[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Liver; PubMed=2647728 [NCBI, ExPASy, EBI, Israel, Japan] Rougraff P.M., Zhang B., Kuntz M.J., Harris R.A., Crabb D.W.; "Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate dehydrogenase. Evidence for its evolutionary relationship to other pyridine nucleotide-dependent dehydrogenases."; J. Biol. Chem. 264:5899-5903(1989).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Ovary; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	PROTEIN SEQUENCE OF 60-75; 297-310 AND 321-330, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Spinal cord; Lubec G., Afjehi-Sadat L.; Submitted (NOV-2006) to UniProtKB.
[4]	MUTAGENESIS. DOI=10.1016/0014-5793(96)00597-2; PubMed=8766712 [NCBI, ExPASy, EBI, Israel, Japan] Hawes J.W., Harper E.T., Crabb D.W., Harris R.A.; "Structural and mechanistic similarities of 6-phosphogluconate and 3-hydroxyisobutyrate dehydrogenases reveal a new enzyme family, the 3-hydroxyacid dehydrogenases."; FEBS Lett. 389:263-267(1996).

Comments

CATALYTIC ACTIVITY: 3-hydroxy-2-methylpropanoate + NAD⁺ = 2-methyl-3-oxopropanoate + NADH.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Mitochondrion.
TISSUE SPECIFICITY: Higher level in kidney, liver, and heart than in muscle.
SIMILARITY: Belongs to the 3-hydroxyisobutyrate dehydrogenase family.
SEQUENCE CAUTION:
- Sequence=AAA50312.1; Type=Frameshift; Positions=10;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J04628; AAA50312.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC127442; AAI27443.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A32867; A32867.

NP_071579.1; -.

3D structure databases

SMR

P29266; 40-334.

ModBase

P29266.

Organism-specific databases

RGD

708399; Hibadh.

Gene expression databases

ArrayExpress

P29266; -.

GermOnline

ENSRNOG00000008063; Rattus norvegicus.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0008442;	Molecular function: 3-hydroxyisobutyrate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0004616;	Molecular function: phosphogluconate dehydrogenase (decarboxylating) activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006098;	Biological process: pentose-phosphate shunt (inferred from electronic annotation from InterPro).
GO:0006573;	Biological process: valine metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002204; 3-OH-isobutyrate_DHase-rel_CS.
IPR015815; 3hydroxyacid_DHase/Rdtase.
IPR006183; 6-phosphogluconate_DHase.
IPR006115; 6PGDH_NAD-bd.
IPR013328; DHase_multihelical.
IPR011548; IsoBut3OH_DH.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.

PANTHER

PTHR22981; 3hydroxy_acid_DH; 1.

Pfam

PF03446; NAD_binding_2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00076; 6PGDHDRGNASE.

TIGRFAMs

TIGR01692; HIBADH; 1.

PROSITE

PS00895; 3_HYDROXYISOBUT_DH; 1.

ProtoNet

P29266.

Genome annotation databases

Ensembl

ENSRNOG00000008063; Rattus norvegicus. [Contig view]

GeneID

63938; -.

KEGG

rno:63938; -.

Phylogenomic databases

HOVERGEN

P29266; -.

Other

NextBio

612544; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 35`	`35`	`Mitochondrion (By similarity).`
`CHAIN`	`36 335`	`300`	`3-hydroxyisobutyrate dehydrogenase, mitochondrial.`	`PRO_0000007160`
`NP_BIND`	`39 68`	`30`	`NAD (By similarity).`
`NP_BIND`	`102 103`	`2`	`NAD (By similarity).`
`ACT_SITE`	`208 208`		`Probable.`
`BINDING`	`107 107`		`NAD (By similarity).`
`BINDING`	`133 133`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`283 283`		`NAD (By similarity).`
`MUTAGEN`	`68 68`		`D->R: Decrease of activity with NAD, increase of activity with NADP.`
`MUTAGEN`	`208 208`		`K->A,H,N,R: Complete loss of activity.`
`MUTAGEN`	`212 212`		`N->Q: Decrease in activity.`

Sequence information

Length: 335 AA [This is the length of the unprocessed precursor]

Molecular weight: 35303 Da [This is the MW of the unprocessed precursor]

CRC64: D266A7838500295A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAASLGFRGA ASGLRYWSGR RRPVGSLAAV CSRSMASKTP VGFIGLGNMG NPMAKNLIKH 

        70         80         90        100        110        120 
GYPLILYDVF PDVCKEFKEA GEQVASSPAD VAEKADRIIT MLPSSMNSIE VYSGANGILK 

       130        140        150        160        170        180 
KVKKGSLLID SSTIDPSVSK ELAKEVEKMG AVFMDAPVSG GVGAARSGNL TFMVGGVENE 

       190        200        210        220        230        240 
FAAAQELLGC MGSNVLYCGA VGSGQSAKIC NNMLLAISMI GTAEAMNLGI RSGLDPKLLA 

       250        260        270        280        290        300 
KILNMSSGRC WSSDTYNPVP GVMDGVPSSN NYQGGFGTTL MAKDLGLAQD SATSTKTPIL 

       310        320        330 
LGSVAHQIYR MMCSKGYSKK DFSSVFQYLR EEETF

P29266 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools