Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

3-hydroxyisobutyrate dehydrogenase, mitochondrial

Gene

Hibadh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei107 – 1071NADBy similarity
Binding sitei133 – 1331NAD; via amide nitrogenBy similarity
Active sitei208 – 2081By similarity
Binding sitei283 – 2831NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 6830NADBy similarityAdd
BLAST
Nucleotide bindingi102 – 1032NADBy similarity

GO - Molecular functioni

  1. 3-hydroxyisobutyrate dehydrogenase activity Source: UniProtKB
  2. NAD binding Source: InterPro
  3. phosphogluconate dehydrogenase (decarboxylating) activity Source: InterPro

GO - Biological processi

  1. pentose-phosphate shunt Source: InterPro
  2. valine catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Branched-chain amino acid catabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_305961. Branched-chain amino acid catabolism.
UniPathwayiUPA00362.

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxyisobutyrate dehydrogenase, mitochondrial (EC:1.1.1.31)
Short name:
HIBADH
Gene namesi
Name:Hibadh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1889802. Hibadh.

Subcellular locationi

  1. Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535MitochondrionBy similarityAdd
BLAST
Chaini36 – 3353003-hydroxyisobutyrate dehydrogenase, mitochondrialPRO_0000007159Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591N6-acetyllysine; alternate1 Publication
Modified residuei59 – 591N6-succinyllysine; alternate1 Publication
Modified residuei75 – 751N6-acetyllysine; alternate1 Publication
Modified residuei75 – 751N6-succinyllysine; alternate1 Publication
Modified residuei78 – 781N6-acetyllysine; alternate1 Publication
Modified residuei78 – 781N6-succinyllysine; alternate1 Publication
Modified residuei94 – 941N6-succinyllysine1 Publication
Modified residuei120 – 1201N6-acetyllysine1 Publication
Modified residuei140 – 1401N6-succinyllysine1 Publication
Modified residuei144 – 1441N6-acetyllysine1 Publication
Modified residuei148 – 1481N6-acetyllysine; alternate1 Publication
Modified residuei148 – 1481N6-succinyllysine; alternate1 Publication
Modified residuei237 – 2371N6-acetyllysine; alternate1 Publication
Modified residuei237 – 2371N6-succinyllysine; alternate1 Publication
Modified residuei241 – 2411N6-acetyllysine; alternate1 Publication
Modified residuei241 – 2411N6-succinyllysine; alternate1 Publication
Modified residuei296 – 2961N6-succinyllysine1 Publication
Modified residuei320 – 3201N6-acetyllysine; alternate1 Publication
Modified residuei320 – 3201N6-succinyllysine; alternate1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ99L13.
PaxDbiQ99L13.
PRIDEiQ99L13.

2D gel databases

REPRODUCTION-2DPAGEQ99L13.

PTM databases

PhosphoSiteiQ99L13.

Expressioni

Gene expression databases

BgeeiQ99L13.
CleanExiMM_HIBADH.
GenevestigatoriQ99L13.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ99L13. 2 interactions.
MINTiMINT-1841750.

