Reviewed, UniProtKB/Swiss-Prot P0A0A1 (ODPB_STAAM)

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:	SAV1094

Organism

Staphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]

Taxonomic identifier

158878 [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_0000162229
Sites
	Binding site	60	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A0A1-1 [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

[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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000017 Genomic DNA. Translation: BAB57256.1.
RefSeq	NP_371618.1.
3D structure databases
HSSP	HSSP built from PDB template 1IK6 based on UniProtKB Q8ZUR7.
SMR	P0A0A1. Positions 2-325.
ModBase	Search...
2-D gel databases
World-2DPAGE	0002:P0A0A1.
Genome annotation databases
GeneID	1121071.
GenomeReviews	Gene locus SAV1094 in contig BA000017_GR.
KEGG	sav:SAV1094.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0A0A1.
OMA	P0A0A1. GQAENIW.
Enzyme and pathway databases
BioCyc	SAUR158878:SAV1094-MON.
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_STAAM

Accession

Primary (citable) accession number: P0A0A1
Secondary accession number(s): Q9L6H5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	June 16, 2009
This is version 28 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)