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Protein

Enolase

Gene

eno

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity). Binds laminin when expressed on the bacterial cell surface; this probably induces destruction of the extracellular matrix, favoring invasion and dissemination.UniRule annotation1 Publication

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. Glyceraldehyde-3-phosphate dehydrogenase (gapA)
  2. Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (pgm_2), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (pgm_1), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (pgm), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (pgm_2), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (pgm_1), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (pgm_2), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (pgm_2), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (pgm), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (HMPREF3211_00061)
  4. Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno)
  5. Pyruvate kinase, Pyruvate kinase (pyk), Pyruvate kinase (pykA), Pyruvate kinase (pykA), Pyruvate kinase (RK97_07530), 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei157 – 1571SubstrateUniRule annotation
Binding sitei166 – 1661SubstrateUniRule annotation
Active sitei207 – 2071Proton donorUniRule annotation
Metal bindingi244 – 2441MagnesiumUniRule annotation
Metal bindingi291 – 2911MagnesiumUniRule annotation
Binding sitei291 – 2911SubstrateUniRule annotation
Metal bindingi318 – 3181MagnesiumUniRule annotation
Binding sitei318 – 3181SubstrateUniRule annotation
Active sitei343 – 3431Proton acceptorUniRule annotation
Binding sitei343 – 3431Substrate (covalent); in inhibited formUniRule annotation
Binding sitei394 – 3941SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis, Virulence

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi4.2.1.11. 3352.
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
Laminin-binding protein
Gene namesi
Name:enoUniRule annotation
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication
  • Secreted UniRule annotation1 Publication
  • Cell surface UniRule annotation1 Publication

  • 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.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434EnolasePRO_0000133970Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi93062.SACOL0842.

Structurei

Secondary structure

1
434
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1311Combined sources
Beta strandi19 – 279Combined sources
Beta strandi32 – 365Combined sources
Beta strandi45 – 473Combined sources
Helixi59 – 613Combined sources
Helixi65 – 739Combined sources
Helixi75 – 817Combined sources
Helixi89 – 10012Combined sources
Turni106 – 1083Combined sources
Helixi110 – 12819Combined sources
Helixi132 – 1376Combined sources
Beta strandi149 – 1535Combined sources
Helixi155 – 1573Combined sources
Beta strandi159 – 1613Combined sources
Beta strandi165 – 1706Combined sources
Helixi177 – 19721Combined sources
Helixi217 – 23014Combined sources
Turni236 – 2383Combined sources
Beta strandi239 – 2446Combined sources
Helixi247 – 2504Combined sources
Beta strandi255 – 2573Combined sources
Helixi259 – 2624Combined sources
Helixi271 – 28414Combined sources
Beta strandi287 – 2926Combined sources
Helixi299 – 30911Combined sources
Turni310 – 3123Combined sources
Beta strandi313 – 3186Combined sources
Turni319 – 3235Combined sources
Helixi325 – 33410Combined sources
Beta strandi338 – 3425Combined sources
Helixi344 – 3474Combined sources
Helixi350 – 36213Combined sources
Beta strandi366 – 3705Combined sources
Helixi380 – 3878Combined sources
Beta strandi392 – 3943Combined sources
Beta strandi398 – 4003Combined sources
Helixi401 – 41717Combined sources
Helixi418 – 4203Combined sources
Helixi425 – 4284Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5BOEX-ray1.60A/B1-434[»]
5BOFX-ray2.45A/B1-434[»]
ProteinModelPortaliO69174.
SMRiO69174. Positions 1-432.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 3734Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O69174-1 [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 LKSILSQRGL
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:August 1, 1998 - v1
Checksum:iC4A19BA3675429B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF065394 Genomic DNA. Translation: AAC17130.1.
PIRiT47276.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF065394 Genomic DNA. Translation: AAC17130.1.
PIRiT47276.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5BOEX-ray1.60A/B1-434[»]
5BOFX-ray2.45A/B1-434[»]
ProteinModelPortaliO69174.
SMRiO69174. Positions 1-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL0842.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BRENDAi4.2.1.11. 3352.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification of enolase as a laminin binding protein at the surface of Staphylococcus aureus."
    Choi G.H., Simpson A.J.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ISP3.
  2. "Identification of enolase as a laminin-binding protein on the surface of Staphylococcus aureus."
    Carneiro C.R.W., Postol E., Nomizo R., Reis L.F.L., Brentani R.R.
    Microbes Infect. 6:604-608(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, FUNCTION IN VIRULENCE, BINDING TO LAMININ.
    Strain: ATCC 10832 / Wood 46.

Entry informationi

Entry nameiENO_STAAU
AccessioniPrimary (citable) accession number: O69174
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 1, 1998
Last modified: May 11, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.