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Protein

D-beta-hydroxybutyrate dehydrogenase, mitochondrial

Gene

BDH1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH.By similarity

Enzyme regulationi

Requires phosphatidylcholine as an allosteric activator for enzymatic activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei195 – 1951SubstrateBy similarity
Active sitei208 – 2081Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi59 – 8325NADBy similarityAdd
BLAST

GO - Molecular functioni

  • 3-hydroxybutyrate dehydrogenase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-BTA-77108. Utilization of Ketone Bodies.
R-BTA-77111. Synthesis of Ketone Bodies.
SABIO-RKQ02337.

Names & Taxonomyi

Protein namesi
Recommended name:
D-beta-hydroxybutyrate dehydrogenase, mitochondrialCurated (EC:1.1.1.30By similarity)
Alternative name(s):
3-hydroxybutyrate dehydrogenase1 Publication
Short name:
BDH1 Publication
Gene namesi
Name:BDH1By similarity
Synonyms:BDH1 Publication
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  • matrix side of mitochondrial inner membrane Source: UniProtKB
  • mitochondrial matrix Source: UniProtKB-SubCell
  • nucleoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646Mitochondrion1 PublicationAdd
BLAST
Chaini47 – 344298D-beta-hydroxybutyrate dehydrogenase, mitochondrialPRO_0000054526Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei73 – 731N6-acetyllysineBy similarity
Modified residuei97 – 971N6-acetyllysineBy similarity
Modified residuei103 – 1031N6-acetyllysine; alternateBy similarity
Modified residuei103 – 1031N6-succinyllysine; alternateBy similarity
Modified residuei177 – 1771N6-acetyllysineBy similarity
Modified residuei212 – 2121N6-acetyllysineBy similarity
Glycosylationi219 – 2191O-linked (GlcNAc)By similarity
Modified residuei246 – 2461PhosphoserineBy similarity
Modified residuei260 – 2601N6-acetyllysine; alternateBy similarity
Modified residuei260 – 2601N6-succinyllysine; alternateBy similarity
Modified residuei281 – 2811N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ02337.
PRIDEiQ02337.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000573.

Structurei

3D structure databases

ProteinModelPortaliQ02337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1610. Eukaryota.
ENOG410Y7FK. LUCA.
GeneTreeiENSGT00840000129713.
HOVERGENiHBG005482.
InParanoidiQ02337.
KOiK00019.
OMAiKGHDGVK.
OrthoDBiEOG7FXZZX.
TreeFamiTF325617.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q02337-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTARLSRPL SQLPRKTLNF SDRENGTRGS LLLYSAPFVP VGRRTYAASV
60 70 80 90 100
DPVGSKAVLI TGCDSGFGFS LAKHLHSEGF LVFAGCLMKD KGSDGVKELD
110 120 130 140 150
SMKSDRLRTV QLNVCKSEEV DKAAEVIRSS LEDPEKGLWG LVNNAGISTF
160 170 180 190 200
GDVEFTSMET YKEVAEVNLW GTVRVTKAFL PLIRRAKGRV VNISSMMGRM
210 220 230 240 250
ANVARSPYCI TKFGVEAFSD CLRYEMHPLG VKVSVVEPGN FIAATSLYGG
260 270 280 290 300
TERIQAIANK MWEELPEVVR QDYGRKYFDE KVARMESYCT SGSTDTSPVI
310 320 330 340
KAVTHALTAT TPYTRYHPMD YYWWLRMQIM THFPGAISDR IYIH
Length:344
Mass (Da):38,391
Last modified:July 25, 2006 - v2
Checksum:iC8C7AC75FA09880E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC103051 mRNA. Translation: AAI03052.1.
PIRiB42845.
RefSeqiNP_001029772.1. NM_001034600.2.
XP_005201562.1. XM_005201505.3.
UniGeneiBt.49607.

Genome annotation databases

EnsembliENSBTAT00000000573; ENSBTAP00000000573; ENSBTAG00000000448.
GeneIDi534090.
KEGGibta:534090.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC103051 mRNA. Translation: AAI03052.1.
PIRiB42845.
RefSeqiNP_001029772.1. NM_001034600.2.
XP_005201562.1. XM_005201505.3.
UniGeneiBt.49607.

3D structure databases

ProteinModelPortaliQ02337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000573.

Proteomic databases

PaxDbiQ02337.
PRIDEiQ02337.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000000573; ENSBTAP00000000573; ENSBTAG00000000448.
GeneIDi534090.
KEGGibta:534090.

Organism-specific databases

CTDi622.

Phylogenomic databases

eggNOGiKOG1610. Eukaryota.
ENOG410Y7FK. LUCA.
GeneTreeiENSGT00840000129713.
HOVERGENiHBG005482.
InParanoidiQ02337.
KOiK00019.
OMAiKGHDGVK.
OrthoDBiEOG7FXZZX.
TreeFamiTF325617.

Enzyme and pathway databases

ReactomeiR-BTA-77108. Utilization of Ketone Bodies.
R-BTA-77111. Synthesis of Ketone Bodies.
SABIO-RKQ02337.

Miscellaneous databases

NextBioi20876263.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Heart ventricle.
  2. "Molecular cloning and characterization of (R)-3-hydroxybutyrate dehydrogenase from human heart."
    Marks A.R., McIntyre J.O., Duncan T.M., Erdjument-Bromage H., Tempst P., Fleischer S.
    J. Biol. Chem. 267:15459-15463(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 47-89; 138-174; 213-231; 233-259; 285-322 AND 331-344.
    Tissue: Heart.
  3. "Amino acid sequences of two tryptic peptides from D(-)-beta-hydroxybutyrate dehydrogenase radiolabeled at essential carboxyl and sulfhydryl groups."
    Prasad P.V., Hatefi Y.
    Biochem. Int. 12:941-949(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 163-174 AND 285-301.
    Tissue: Heart.
  4. "The orientation of D-beta-hydroxybutyrate dehydrogenase in the mitochondrial inner membrane."
    McIntyre J.O., Bock H.G., Fleischer S.
    Biochim. Biophys. Acta 513:255-267(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Target size of D-beta-hydroxybutyrate dehydrogenase. Functional and structural molecular weight based on radiation inactivation."
    McIntyre J.O., Churchill P., Maurer A., Berenski C.J., Jung C.Y., Fleischer S.
    J. Biol. Chem. 258:953-959(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  6. "Coenzyme binding by 3-hydroxybutyrate dehydrogenase, a lipid-requiring enzyme: lecithin acts as an allosteric modulator to enhance the affinity for coenzyme."
    Rudy B., Dubois H., Mink R., Trommer W.E., McIntyre J.O., Fleischer S.
    Biochemistry 28:5354-5366(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.

Entry informationi

Entry nameiBDH_BOVIN
AccessioniPrimary (citable) accession number: Q02337
Secondary accession number(s): Q3ZBX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: July 25, 2006
Last modified: May 11, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.