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UniProtKB/Swiss-Prot entry P60089

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

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Entry information
Entry name ODPA_STAAM
Primary accession number P60089
Secondary accession number Q931U0
Integrated into Swiss-Prot on November 28, 2003
Sequence was last modified on November 28, 2003 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 32)
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: SAV1093
From
Staphylococcus aureus (strain Mu50 / ATCC 700699) [TaxID: 158878] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Staphylococcus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/S0140-6736(00)04403-2; PubMed=11418146 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
Lancet 357:1225-1240(2001).
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
BA000017; BAB57255.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_371617.1; -.
3D structure databases
SMR P60089; 8-370.
ModBase P60089.
Enzyme and pathway databases
BioCyc SAUR158878:SAV1093-MON; -.
2D gel databases
World-2DPAGE 0002:P60089; -.
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.
ProtoNet P60089.
Genome annotation databases
GeneID 1121070; -.
GenomeReviews BA000017_GR; SAV1093.
KEGG sav:SAV1093; -.
Phylogenomic databases
HOGENOM P60089; -.
Genome annotation databases
CMR P60089; SAV1093.
Other
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_0000162206
Sequence information
Length: 370 AA [This is the length of the unprocessed precursor] Molecular weight: 41383 Da [This is the MW of the unprocessed precursor] CRC64: 66BD3BF8A0C9565F [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 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
P60089 in FASTA format

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