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Protein

Enolase

Gene

eno

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
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. Binds plasminogen when expressed at the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to the degradation of the extracellular matrix and transmigration of the bacteria.UniRule annotation3 Publications

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.UniRule annotation1 Publication

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

Kineticsi

Catalytically active also when expressed on the bacterial cell surface.

  1. KM=4.5 mM for 2-phospho-D-glycerate1 Publication
  1. Vmax=2.792 µmol/min/mg enzyme1 Publication

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)
  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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei155 – 1551SubstrateUniRule annotation
Binding sitei164 – 1641SubstrateUniRule annotation
Active sitei205 – 2051Proton donorUniRule annotation
Metal bindingi242 – 2421MagnesiumUniRule 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

BioCyciSPNE170187:GHGN-1133-MONOMER.
SABIO-RKQ97QS2.
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:SP_1128
OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Taxonomic identifieri170187 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000585 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm
  • Secreted
  • Cell surface

  • 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, probably in complex with plasminogen.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi251 – 2511K → L: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with G-252 and L-254. 1 Publication
Mutagenesisi252 – 2521E → G: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with L-251 and L-254. 1 Publication
Mutagenesisi254 – 2541K → L: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with L-251 and G-252. 1 Publication
Mutagenesisi433 – 4331K → L: Decrease in ability to bind plasminogen under denaturing conditions. No effect on ability to bind plasminogen under non-denaturing conditions. Loss of ability to form homooctamers. Decrease in virulence; when associated with L-434. 2 Publications
Mutagenesisi434 – 4341K → L: Decrease in ability to bind plasminogen under denaturing conditions. No effect on ability to bind plasminogen under non-denaturing conditions. 2 Publications
Mutagenesisi434 – 4341K → L: Decrease in ability to bind plasminogen under denaturing conditions. No effect on ability to bind plasminogen under non-denaturing conditions. Loss of ability to form homooctamers. Decrease in virulence; when associated with L-433. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434EnolasePRO_0000133980Add
BLAST

Proteomic databases

PRIDEiQ97QS2.

Interactioni

Subunit structurei

Homooctamer. Forms a ring-shaped structure.

Binary interactionsi

WithEntry#Exp.IntActNotes
aroAQ9S4002EBI-2207206,EBI-2207276
asnSQ97PR02EBI-2207206,EBI-2207302
dnaJP958302EBI-2207206,EBI-2207079
gatAQ97SE62EBI-2207206,EBI-2207039
gatBQ97SE72EBI-2207206,EBI-2207023
gatCQ97SE52EBI-2207206,EBI-2207053
gltXQ97NG12EBI-2207206,EBI-2207733
groSQ97NV32EBI-2207206,EBI-2206949
grpEQ97S732EBI-2207206,EBI-2207065
lysSQ97RS93EBI-2207206,EBI-2207121
purAP658872EBI-2207206,EBI-2206955
pyrRP659462EBI-2207206,EBI-2207248
uppSQ97SR42EBI-2207206,EBI-2206983
xerSQ97QP22EBI-2207206,EBI-2207218

Protein-protein interaction databases

IntActiQ97QS2. 14 interactions.
STRINGi170187.SpneT_02000650.

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
Helixi59 – 613Combined sources
Helixi65 – 739Combined sources
Helixi75 – 795Combined sources
Helixi87 – 9812Combined sources
Turni104 – 1063Combined sources
Helixi108 – 12619Combined sources
Helixi130 – 1356Combined sources
Beta strandi147 – 1515Combined sources
Helixi153 – 1553Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi163 – 1686Combined sources
Helixi175 – 19521Combined sources
Helixi215 – 22814Combined sources
Turni233 – 2353Combined sources
Beta strandi238 – 2425Combined sources
Helixi245 – 2484Combined 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
1W6TX-ray2.10A/B1-434[»]
ProteinModelPortaliQ97QS2.
SMRiQ97QS2. Positions 1-432.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ97QS2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 639Antigenic epitope
Regioni370 – 3734Substrate bindingUniRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi248 – 2569Plasminogen-binding

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.
HOGENOMiHOG000072174.
KOiK01689.
OMAiEFMIIPV.
OrthoDBiEOG65J589.

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.

