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Protein

Enolase

Gene

eno

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionLyase
Biological processGlycolysis, Virulence
LigandMagnesium, Metal-binding

Enzyme and pathway databases

SABIO-RKiQ97QS2
UniPathwayiUPA00109; UER00187

Protein family/group databases

MoonProtiQ97QS2

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

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

Interactioni

Subunit structurei

Homooctamer. Forms a ring-shaped structure.

Binary interactionsi

Show more details

Protein-protein interaction databases

IntActiQ97QS2, 14 interactors

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
InterProiView protein in InterPro
IPR000941 Enolase
IPR036849 Enolase-like_C_sf
IPR029017 Enolase-like_N
IPR034390 Enolase-like_superfamily
IPR020810 Enolase_C
IPR020809 Enolase_CS
IPR020811 Enolase_N
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
TIGRFAMsiTIGR01060 eno, 1 hit
PROSITEiView protein in PROSITE
PS00164 ENOLASE, 1 hit

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
GeneIDi31536454
KEGGispn:SP_1128

Similar proteinsi

Entry informationi

Entry nameiENO_STRPN
AccessioniPrimary (citable) accession number: Q97QS2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: October 1, 2001
Last modified: May 23, 2018
This is version 125 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

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

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