Structurei

3D structure databases

ProteinModelPortaliQ99L13.
SMRiQ99L13. Positions 40-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2084.
GeneTreeiENSGT00530000063270.
HOGENOMiHOG000219610.
HOVERGENiHBG050424.
InParanoidiQ99L13.
KOiK00020.
OMAiHQPVILG.
OrthoDBiEOG7NSB31.
PhylomeDBiQ99L13.
TreeFamiTF314043.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR002204. 3-OH-isobutyrate_DH-rel_CS.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006115. 6PGDH_NADP-bd.
IPR011548. HIBADH.
IPR015815. HIBADH-related.
IPR016040. NAD(P)-bd_dom.
IPR029154. NADP-bd.
[Graphical view]
PfamiPF14833. NAD_binding_11. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000103. HIBADH. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR01692. HIBADH. 1 hit.
PROSITEiPS00895. 3_HYDROXYISOBUT_DH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99L13-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASLGFRGA ASGLWYWSGR RRPVGSLAAV CSRSMASKTP VGFIGLGNMG
60 70 80 90 100
NPMAKNLMKH GYPLILYDVF PDVCKEFKEA GEQVASSPAE VAEKADRIIT
110 120 130 140 150
MLPSSMNAVE VYSGANGILK KVKKGSLLID SSTIDPSVSK ELAKEVEKMG
160 170 180 190 200
AVFMDAPVSG GVGAARSGNL TFMVGGVEDE FAAAQELLEC MGSNVVYCGA
210 220 230 240 250
VGTGQSAKIC NNMLLAISMI GTAEAMNLGI RSGLDPKLLA KILNMSSGRC
260 270 280 290 300
WSSDTYNPVP GVMHGVPSSN NYQGGFGTTL MAKDLGLAQD SATSTKTPIL
310 320 330
LGSLAHQIYR MMCSKGYSKK DFSSVFQYLR EEEPF
Length:335
Mass (Da):35,440
Last modified:June 1, 2001 - v1
Checksum:i5E9ECB03997DB110
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → S in BAC37162 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC003914 mRNA. Translation: AAH03914.1.
AK078175 mRNA. Translation: BAC37162.1.
CCDSiCCDS20151.1.
RefSeqiNP_663542.1. NM_145567.1.
UniGeneiMm.286458.

Genome annotation databases

EnsembliENSMUST00000031788; ENSMUSP00000031788; ENSMUSG00000029776.
GeneIDi58875.
KEGGimmu:58875.
UCSCiuc009byw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC003914 mRNA. Translation: AAH03914.1.
AK078175 mRNA. Translation: BAC37162.1.
CCDSiCCDS20151.1.
RefSeqiNP_663542.1. NM_145567.1.
UniGeneiMm.286458.

3D structure databases

ProteinModelPortaliQ99L13.
SMRiQ99L13. Positions 40-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99L13. 2 interactions.
MINTiMINT-1841750.

PTM databases

PhosphoSiteiQ99L13.

2D gel databases

REPRODUCTION-2DPAGEQ99L13.

Proteomic databases

MaxQBiQ99L13.
PaxDbiQ99L13.
PRIDEiQ99L13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031788; ENSMUSP00000031788; ENSMUSG00000029776.
GeneIDi58875.
KEGGimmu:58875.
UCSCiuc009byw.1. mouse.

Organism-specific databases

CTDi11112.
MGIiMGI:1889802. Hibadh.

Phylogenomic databases

eggNOGiCOG2084.
GeneTreeiENSGT00530000063270.
HOGENOMiHOG000219610.
HOVERGENiHBG050424.
InParanoidiQ99L13.
KOiK00020.
OMAiHQPVILG.
OrthoDBiEOG7NSB31.
PhylomeDBiQ99L13.
TreeFamiTF314043.

Enzyme and pathway databases

UniPathwayiUPA00362.
ReactomeiREACT_305961. Branched-chain amino acid catabolism.

Miscellaneous databases

ChiTaRSiHibadh. mouse.
NextBioi314442.
PROiQ99L13.
SOURCEiSearch...

Gene expression databases

BgeeiQ99L13.
CleanExiMM_HIBADH.
GenevestigatoriQ99L13.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR002204. 3-OH-isobutyrate_DH-rel_CS.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006115. 6PGDH_NADP-bd.
IPR011548. HIBADH.
IPR015815. HIBADH-related.
IPR016040. NAD(P)-bd_dom.
IPR029154. NADP-bd.
[Graphical view]
PfamiPF14833. NAD_binding_11. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000103. HIBADH. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR01692. HIBADH. 1 hit.
PROSITEiPS00895. 3_HYDROXYISOBUT_DH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Olfactory bulb.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-75; LYS-78; LYS-94; LYS-140; LYS-148; LYS-237; LYS-241; LYS-296 AND LYS-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-75; LYS-78; LYS-120; LYS-144; LYS-148; LYS-237; LYS-241 AND LYS-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry namei3HIDH_MOUSE
AccessioniPrimary (citable) accession number: Q99L13
Secondary accession number(s): Q8BJY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 1, 2001
Last modified: April 29, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.