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P35738 (ODBB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
EC=1.2.4.4
Alternative name(s):
Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
Short name=BCKDE1B
Short name=BCKDH E1-beta
Gene names
Name:Bckdhb
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. 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 structure

Heterodimer of an alpha and a beta chain.

Subcellular location

Mitochondrion matrix.

Sequence caution

The sequence AAA73899.1 differs from that shown. Reason: Frameshift at positions 101 and 120.

The sequence AAA73899.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4848Mitochondrion Potential
Chain49 – 3903422-oxoisovalerate dehydrogenase subunit beta, mitochondrial
PRO_0000020471

Amino acid modifications

Modified residue2391N6-acetyllysine By similarity

Experimental info

Sequence conflict2551K → R in AAA73899. Ref.3
Sequence conflict3031R → T in AAA73899. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P35738 [UniParc].

Last modified December 4, 2007. Version 3.
Checksum: 7A562A868823A1BF

FASTA39042,823
        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

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
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. expand/collapse author list , 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.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]The MGC Project Team
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-230.
[3]"Molecular cloning of the E1 beta subunit of the rat branched chain alpha-ketoacid dehydrogenase."
Zhao Y., Kuntz M.J., Harris R.A., Crabb D.W.
Biochim. Biophys. Acta 1132:207-210(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-390, PROTEIN SEQUENCE OF 49-75.
[4]Erratum
Zhao Y., Kuntz M.J., Harris R.A., Crabb D.W.
Biochim. Biophys. Acta 1260:243-243(1995) [PubMed] [Europe PMC] [Abstract]
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AABR03062593 Genomic DNA. No translation available.
AABR03062720 Genomic DNA. No translation available.
AABR03063125 Genomic DNA. No translation available.
AABR03063398 Genomic DNA. No translation available.
M94040 mRNA. Translation: AAA73899.1. Sequence problems.
IPIIPI00201636.
PIRS28950.
RefSeqNP_062140.1. NM_019267.1.
UniGeneRn.15623.

3D structure databases

ProteinModelPortalP35738.
SMRP35738. Positions 65-390.
ModBaseSearch...

Proteomic databases

PaxDbP35738.
PRIDEP35738.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29711.
KEGGrno:29711.
UCSCRGD:2197. rat.

Organism-specific databases

CTD594.
RGD2197. Bckdhb.

Phylogenomic databases

eggNOGCOG0022.
HOGENOMHOG000281451.
HOVERGENHBG108210.
InParanoidP35738.
KOK00167.
OrthoDBEOG4HQDJN.

Enzyme and pathway databases

SABIO-RKP35738.

Gene expression databases

ArrayExpressP35738.
GenevestigatorP35738.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
InterProIPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52922. Transketo_C_like. 1 hit.
ProtoNetSearch...

Other

NextBio610143.

Entry information

Entry nameODBB_RAT
AccessionPrimary (citable) accession number: P35738
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 4, 2007
Last modified: April 3, 2013
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info