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UniProtKB/Swiss-Prot entry P35738


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

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Entry information
Entry name ODBB_RAT
Primary accession number P35738
Secondary accession numbers None
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on December 4, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 63)
Name and origin of the protein
Protein name 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial [Precursor]
Synonyms EC 1.2.4.4
Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
BCKDH E1-beta
Gene name
Name: Bckdhb
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
DOI=10.1038/nature02426; PubMed=15057822 [NCBI, ExPASy, EBI, Israel, Japan]
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into mammalian evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-230.
The MGC Project Team;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 29-390, AND PROTEIN SEQUENCE OF 49-75.
DOI=10.1016/0167-4781(92)90014-Q; PubMed=1390893 [NCBI, ExPASy, EBI, Israel, Japan]
Zhao Y., Kuntz M.J., Harris R.A., Crabb D.W.;
"Molecular cloning of the E1 beta subunit of the rat branched chain alpha-ketoacid dehydrogenase.";
Biochim. Biophys. Acta 1132:207-210(1992).
[4]
ERRATUM.
PubMed=7841205 [NCBI, ExPASy, EBI, Israel, Japan]
Zhao Y., Kuntz M.J., Harris R.A., Crabb D.W.;
Biochim. Biophys. Acta 1260:243-243(1995).
Comments
  • FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
  • CATALYTIC ACTIVITY: 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2.
  • SUBUNIT: Heterodimer of an alpha and a beta chain.
  • SUBCELLULAR LOCATION: Mitochondrion matrix.
  • SEQUENCE CAUTION:
    • Sequence=AAA73899.1; Type=Frameshift; Positions=101, 120;
    • Sequence=AAA73899.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part
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
AABR03062593; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AABR03062720; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AABR03063125; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AABR03063398; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
M94040; AAA73899.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S28950; S28950.
RefSeq NP_062140.1; -.
UniGene Rn.15623
3D structure databases
HSSP P21953; 1DTW. [HSSP ENTRY / PDB]
SMR P35738; 40-369.
ModBase P35738.
Organism-specific databases
RGD 2197; Bckdhb.
Ontologies
GO
GO:0005947; Cellular component: mitochondrial alpha-ketoglutarate dehydrogenase complex (inferred from sequence or structural similarity from HGNC).
GO:0009083; Biological process: branched chain family amino acid catabolic process (inferred from sequence or structural similarity from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR005476; Transketo_C.
IPR005475; Transketo_Cen_R.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.920; Transketo_C_like; 2.
Pfam PF02779; Transket_pyr; 2.
PF02780; Transketolase_C; 2.
Pfam graphical view of domain structure.
BLOCKS P35738.
Genome annotation databases
Ensembl ENSRNOG00000009928; Rattus norvegicus. [Contig view]
GeneID 29711; -.
KEGG rno:29711; -.
Phylogenomic databases
HOVERGEN P35738; -.
Other
ProtoNet P35738.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; Mitochondrion; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    48  48     Mitochondrion (Potential). 
CHAIN   49   390  342     2-oxoisovalerate dehydrogenase subunit beta, mitochondrial. PRO_0000020471
CONFLICT   255   255        K -> R (in Ref. 3; AAA73899). 
CONFLICT   303   303        R -> T (in Ref. 3; AAA73899). 
Sequence information
Length: 390 AA [This is the length of the unprocessed precursor] Molecular weight: 42823 Da [This is the MW of the unprocessed precursor] CRC64: 7A562A868823A1BF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAVAARAGG LLRLGAAGAE RRRRGLRCAA LVQGFLQPAV DDASQKRRVA HFTFQPDPES 

        70         80         90        100        110        120 
LQYGQTQKMN LFQSITSALD NSLAKDPTAV IFGEDVAFGG VFRCTVGLRD KYGKDRVFNT 

       130        140        150        160        170        180 
PLCEQGIVGF GIGIAVTGAT AIAEIQFADY IFPAFDQIVN EAAKYRYRSG DLFNCGSLTI 

       190        200        210        220        230        240 
RAPWGCVGHG ALYHSQSPEA FFAHCPGIKV VIPRSPFQAK GLLLSCIEDK NPCIFFEPKI 

       250        260        270        280        290        300 
LYRAAVEQVP VEPYKIPLSQ AEVIQEGSDV TLVAWGTQVH VIREVASMAQ EKLGVSCEVI 

       310        320        330        340        350        360 
DLRTIVPWDV DTVCKSVIKT GRLLISHEAP LTGGFASEIS STVQEECFLN LEAPISRVCG 

       370        380        390 
YDTPFPHIFE PFYIPDKWKC YDALRKMINY 

P35738 in FASTA format

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View entry in raw text format (no links)
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