[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Heart ventricle; NIH - Mammalian Gene Collection (MGC) project; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[2]	PROTEIN SEQUENCE OF 47-89; 138-174; 213-231; 233-259; 285-322 AND 331-344. TISSUE=Heart; PubMed=1639787 [NCBI, ExPASy, EBI, Israel, Japan] Marks A.R., McIntyre J.O., Duncan T.M., Erdjument-Bromage H., Tempst P., Fleischer S.; "Molecular cloning and characterization of (R)-3-hydroxybutyrate dehydrogenase from human heart."; J. Biol. Chem. 267:15459-15463(1992).
[3]	PROTEIN SEQUENCE OF 163-174 AND 285-301. TISSUE=Heart; PubMed=3527172 [NCBI, ExPASy, EBI, Israel, Japan] Prasad P.V., Hatefi Y.; "Amino acid sequences of two tryptic peptides from D(-)-beta-hydroxybutyrate dehydrogenase radiolabeled at essential carboxyl and sulfhydryl groups."; Biochem. Int. 12:941-949(1986).

Comments

CATALYTIC ACTIVITY: (R)-3-hydroxybutanoate + NAD⁺ = acetoacetate + NADH.
ENZYME REGULATION: Requires phosphatidylcholine as an allosteric activator for enzymic activity.
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Mitochondrion matrix.
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.

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

BC103051; AAI03052.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

B42845; B42845.

NP_001029772.1; -.

3D structure databases

ModBase

Q02337.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003858;	Molecular function: 3-hydroxybutyrate dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

PROSITE

PS00061; ADH_SHORT; 1.

Genome annotation databases

Ensembl

ENSBTAG00000000448; Bos taurus. [Contig view]

GeneID

534090; -.

KEGG

bta:534090; -.

Phylogenomic databases

HOVERGEN

Q02337; -.

Other

UniRef

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

Keywords

Acetylation; Allosteric enzyme; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 46`	`46`	`Mitochondrion.`
`CHAIN`	`47 344`	`298`	`D-beta-hydroxybutyrate dehydrogenase, mitochondrial.`	`PRO_0000054526`
`NP_BIND`	`59 83`	`25`	`NAD (By similarity).`
`ACT_SITE`	`208 208`		`Proton acceptor (By similarity).`
`BINDING`	`195 195`		`Substrate (By similarity).`
`MOD_RES`	`276 276`		`N6-acetyllysine (By similarity).`

Sequence information

Length: 344 AA [This is the length of the unprocessed precursor]

Molecular weight: 38391 Da [This is the MW of the unprocessed precursor]

CRC64: C8C7AC75FA09880E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLTARLSRPL SQLPRKTLNF SDRENGTRGS LLLYSAPFVP VGRRTYAASV DPVGSKAVLI 

        70         80         90        100        110        120 
TGCDSGFGFS LAKHLHSEGF LVFAGCLMKD KGSDGVKELD SMKSDRLRTV QLNVCKSEEV 

       130        140        150        160        170        180 
DKAAEVIRSS LEDPEKGLWG LVNNAGISTF GDVEFTSMET YKEVAEVNLW GTVRVTKAFL 

       190        200        210        220        230        240 
PLIRRAKGRV VNISSMMGRM ANVARSPYCI TKFGVEAFSD CLRYEMHPLG VKVSVVEPGN 

       250        260        270        280        290        300 
FIAATSLYGG TERIQAIANK MWEELPEVVR QDYGRKYFDE KVARMESYCT SGSTDTSPVI 

       310        320        330        340 
KAVTHALTAT TPYTRYHPMD YYWWLRMQIM THFPGAISDR IYIH

Q02337 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