Q97QS2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIITDVYAR EVLDSRGNPT LEVEVYTESG AFGRGMVPSG ASTGEHEAVE
60 70 80 90 100
LRDGDKSRYG GLGTQKAVDN VNNIIAEAII GYDVRDQQAI DRAMIALDGT
110 120 130 140 150
PNKGKLGANA ILGVSIAVAR AAADYLEIPL YSYLGGFNTK VLPTPMMNII
160 170 180 190 200
NGGSHSDAPI AFQEFMILPV GAPTFKEALR YGAEIFHALK KILKSRGLET
210 220 230 240 250
AVGDEGGFAP RFEGTEDGVE TILAAIEAAG YVPGKDVFIG FDCASSEFYD
260 270 280 290 300
KERKVYDYTK FEGEGAAVRT SAEQIDYLEE LVNKYPIITI EDGMDENDWD
310 320 330 340 350
GWKALTERLG KKVQLVGDDF FVTNTDYLAR GIQEGAANSI LIKVNQIGTL
360 370 380 390 400
TETFEAIEMA KEAGYTAVVS HRSGETEDST IADIAVATNA GQIKTGSLSR
410 420 430
TDRIAKYNQL LRIEDQLGEV AEYRGLKSFY NLKK
Length:434
Mass (Da):47,103
Last modified:October 1, 2001 - v1
Checksum:i0D64F8F04BBB99C4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21Missing AA sequence (PubMed:11442827).Curated
Sequence conflicti20 – 201T → P AA sequence (PubMed:11442827).Curated
Sequence conflicti24 – 241E → G AA sequence (PubMed:12435062).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005672 Genomic DNA. Translation: AAK75238.1.
PIRiE95130.
RefSeqiWP_000022813.1. NZ_AKVY01000001.1.

Genome annotation databases

EnsemblBacteriaiAAK75238; AAK75238; SP_1128.
KEGGispn:SP_1128.
PATRICi19706667. VBIStrPne105772_1178.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005672 Genomic DNA. Translation: AAK75238.1.
PIRiE95130.
RefSeqiWP_000022813.1. NZ_AKVY01000001.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W6TX-ray2.10A/B1-434[»]
ProteinModelPortaliQ97QS2.
SMRiQ97QS2. Positions 1-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ97QS2. 14 interactions.
STRINGi170187.SpneT_02000650.

Proteomic databases

PRIDEiQ97QS2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK75238; AAK75238; SP_1128.
KEGGispn:SP_1128.
PATRICi19706667. VBIStrPne105772_1178.

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.
HOGENOMiHOG000072174.
KOiK01689.
OMAiEFMIIPV.
OrthoDBiEOG65J589.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BioCyciSPNE170187:GHGN-1133-MONOMER.
SABIO-RKQ97QS2.

Miscellaneous databases

EvolutionaryTraceiQ97QS2.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-334 / TIGR4.
  2. "Alpha-enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface."
    Bergmann S., Rohde M., Chhatwal G.S., Hammerschmidt S.
    Mol. Microbiol. 40:1273-1287(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20, SUBCELLULAR LOCATION, FUNCTION IN VIRULENCE, BINDING TO PLASMINOGEN, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-433 AND LYS-434.
    Strain: ATCC 11733 / Seroytpe 2.
  3. "Purification of native alpha-enolase from Streptococcus pneumoniae that binds plasminogen and is immunogenic."
    Whiting G.C., Evans J.T., Patel S., Gillespie S.H.
    J. Med. Microbiol. 51:837-843(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-31, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BINDING TO PLASMINOGEN, IMMUNOGENICITY.
  4. "Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae."
    Bergmann S., Wild D., Diekmann O., Frank R., Bracht D., Chhatwal G.S., Hammerschmidt S.
    Mol. Microbiol. 49:411-423(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PLASMINOGEN-BINDING MOTIF, MUTAGENESIS OF LYS-251; GLU-252; LYS-254; LYS-433 AND LYS-434.
    Strain: ATCC 11733 / Seroytpe 2 and D39 / Serotype 2.
  5. "The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration."
    Bergmann S., Rohde M., Preissner K.T., Hammerschmidt S.
    Thromb. Haemost. 94:304-311(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF PLASMINOGEN-BINDING MOTIF ON DEGRADATION OF EXTRACELLULAR MATRIX.
    Strain: D39 / Serotype 2.
  6. "Streptococcus pneumoniae enolase is important for plasminogen binding despite low abundance of enolase protein on the bacterial cell surface."
    Kolberg J., Aase A., Bergmann S., Herstad T.K., Roedal G., Frank R., Rohde M., Hammerschmidt S.
    Microbiology 152:1307-1317(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: EPITOPE MAPPING, ANTIGENICITY.
    Strain: ATCC 11733 / Seroytpe 2.
  7. "Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: crystal structure and evaluation of plasmin(ogen)-binding sites."
    Ehinger S., Schubert W.-D., Bergmann S., Hammerschmidt S., Heinz D.W.
    J. Mol. Biol. 343:997-1005(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    Strain: ATCC 11733 / Seroytpe 2.

Entry informationi

Entry nameiENO_STRPN
AccessioniPrimary (citable) accession number: Q97QS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: October 1, 2001
Last modified: May 11, 2016
This is version 112 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, Complete proteome, 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.