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UniProtKB/Swiss-Prot entry Q5HGZ0


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

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Entry information
Entry name ODPB_STAAC
Primary accession number Q5HGZ0
Secondary accession numbers None
Integrated into Swiss-Prot on December 20, 2005
Sequence was last modified on February 15, 2005 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 29)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit beta
Synonym EC 1.2.4.1
Gene name
Name: pdhB
OrderedLocusNames: SACOL1103
From
Staphylococcus aureus (strain COL) [TaxID: 93062] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Staphylococcus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.187.7.2426-2438.2005; PubMed=15774886 [NCBI, ExPASy, EBI, Israel, Japan]
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.;
"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain.";
J. Bacteriol. 187:2426-2438(2005).
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
CP000046; AAW37983.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_185967.1; -.
3D structure databases
SMR Q5HGZ0; 2-325.
ModBase Q5HGZ0.
Enzyme and pathway databases
BioCyc SAUR93062:SACOL1103-MON; -.
Family and domain databases
InterPro IPR005476; Transketo_C.
IPR005475; Transketo_Cen_R.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.920; Transketo_C_like; 1.
Pfam PF02779; Transket_pyr; 1.
PF02780; Transketolase_C; 1.
Pfam graphical view of domain structure.
BLOCKS Q5HGZ0.
Genome annotation databases
GeneID 3237846; -.
GenomeReviews CP000046_GR; SACOL1103.
KEGG sac:SACOL1103; -.
TIGR SACOL1103; -.
Phylogenomic databases
HOGENOM Q5HGZ0; -.
Other
ProtoNet Q5HGZ0.
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   325  325     Pyruvate dehydrogenase E1 component subunit beta. PRO_0000162228
BINDING   60    60        Thiamine pyrophosphate (By similarity). 
Sequence information
Length: 325 AA [This is the length of the unprocessed precursor] Molecular weight: 35216 Da [This is the MW of the unprocessed precursor] CRC64: EDFFFCB83E726E0F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAQMTMVQAI NDALKTELKN DQDVLIFGED VGVNGGVFRV TEGLQKEFGE DRVFDTPLAE 

        70         80         90        100        110        120 
SGIGGLAMGL AVEGFRPVME VQFLGFVFEV FDAIAGQIAR TRFRSGGTKT APVTIRGPFG 

       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 

Q5HGZ0 in FASTA format

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