Reviewed, UniProtKB/Swiss-Prot P11966 (ODPB_BOVIN)

Names and origin

Protein names

Recommended name:
    Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
      Short name=PDHE1-B
    EC=1.2.4.1

Gene names

Name:

PDHB

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	359 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 pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
Cofactor	Thiamine pyrophosphate.
Subunit structure	Tetramer of 2 alpha and 2 beta subunits.
Subcellular location	Mitochondrion matrix.
Sequence caution	The sequence AAX46758.1 differs from that shown. Reason: Frameshift at position 201.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 30	30	Mitochondrion Ref.3
	Chain	31 – 359	329	Pyruvate dehydrogenase E1 component subunit beta, mitochondrial		PRO_0000162216
Sites
	Binding site	89	1	Thiamine pyrophosphate By similarity
Amino acid modifications
	Modified residue	67	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P11966-1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 584B86D36A233EFC	FASTA	359	39,126
	10 20 30 40 50 60 MAVVAVLVRK PLEQVSGLLR RRFHRTAPAA LQVTVREAIN QGMDEELERD EKVFLLGEEV 70 80 90 100 110 120 AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI 130 140 150 160 170 180 DQVINSAAKT YYMSGGLQSV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWSS 190 200 210 220 230 240 EDAKGLIKSA IRDNNPVVVL ENELMYGVPF ELPSEAQSKD FLIPIGKAKI ERQGTHVTIV 250 260 270 280 290 300 AHSRPVGHCL EAATVLSKEG IECEVINLRT IRPMDIETIE GSVMKTNHLV TVEGGWPQFG 310 320 330 340 350 VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSVPQVKDII FAIKKTLNI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Heart ventricle.
[3]	"Identification of a cDNA clone for the beta-subunit of the pyruvate dehydrogenase component of human pyruvate dehydrogenase complex." Ho L., Javed A.A., Pepin R.A., Thekkumkara T.J., Raefsky C., Mole J.E., Caliendo A.M., Kwon M.S., Kerr D.S., Patel M.S. Biochem. Biophys. Res. Commun. 150:904-908(1988) [PubMed: 2829898] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-54.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BT021911 mRNA. Translation: AAX46758.1. Frameshift. BC150020 mRNA. Translation: AAI50021.1.
IPI	IPI00703729.
PIR	B27712.
RefSeq	NP_001030512.2.
UniGene	Bt.49794
3D structure databases
HSSP	HSSP built from PDB template 1NI4 based on UniProtKB P11177.
SMR	P11966. Positions 30-359.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000021724. Bos taurus. [Contig view]
GeneID	613610.
KEGG	bta:613610.
Phylogenomic databases
HOVERGEN	P11966.
OMA	P11966. AAKMHYM.
Enzyme and pathway databases
BRENDA	1.2.4.1. 251.
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. 1 hit.
Pfam	PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODPB_BOVIN

Accession

Primary (citable) accession number: P11966
Secondary accession number(s): A6QQW6, Q58CN6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 17, 2006
Last modified:	June 16, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)