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UniProtKB/Swiss-Prot entry Q8CPN3

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

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Entry information
Entry name ODPA_STAES
Primary accession number Q8CPN3
Secondary accession numbers None
Integrated into Swiss-Prot on November 28, 2003
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 39)
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: SE_0791
From
Staphylococcus epidermidis (strain ATCC 12228) [TaxID: 176280] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Staphylococcus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1046/j.1365-2958.2003.03671.x; PubMed=12950922 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
"Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228).";
Mol. Microbiol. 49:1577-1593(2003).
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
AE015929; AAO04388.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_764346.1; -.
3D structure databases
HSSP P12694; 1DTW. [HSSP ENTRY / PDB]
SMR Q8CPN3; 8-370.
ModBase Q8CPN3.
Enzyme and pathway databases
BioCyc SEPI176280:SE_0791-MON; -.
Ontologies
GO
GO:0004739; Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
Genome annotation databases
GeneID 1057335; -.
GenomeReviews AE015929_GR; SE_0791.
KEGG sep:SE0791; -.
Phylogenomic databases
HOGENOM Q8CPN3; -.
Genome annotation databases
CMR Q8CPN3; SE_0791.
Other
ProtoNet Q8CPN3.
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_0000162211
Sequence information
Length: 370 AA [This is the length of the unprocessed precursor] Molecular weight: 41330 Da [This is the MW of the unprocessed precursor] CRC64: F691D1D8C2E3EEB4 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAPKLQAQFD AVKVLNETQS KFEMVQILDE DGNVVNEDLV PDLTDEQLVE LMERMVWTRI 

        70         80         90        100        110        120 
LDQRSISLNR QGRLGFYAPT AGQEASQLAS QYALESEDFI LPGYRDVPQI IWHGLPLTDA 

       130        140        150        160        170        180 
FLFSRGHFKG NQFPEGVNAL SPQIIIGAQY IQTAGVAFGL KKRGKNAVAI TYTGDGGSSQ 

       190        200        210        220        230        240 
GDFYEGINFA SAYKAPAIFV IQNNNYAIST PRSKQTAAET LAQKAISVGI PGIQVDGMDA 

       250        260        270        280        290        300 
LAVYQATLEA RERAVAGEGP TVIETLTYRY GPHTMAGDDP TRYRTSDEDA EWEKKDPLVR 

       310        320        330        340        350        360 
FRKYLEAKGL WNEDKENEVV ERAKSEIKAA IKEADNTEKQ TVTSLMDIMY EEMPQNLAEQ 

       370 
YEIYKEKESK
Q8CPN3 in FASTA format

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