hydroxyisobutyrate dehydrogenase, mitochondrial;
DE            Short=HIBADH;
DE            EC=1.1.1.31;
DE   Flags: Precursor;
GN   Name=Hibadh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-75; LYS-78; LYS-94;
RP   LYS-140; LYS-148; LYS-237; LYS-241; LYS-296 AND LYS-320, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-75; LYS-78; LYS-120;
RP   LYS-144; LYS-148; LYS-237; LYS-241 AND LYS-320, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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}.
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DR   EMBL; BC003914; AAH03914.1; -; mRNA.
DR   EMBL; AK078175; BAC37162.1; -; mRNA.
DR   CCDS; CCDS20151.1; -.
DR   RefSeq; NP_663542.1; NM_145567.1.
DR   AlphaFoldDB; Q99L13; -.
DR   SMR; Q99L13; -.
DR   BioGRID; 208456; 18.
DR   IntAct; Q99L13; 1.
DR   STRING; 10090.ENSMUSP00000031788; -.
DR   iPTMnet; Q99L13; -.
DR   PhosphoSitePlus; Q99L13; -.
DR   SwissPalm; Q99L13; -.
DR   REPRODUCTION-2DPAGE; Q99L13; -.
DR   EPD; Q99L13; -.
DR   jPOST; Q99L13; -.
DR   MaxQB; Q99L13; -.
DR   PaxDb; 10090-ENSMUSP00000031788; -.
DR   PeptideAtlas; Q99L13; -.
DR   ProteomicsDB; 286030; -.
DR   Pumba; Q99L13; -.
DR   Antibodypedia; 12430; 310 antibodies from 32 providers.
DR   DNASU; 58875; -.
DR   Ensembl; ENSMUST00000031788.9; ENSMUSP00000031788.9; ENSMUSG00000029776.12.
DR   GeneID; 58875; -.
DR   KEGG; mmu:58875; -.
DR   UCSC; uc009byw.1; mouse.
DR   AGR; MGI:1889802; -.
DR   CTD; 11112; -.
DR   MGI; MGI:1889802; Hibadh.
DR   VEuPathDB; HostDB:ENSMUSG00000029776; -.
DR   eggNOG; KOG0409; Eukaryota.
DR   GeneTree; ENSGT00940000155255; -.
DR   HOGENOM; CLU_035117_6_0_1; -.
DR   InParanoid; Q99L13; -.
DR   OMA; MGKKVWH; -.
DR   OrthoDB; 203032at2759; -.
DR   PhylomeDB; Q99L13; -.
DR   TreeFam; TF314043; -.
DR   Reactome; R-MMU-70895; Branched-chain amino acid catabolism.
DR   UniPathway; UPA00362; -.
DR   BioGRID-ORCS; 58875; 5 hits in 77 CRISPR screens.
DR   ChiTaRS; Hibadh; mouse.
DR   PRO; PR:Q99L13; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q99L13; Protein.
DR   Bgee; ENSMUSG00000029776; Expressed in right kidney and 256 other cell types or tissues.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
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:0006574; P: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; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR011548; HIBADH.
DR   InterPro; IPR029154; HIBADH-like_NADP-bd.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01692; HIBADH; 1.
DR   PANTHER; PTHR22981:SF7; 3-HYDROXYISOBUTYRATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22981; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000103; HIBADH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
DR   Genevisible; Q99L13; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Branched-chain amino acid catabolism; Mitochondrion; NAD;
KW   Oxidoreductase; 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_0000007159"
FT   ACT_SITE        208
FT                   /evidence="ECO:0000250"
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:0007744|PubMed:23576753"
FT   MOD_RES         59
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         75
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         75
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         78
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         78
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         94
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         120
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         140
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         144
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         148
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         148
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         237
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         237
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         241
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         241
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         296
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         320
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         320
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   CONFLICT        2
FT                   /note="A -> S (in Ref. 1; BAC37162)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   335 AA;  35440 MW;  5E9ECB03997DB110 CRC64;
     MAASLGFRGA ASGLWYWSGR RRPVGSLAAV CSRSMASKTP VGFIGLGNMG NPMAKNLMKH
     GYPLILYDVF PDVCKEFKEA GEQVASSPAE VAEKADRIIT MLPSSMNAVE VYSGANGILK
     KVKKGSLLID SSTIDPSVSK ELAKEVEKMG AVFMDAPVSG GVGAARSGNL TFMVGGVEDE
     FAAAQELLEC MGSNVVYCGA VGTGQSAKIC NNMLLAISMI GTAEAMNLGI RSGLDPKLLA
     KILNMSSGRC WSSDTYNPVP GVMHGVPSSN NYQGGFGTTL MAKDLGLAQD SATSTKTPIL
     LGSLAHQIYR MMCSKGYSKK DFSSVFQYLR EEEPF
//