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UniProtKB/Swiss-Prot entry Q6GHZ2


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODPA_STAAR
Primary accession number Q6GHZ2
Secondary accession numbers None
Integrated into Swiss-Prot on March 1, 2005
Sequence was last modified on July 19, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 26)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit alpha
Synonym EC 1.2.4.1
Gene name
Name: pdhA
OrderedLocusNames: SAR1067
From
Staphylococcus aureus (strain MRSA252) [TaxID: 282458] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Staphylococcus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0402521101; PubMed=15213324 [NCBI, ExPASy, EBI, Israel, Japan]
Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance.";
Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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 + CO2.
  • COFACTOR: Thiamine pyrophosphate (By similarity).
  • SUBUNIT: Heterodimer of an alpha and a beta chain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
BX571856; CAG40069.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_040480.1; -.
3D structure databases
SMR Q6GHZ2; 8-370.
ModBase Q6GHZ2.
Enzyme and pathway databases
BioCyc SAUR282458:SAR1067-MON; -.
Ontologies
GO
GO:0004739; Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR001017; DHase_E1.
IPR017596; Pyrv_DH_E1_asu_subgrp-x.
Graphical view of domain structure.
Pfam PF00676; E1_dh; 1.
Pfam graphical view of domain structure.
BLOCKS Q6GHZ2.
Genome annotation databases
GeneID 2859889; -.
GenomeReviews BX571856_GR; SAR1067.
KEGG sar:SAR1067; -.
Phylogenomic databases
HOGENOM Q6GHZ2; -.
Genome annotation databases
CMR Q6GHZ2; SAR1067.
Other
ProtoNet Q6GHZ2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   370  370     Pyruvate dehydrogenase E1 component subunit alpha. PRO_0000162208
Sequence information
Length: 370 AA [This is the length of the unprocessed precursor] Molecular weight: 41413 Da [This is the MW of the unprocessed precursor] CRC64: 5172134E6FE80EE0 [This is a checksum on the sequence]
        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 IQTAGVAFAL 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 

Q6GHZ2 in FASTA format

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