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Q5HQ76 (ODPA_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component subunit alpha

EC=1.2.4.1
Gene names
Name:pdhA
Ordered Locus Names:SERP0680
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. 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 structure

Heterodimer of an alpha and a beta chain.

Ontologies

Keywords
   Biological processGlycolysis
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: UniProtKB-EC

thiamine pyrophosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Pyruvate dehydrogenase E1 component subunit alpha
PRO_0000162212

Sequences

Sequence LengthMass (Da)Tools
Q5HQ76 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: F691D1D8C2E3EEB4

FASTA37041,330
        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 

« Hide

References

[1]"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."
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. expand/collapse author list , 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.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW54052.1.
RefSeqYP_188264.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HQ76.
SMRQ5HQ76. Positions 8-370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176279.SERP0680.

Proteomic databases

PRIDEQ5HQ76.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW54052; AAW54052; SERP0680.
GeneID3240395.
KEGGser:SERP0680.
PATRIC19612229. VBIStaEpi130894_0658.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1071.
HOGENOMHOG000281335.
KOK00161.
OMANNGYAIT.
OrthoDBEOG6VMTKR.

Enzyme and pathway databases

BioCycSEPI176279:GJJB-705-MONOMER.

Family and domain databases

Gene3D3.40.50.970. 1 hit.
InterProIPR001017. DH_E1.
IPR017596. Pyrv_DH_E1_asu_subgrp-x.
IPR029061. THDP-binding.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 1 hit.
TIGRFAMsTIGR03181. PDH_E1_alph_x. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODPA_STAEQ
AccessionPrimary (citable) accession number: Q5HQ76
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 15, 2005
Last modified: June 11, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program