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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)DescriptionActionsGraphical viewLength
Binding sitei155SubstrateUniRule annotation1
Binding sitei164SubstrateUniRule annotation1
Active sitei205Proton donorUniRule annotation1
Metal bindingi242MagnesiumUniRule 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

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)DescriptionActionsGraphical viewLength
Mutagenesisi251K → L: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with G-252 and L-254. 1 Publication1
Mutagenesisi252E → G: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with L-251 and L-254. 1 Publication1
Mutagenesisi254K → L: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with L-251 and G-252. 1 Publication1
Mutagenesisi433K → 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 Publications1
Mutagenesisi434K → L: Decrease in ability to bind plasminogen under denaturing conditions. No effect on ability to bind plasminogen under non-denaturing conditions. 2 Publications1
Mutagenesisi434K → 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 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001339801 – 434EnolaseAdd BLAST434

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 interactors.
STRINGi170187.SpneT_02000650.

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
Helixi59 – 61Combined sources3
Helixi65 – 73Combined sources9
Helixi75 – 79Combined sources5
Helixi87 – 98Combined sources12
Turni104 – 106Combined sources3
Helixi108 – 126Combined sources19
Helixi130 – 135Combined sources6
Beta strandi147 – 151Combined sources5
Helixi153 – 155Combined sources3
Beta strandi157 – 159Combined sources3
Beta strandi163 – 168Combined sources6
Helixi175 – 195Combined sources21
Helixi215 – 228Combined sources14
Turni233 – 235Combined sources3
Beta strandi238 – 242Combined sources5
Helixi245 – 248Combined sources4
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
1W6TX-ray2.10A/B1-434[»]
ProteinModelPortaliQ97QS2.
SMRiQ97QS2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ97QS2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni55 – 63Antigenic epitope9
Regioni370 – 373Substrate bindingUniRule annotation4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi248 – 256Plasminogen-binding9

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.
HOGENOMiHOG000072174.
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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti2Missing AA sequence (PubMed:11442827).Curated1
Sequence conflicti20T → P AA sequence (PubMed:11442827).Curated1
Sequence conflicti24E → G AA sequence (PubMed:12435062).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W6TX-ray2.10A/B1-434[»]
ProteinModelPortaliQ97QS2.
SMRiQ97QS2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ97QS2. 14 interactors.
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.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
SABIO-RKQ97QS2.

Miscellaneous databases

EvolutionaryTraceiQ97QS2.

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_STRPN
AccessioniPrimary (citable) accession number: Q97QS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: October 1, 2001
Last modified: November 2, 2016
This is version 115 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.