Reviewed, UniProtKB/Swiss-Prot P99063 (ODPB_STAAN)

Names and origin

Protein names

Recommended name:
    Pyruvate dehydrogenase E1 component subunit beta
    EC=1.2.4.1

Gene names

Name:	pdhB
Ordered Locus Names:	SA0944

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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) By similarity.
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
Cofactor	Thiamine pyrophosphate By similarity.
Subunit structure	Heterodimer of an alpha and a beta chain.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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
	Chain	1 – 325	325	Pyruvate dehydrogenase E1 component subunit beta		PRO_0000162230
Sites
	Binding site	60	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P99063-1 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: 432ABDF6E4A720D5	FASTA	325	35,246
	10 20 30 40 50 60 MAQMTMVQAI NDALKTELKN DQDVLIFGED VGVNGGVFRV TEGLQKEFGE DRVFDTPLAE 70 80 90 100 110 120 SGIGGLAMGL AVEGFRPVME VQFLGFVFEV FDAIAGQIAR TRFRSGGTKT APVTIRSPFG 130 140 150 160 170 180 GGVHTPELHA DNLEGILAQS PGLKVVIPSG PYDAKGLLIS SIRSNDPVVY LEHMKLYRSF 190 200 210 220 230 240 REEVPEEEYT IDIGKANVKK EGNDISIITY GAMVQESMKA AEELEKDGYS VEVIDLRTVQ 250 260 270 280 290 300 PIDVDTIVAS VEKTGRAVVV QEAQRQAGVG AAVVAELSER AILSLEAPIG RVAAADTIYP 310 320 FTQAENVWLP NKNDIIEKAK ETLEF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth." Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J. J. Microbiol. Methods 60:247-257(2005) [PubMed: 15590099] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[3]	"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000018 Genomic DNA. Translation: BAB42190.1.
PIR	C89879.
RefSeq	NP_374212.1.
3D structure databases
HSSP	HSSP built from PDB template 1IK6 based on UniProtKB Q8ZUR7.
SMR	P99063. Positions 2-325.
ModBase	Search...
Protein-protein interaction databases
STRING	P99063.
2-D gel databases
SWISS-2DPAGE	P99063.
Genome annotation databases
GeneID	1123769.
GenomeReviews	Gene locus SA0944 in contig BA000018_GR.
KEGG	sau:SA0944.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P99063.
OMA	GQAENIW.
Enzyme and pathway databases
BioCyc	SAUR158879:SA0944-MON.
Family and domain databases
InterPro	IPR015941. Transketolase-like_C. IPR005475. Transketolase-like_Pyr-bd. IPR005476. Transketolase_C. [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_STAAN

Accession

Primary (citable) accession number: P99063
Secondary accession number(s): Q9L6H5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	November 3, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)