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UniProtKB/Swiss-Prot entry Q80XN0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BDH_MOUSE
Primary accession number Q80XN0
Secondary accession numbers Q3UJS9 Q8BK53 Q8R0C8
Integrated into Swiss-Prot on July 19, 2005
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 55)
Name and origin of the protein
Protein name D-beta-hydroxybutyrate dehydrogenase, mitochondrial [Precursor]
Synonyms BDH
EC 1.1.1.30
3-hydroxybutyrate dehydrogenase
Gene name
Name: Bdh1
Synonyms: Bdh
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and DBA/2;
TISSUE=Testis;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Kidney, and Liver;
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 224-252, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[4]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132 AND LYS-275, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
Comments
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
AK076718; BAC36453.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK146321; BAE27076.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027063; AAH27063.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC043683; AAH43683.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC096457; AAH96457.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
UniGene Mm.293470
3D structure databases
HSSP P14061; 1FDW. [HSSP ENTRY / PDB]
ModBase Q80XN0.
Protein-protein interaction databases
IntAct Q80XN0; -.
PTM databases
PhosphoSite Q80XN0; -.
Organism-specific databases
MGI MGI:1919161; Bdh1.
Gene expression databases
ArrayExpress Q80XN0; -.
CleanEx MM_BDH1; -.
GermOnline ENSMUSG00000046598; Mus musculus.
Ontologies
GO
GO:0005743; Cellular component: mitochondrial inner membrane (inferred from direct assay from MGI).
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.
BLOCKS Q80XN0.
Genome annotation databases
Ensembl ENSMUSG00000046598; Mus musculus. [Contig view]
KEGG mmu:71911; -.
Phylogenomic databases
HOGENOM Q80XN0; -.
HOVERGEN Q80XN0; -.
Other
SOURCE Bdh1; Mus musculus.
ProtoNet Q80XN0.
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
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    46  46     Mitochondrion (By similarity). 
CHAIN   47   343  297     D-beta-hydroxybutyrate dehydrogenase, mitochondrial. PRO_0000031961
NP_BIND   60    84  25     NAD (By similarity). 
ACT_SITE   209   209        Proton acceptor (By similarity). 
BINDING   196   196        Substrate (By similarity). 
MOD_RES   132   132        N6-acetyllysine. 
MOD_RES   275   275        N6-acetyllysine. 
CONFLICT   152   152        E -> G (in Ref. 1; BAC36453). 
CONFLICT   215   215        V -> I (in Ref. 1; BAC36453). 
Sequence information
Length: 343 AA [This is the length of the unprocessed precursor] Molecular weight: 38285 Da [This is the MW of the unprocessed precursor] CRC64: BD1817C0713EC9EF [This is a checksum on the sequence]
        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 

Q80XN0 in FASTA format

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