Reviewed, UniProtKB/Swiss-Prot Q99L13 (3HIDH_MOUSE)

Names and origin

Protein names

Recommended name:
    3-hydroxyisobutyrate dehydrogenase, mitochondrial
      Short name=HIBADH
    EC=1.1.1.31

Gene names

Name:

Hibadh

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the 3-hydroxyisobutyrate dehydrogenase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pentose-phosphate shunt Inferred from electronic annotation. Source: InterPro valine metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	3-hydroxyisobutyrate dehydrogenase activity Inferred from electronic annotation. Source: EC NAD or NADH binding Inferred from electronic annotation. Source: InterPro phosphogluconate dehydrogenase (decarboxylating) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 35	35	Mitochondrion By similarity
	Chain	36 – 335	300	3-hydroxyisobutyrate dehydrogenase, mitochondrial		PRO_0000007159
Regions
	Nucleotide binding	39 – 68	30	NAD By similarity
	Nucleotide binding	102 – 103	2	NAD By similarity
Sites
	Active site	208	1	By similarity
	Binding site	107	1	NAD By similarity
	Binding site	133	1	NAD; via amide nitrogen By similarity
	Binding site	283	1	NAD By similarity
Experimental info
	Sequence conflict	2	1	A → S in BAC37162. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q99L13-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 5E9ECB03997DB110	FASTA	335	35,440
	10 20 30 40 50 60 MAASLGFRGA ASGLWYWSGR RRPVGSLAAV CSRSMASKTP VGFIGLGNMG NPMAKNLMKH 70 80 90 100 110 120 GYPLILYDVF PDVCKEFKEA GEQVASSPAE VAEKADRIIT MLPSSMNAVE VYSGANGILK 130 140 150 160 170 180 KVKKGSLLID SSTIDPSVSK ELAKEVEKMG AVFMDAPVSG GVGAARSGNL TFMVGGVEDE 190 200 210 220 230 240 FAAAQELLEC MGSNVVYCGA VGTGQSAKIC NNMLLAISMI GTAEAMNLGI RSGLDPKLLA 250 260 270 280 290 300 KILNMSSGRC WSSDTYNPVP GVMHGVPSSN NYQGGFGTTL MAKDLGLAQD SATSTKTPIL 310 320 330 LGSLAHQIYR MMCSKGYSKK DFSSVFQYLR EEEPF

References

[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: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC003914 mRNA. Translation: AAH03914.1. AK078175 mRNA. Translation: BAC37162.1.
IPI	IPI00116222.
RefSeq	NP_663542.1.
UniGene	Mm.286458
3D structure databases
SMR	Q99L13. Positions 40-333.
ModBase	Search...
2-D gel databases
REPRODUCTION-2DPAGE	Q99L13.
Proteomic databases
PRIDE	Q99L13.
Genome annotation databases
Ensembl	ENSMUSG00000029776. Mus musculus. [Contig view]
GeneID	58875.
KEGG	mmu:58875.
NMPDR	fig|10090.3.peg.14407.
Organism-specific databases
MGI	MGI:1889802. Hibadh.
Phylogenomic databases
HOGENOM	Q99L13.
HOVERGEN	Q99L13.
OMA	Q99L13. PMARNLI.
Enzyme and pathway databases
BRENDA	1.1.1.31. 244.
Gene expression databases
ArrayExpress	Q99L13.
Bgee	Q99L13.
CleanEx	MM_HIBADH.
GermOnline	ENSMUSG00000029776. Mus musculus.
Family and domain databases
InterPro	IPR002204. 3-OH-isobutyrate_DH-rel_CS. IPR015815. 3hydroxyacid_DH/Rdtase. IPR006183. 6-phosphogluconate_DH. IPR006115. 6PGDH_NAD-bd. IPR013328. DH_multihelical. IPR011548. IsoBut3OH_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PANTHER	PTHR22981. 3hydroxy_acid_DH. 1 hit.
Pfam	PF03446. NAD_binding_2. 1 hit. [Graphical view]
PRINTS	PR00076. 6PGDHDRGNASE.
TIGRFAMs	TIGR01692. HIBADH. 1 hit.
PROSITE	PS00895. 3_HYDROXYISOBUT_DH. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	314442.
SOURCE	Search...

Entry information

Entry name

3HIDH_MOUSE

Accession

Primary (citable) accession number: Q99L13
Secondary accession number(s): Q8BJY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2003
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)