Reviewed, UniProtKB/Swiss-Prot P29266 (3HIDH_RAT)

Names and origin

Protein names

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

Gene names

Name:

Hibadh

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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 protein level.

General annotation (Comments)

Catalytic activity	3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH.
Subunit structure	Homodimer.
Subcellular location	Mitochondrion.
Tissue specificity	Higher level in kidney, liver, and heart than in muscle.
Sequence similarities	Belongs to the 3-hydroxyisobutyrate dehydrogenase family.
Sequence caution	The sequence AAA50312.1 differs from that shown. Reason: Frameshift at position 10.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
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 electronic annotation. Source: UniProtKB-SubCell
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_0000007160
Regions
	Nucleotide binding	39 – 68	30	NAD By similarity
	Nucleotide binding	102 – 103	2	NAD By similarity
Sites
	Active site	208	1	Probable
	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
	Mutagenesis	68	1	D → R: Decrease of activity with NAD, increase of activity with NADP.
	Mutagenesis	208	1	K → A, H, N or R: Complete loss of activity.
	Mutagenesis	212	1	N → Q: Decrease in activity.

Sequences

	Sequence		Length	Mass (Da)
	P29266-1 [UniParc]. Last modified January 24, 2001. Version 3. Checksum: D266A7838500295A	FASTA	335	35,303
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate dehydrogenase. Evidence for its evolutionary relationship to other pyridine nucleotide-dependent dehydrogenases." Rougraff P.M., Zhang B., Kuntz M.J., Harris R.A., Crabb D.W. J. Biol. Chem. 264:5899-5903(1989) [PubMed: 2647728] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[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]. Tissue: Ovary.
[3]	Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 60-75; 297-310 AND 321-330, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.
[4]	"Structural and mechanistic similarities of 6-phosphogluconate and 3-hydroxyisobutyrate dehydrogenases reveal a new enzyme family, the 3-hydroxyacid dehydrogenases." Hawes J.W., Harper E.T., Crabb D.W., Harris R.A. FEBS Lett. 389:263-267(1996) [PubMed: 8766712] [Abstract] Cited for: MUTAGENESIS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J04628 mRNA. Translation: AAA50312.1. Frameshift. BC127442 mRNA. Translation: AAI27443.1.
IPI	IPI00202658.
PIR	A32867.
RefSeq	NP_071579.1.
UniGene	Rn.73
3D structure databases
SMR	P29266. Positions 40-334.
ModBase	Search...
Protein-protein interaction databases
STRING	P29266.
Proteomic databases
PRIDE	P29266.
Genome annotation databases
Ensembl	ENSRNOT00000011069; ENSRNOP00000011069; ENSRNOG00000008063; Rattus norvegicus. [Genome view]
GeneID	63938.
KEGG	rno:63938.
UCSC	NM_022243. rat.
Organism-specific databases
CTD	63938.
RGD	708399. Hibadh.
Phylogenomic databases
HOVERGEN	P29266.
OMA	GAEEEFT.
Enzyme and pathway databases
BRENDA	1.1.1.31. 248.
Gene expression databases
ArrayExpress	P29266.
Genevestigator	P29266.
GermOnline	ENSRNOG00000008063. Rattus norvegicus.
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	612544.

Entry information

Entry name

3HIDH_RAT

Accession

Primary (citable) accession number: P29266
Secondary accession number(s): A1L107

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	January 24, 2001
Last modified:	November 3, 2009
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)