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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), 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 (pgm_1), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (pgm_1), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (pgm_2), 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-independent phosphoglycerate mutase (pgm_2), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (pgm_2), 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), Enolase (eno), Enolase (eno)
  5. Pyruvate kinase, Pyruvate kinase (pykA), Pyruvate kinase (pykA), Pyruvate kinase (pyk), Pyruvate kinase (pykA), Pyruvate kinase (pykA), Pyruvate kinase (pykA), Pyruvate kinase (RK97_07530), Pyruvate kinase (pykA), 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

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001339701 – 434EnolaseAdd BLAST434

Interactioni

Protein-protein interaction databases

STRINGi93062.SACOL0842.

Structurei

Secondary structure

1434
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 13Combined sources11
Beta strandi19 – 27Combined sources9
Beta strandi32 – 36Combined sources5
Beta strandi45 – 47Combined sources3
Helixi59 – 61Combined sources3
Helixi65 – 73Combined sources9
Helixi75 – 81Combined sources7
Helixi89 – 100Combined sources12
Turni106 – 108Combined sources3
Helixi110 – 128Combined sources19
Helixi132 – 137Combined sources6
Beta strandi149 – 153Combined sources5
Helixi155 – 157Combined sources3
Beta strandi159 – 161Combined sources3
Beta strandi165 – 170Combined sources6
Helixi177 – 197Combined sources21
Helixi217 – 230Combined sources14
Turni236 – 238Combined sources3
Beta strandi239 – 244Combined sources6
Helixi247 – 250Combined sources4
Beta strandi255 – 257Combined sources3
Helixi259 – 262Combined sources4
Helixi271 – 284Combined sources14
Beta strandi287 – 292Combined sources6
Helixi299 – 309Combined sources11
Turni310 – 312Combined sources3
Beta strandi313 – 318Combined sources6
Turni319 – 323Combined sources5
Helixi325 – 334Combined sources10
Beta strandi338 – 342Combined sources5
Helixi344 – 347Combined sources4
Helixi350 – 362Combined sources13
Beta strandi366 – 370Combined sources5
Helixi380 – 387Combined sources8
Beta strandi392 – 394Combined sources3
Beta strandi398 – 400Combined sources3
Helixi401 – 417Combined sources17
Helixi418 – 420Combined sources3
Helixi425 – 428Combined sources4

3D structure databases

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

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.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5BOEX-ray1.60A/B1-434[»]
5BOFX-ray2.45A/B1-434[»]
ProteinModelPortaliO69174.
SMRiO69174.
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

CDDicd03313. enolase. 1 hit.
Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase. 1 hit.
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...

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: November 2, 2016
This is version 98 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.