Reviewed, UniProtKB/Swiss-Prot P35738 (ODBB_RAT)

Names and origin

Protein names

Recommended 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=BCKDH E1-beta

Gene names

Name:

Bckdhb

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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: Miscellaneous discrepancy. Contaminating sequence. Sequence of unknown origin in the N-terminal part.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	branched chain family amino acid catabolic process Inferred from sequence or structural similarity. Source: HGNC oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to cAMP Inferred from expression pattern. Source: RGD response to glucocorticoid stimulus Inferred from expression pattern. Source: RGD response to nutrient Inferred from expression pattern. Source: RGD
Cellular component	mitochondrial alpha-ketoglutarate dehydrogenase complex Inferred from sequence or structural similarity. Source: HGNC
Molecular function	3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Inferred from electronic annotation. Source: EC protein complex binding Inferred from physical interaction. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 48	48	Mitochondrion Potential
	Chain	49 – 390	342	2-oxoisovalerate dehydrogenase subunit beta, mitochondrial		PRO_0000020471
Experimental info
	Sequence conflict	255	1	K → R in AAA73899. Ref.3
	Sequence conflict	303	1	R → T in AAA73899. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P35738-1 [UniParc]. Last modified December 4, 2007. Version 3. Checksum: 7A562A868823A1BF	FASTA	390	42,823
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 15057822] [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: 1390893] [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: 7841205] [Abstract]

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00201636.
PIR	S28950.
RefSeq	NP_062140.1.
UniGene	Rn.15623
3D structure databases
HSSP	HSSP built from PDB template 1DTW based on UniProtKB P21953.
SMR	P35738. Positions 40-369.
ModBase	Search...
Proteomic databases
PRIDE	P35738.
Genome annotation databases
Ensembl	ENSRNOG00000009928. Rattus norvegicus. [Contig view]
GeneID	29711.
KEGG	rno:29711.
Organism-specific databases
RGD	2197. Bckdhb.
Phylogenomic databases
HOVERGEN	P35738.
Enzyme and pathway databases
BRENDA	1.2.4.4. 248.
Family and domain databases
InterPro	IPR005476. Transketo_C. IPR015941. Transketolase_C-like. IPR005475. Transketolase_central-reg. [Graphical view]
Gene3D	G3DSA:3.40.50.920. Transketo_C_like. 2 hits.
Pfam	PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	610143.

Entry information

Entry name

ODBB_RAT

Accession

Primary (citable) accession number: P35738

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	December 4, 2007
Last modified:	June 16, 2009
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)