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Reviewed, UniProtKB/Swiss-Prot Q80XN0 (BDH_MOUSE)

Last modified November 25, 2008. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    D-beta-hydroxybutyrate dehydrogenase, mitochondrial
      Short name=BDH
    EC=1.1.1.30
Alternative name(s):
    3-hydroxybutyrate dehydrogenase
Gene names
Name: Bdh1
Synonyms: Bdh
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

Enzyme regulation

Requires phosphatidylcholine as an allosteric activator for enzymatic activity By similarity.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrixBy similarity.

Post-translational modification

Acetylation of Lys-132 is observed in liver mitochondria from fasted mice but not from fed mice.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

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Ontologies

Keywords

   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termAllosteric enzyme
Direct protein sequencing

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial inner membrane

Inferred from direct assay. Source: MGI

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-hydroxybutyrate dehydrogenase activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4646Mitochondrion By similarity
Chain47 – 343297D-beta-hydroxybutyrate dehydrogenase, mitochondrial
PRO_0000031961

Regions

Nucleotide binding60 – 8425NAD By similarity

Sites

Active site2091Proton acceptor By similarity
Binding site1961Substrate By similarity

Amino acid modifications

Modified residue1321N6-acetyllysine
Modified residue2751N6-acetyllysine

Experimental info

Sequence conflict1521E → G in BAC36453. Ref.1
Sequence conflict2151V → I in BAC36453. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q80XN0-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: BD1817C0713EC9EF

FASTA34338,285
        10         20         30         40         50         60 
MLAARLSRPL SQLPGKALSV RDRENGTRHT LLFYPASFSP DTRRTYASQA DAASGKAILI 

        70         80         90        100        110        120 
TGCDSGFGFS LAKHLHSKGF LVFAGCLMKD KGDAGVKELD SLKSDRLRTI QLNVCNSEEV 

       130        140        150        160        170        180 
EKAVETIRSG LKDPEKGMWG LVNNAGISTF GEVEFTSMET YKEVAEVNLW GTVRTTKSFL 

       190        200        210        220        230        240 
PLLRRAKGRV VNISSMLGRM ANPARSPYCI TKFGVEAFSD CLRYEMHPLG VKVSVVEPGN 

       250        260        270        280        290        300 
FIAATSLYSP ERIQAIAKKM WDDLPEVVRK DYGRKYFDEK IAKMETYCNS GSTDTSSVIN 

       310        320        330        340 
AVTHALTAAT PYTRYHPMDY YWWLRMQIMT HFPGAISDKI YIH

« Hide

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References

« Hide 'large scale' 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. expand/collapse author list , 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 and DBA/2.
Tissue: Testis.
[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].
Strain: FVB/N.
Tissue: Kidney and Liver.
[3]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 224-252, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[4]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132 AND LYS-275, MASS SPECTROMETRY.
Tissue: Liver.

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Cross-references

Sequence databases

AK076718 mRNA. Translation: BAC36453.1.
AK146321 mRNA. Translation: BAE27076.1.
BC027063 mRNA. Translation: AAH27063.1.
BC043683 mRNA. Translation: AAH43683.1.
BC096457 mRNA. Translation: AAH96457.1.
UniGeneMm.293470

3D structure databases

HSSPHSSP built from PDB template 1FDW based on UniProtKB P14061.
ModBaseSearch...

PTM databases

PhosphoSiteQ80XN0.

Genome annotation databases

EnsemblENSMUSG00000046598. Mus musculus. [Contig view]

Organism-specific databases

MGIMGI:1919161. Bdh1.

Phylogenomic databases

HOGENOMQ80XN0.
HOVERGENQ80XN0.

Gene expression databases

ArrayExpressQ80XN0.
CleanExMM_BDH1.
GermOnlineENSMUSG00000046598. Mus musculus.

Family and domain databases

InterProIPR002198. DHase_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DHase.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

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Entry information

Entry nameBDH_MOUSE
AccessionPrimary (citable) accession number: Q80XN0
Secondary accession number(s): Q3UJS9, Q8BK53, Q8R0C8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: June 1, 2003
Last modified: November 25, 2008
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents