Reviewed, UniProtKB/Swiss-Prot Q820A6 (ODPA_STAAN)

Names and origin

Protein names

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

Gene names

Name:	pdhA
Ordered Locus Names:	SA0943.1

Organism

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

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	370 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 CO(2). 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 + CO(2).
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 – 370	370	Pyruvate dehydrogenase E1 component subunit alpha		PRO_0000162207

Sequences

	Sequence		Length	Mass (Da)
	Q820A6-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 66BD3BF8A0C9565F	FASTA	370	41,383
	10 20 30 40 50 60 MAPKLQAQFD AVKVLNDTQS KFEMVQILDE NGNVVNEDLV PDLTDEQLVE LMERMVWTRI 70 80 90 100 110 120 LDQRSISLNR QGRLGFYAPT AGQEASQLAS QYALEKEDYI LPGYRDVPQI IWHGLPLTEA 130 140 150 160 170 180 FLFSRGHFKG NQFPEGVNAL SPQIIIGAQY IQAAGVAFAL KKRGKNAVAI TYTGDGGSSQ 190 200 210 220 230 240 GDFYEGINFA AAYKAPAIFV IQNNNYAIST PRSKQTAAET LAQKAIAVGI PGIQVDGMDA 250 260 270 280 290 300 LAVYQATKEA RDRAVAGEGP TLIETMTYRY GPHTMAGDDP TRYRTSDEDA EWEKKDPLVR 310 320 330 340 350 360 FRKFLENKGL WNEDKENEVI ERAKADIKAA IKEADNTEKQ TVTSLMEIMY EDMPQNLAEQ 370 YEIYKEKESK

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., Lescuye P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000018 Genomic DNA. Translation: BAC55165.1.
RefSeq	NP_808209.1.
3D structure databases
HSSP	HSSP built from PDB template 1DTW based on UniProtKB P12694.
SMR	Q820A6. Positions 8-370.
ModBase	Search...
2-D gel databases
SWISS-2DPAGE	Q820A6.
Genome annotation databases
GeneID	1123768.
GenomeReviews	Gene locus SA0943.1 in contig BA000018_GR.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q820A6.
Family and domain databases
InterPro	IPR001017. DHase_E1. IPR017596. Pyrv_DH_E1_asu_subgrp-x. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODPA_STAAN

Accession

Primary (citable) accession number: Q820A6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	June 1, 2003
Last modified:	November 4, 2008
This is version 35 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)