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Protein

Enolase

Gene

eno

Organism
Staphylococcus aureus (strain NCTC 8325)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.UniRule annotation

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.UniRule annotation

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.UniRule annotation

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
  4. Enolase (eno)
  5. Pyruvate kinase (pyk)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei157SubstrateUniRule annotation1
Binding sitei166SubstrateUniRule annotation1
Active sitei207Proton donorUniRule annotation1
Metal bindingi244MagnesiumUniRule annotation1
Metal bindingi291MagnesiumUniRule annotation1
Binding sitei291SubstrateUniRule annotation1
Metal bindingi318MagnesiumUniRule annotation1
Binding sitei318SubstrateUniRule annotation1
Active sitei343Proton acceptorUniRule annotation1
Binding sitei343Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei394SubstrateUniRule annotation1

GO - Molecular functioni

  • collagen binding Source: CAFA
  • laminin binding Source: CAFA
  • magnesium ion binding Source: InterPro
  • phosphopyruvate hydratase activity Source: UniProtKB-EC

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processGlycolysis, Virulence
LigandMagnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
EnolaseUniRule annotation (EC:4.2.1.11UniRule annotation)
Alternative name(s):
2-phospho-D-glycerate hydro-lyaseUniRule annotation
2-phosphoglycerate dehydrataseUniRule annotation
Gene namesi
Name:enoUniRule annotation
Ordered Locus Names:SAOUHSC_00799
OrganismiStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifieri93061 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000008816 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Secreted UniRule annotation
  • Cell surface UniRule annotation

  • Note: Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface.UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Disruption phenotypei

Essential, it cannot be deleted, although it can be replaced by its E.coli counterpart.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002671111 – 434EnolaseAdd BLAST434

Interactioni

Subunit structurei

Homodimer (Probable). Component of a possible RNA degradosome complex composed of cshA, eno, pfkA, pnp, rnjA, rnjB, rnpA and rny. Interacts specifically with RNA helicase CshA, PNPase and RNase Y.Curated1 Publication

GO - Molecular functioni

  • collagen binding Source: CAFA
  • laminin binding Source: CAFA

Protein-protein interaction databases

STRINGi93061.SAOUHSC_00799.

Structurei

3D structure databases

ProteinModelPortaliQ2G028.
SMRiQ2G028.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni370 – 373Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.
HOGENOMiHOG000072173.
KOiK01689.
OMAiEFMIIPV.

Family and domain databases

CDDicd03313. enolase. 1 hit.
Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase. 1 hit.
InterProiView protein in InterPro
IPR000941. Enolase.
IPR034390. Enolase-like_superfamily.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiView protein in Pfam
PF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SFLDiSFLDG00178. enolase. 1 hit.
SFLDS00001. Enolase. 1 hit.
SMARTiView protein in SMART
SM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiView protein in PROSITE
PS00164. ENOLASE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q2G028-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIITDVYAR EVLDSRGNPT VEVEVLTESG AFGRALVPSG ASTGEHEAVE
60 70 80 90 100
LRDGDKSRYL GKGVTKAVEN VNEIIAPEII EGEFSVLDQV SIDKMMIALD
110 120 130 140 150
GTPNKGKLGA NAILGVSIAV ARAAADLLGQ PLYKYLGGFN GKQLPVPMMN
160 170 180 190 200
IVNGGSHSDA PIAFQEFMIL PVGATTFKES LRWGTEIFHN LKSILSKRGL
210 220 230 240 250
ETAVGDEGGF APKFEGTEDA VETIIQAIEA AGYKPGEEVF LGFDCASSEF
260 270 280 290 300
YENGVYDYSK FEGEHGAKRT AAEQVDYLEQ LVDKYPIITI EDGMDENDWD
310 320 330 340 350
GWKQLTERIG DRVQLVGDDL FVTNTEILAK GIENGIGNSI LIKVNQIGTL
360 370 380 390 400
TETFDAIEMA QKAGYTAVVS HRSGETEDTT IADIAVATNA GQIKTGSLSR
410 420 430
TDRIAKYNQL LRIEDELFET AKYDGIKSFY NLDK
Length:434
Mass (Da):47,117
Last modified:March 21, 2006 - v1
Checksum:i756D40CED18865D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000253 Genomic DNA. Translation: ABD29927.1.
RefSeqiWP_001121760.1. NC_007795.1.
YP_499355.1. NC_007795.1.

Genome annotation databases

EnsemblBacteriaiABD29927; ABD29927; SAOUHSC_00799.
GeneIDi31213594.
3919362.
KEGGisao:SAOUHSC_00799.
PATRICifig|93061.5.peg.723.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiENO_STAA8
AccessioniPrimary (citable) accession number: Q2G028
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: March 21, 2006
Last modified: June 7, 2017
This is version 89 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families