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Protein

Enolase

Gene

eno

Organism
Streptococcus pyogenes serotype M12 (strain MGAS9429)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.UniRule annotation

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. 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 bindingi243MagnesiumUniRule annotation1
Metal bindingi292MagnesiumUniRule annotation1
Binding sitei292SubstrateUniRule annotation1
Metal bindingi319MagnesiumUniRule annotation1
Binding sitei319SubstrateUniRule annotation1
Active sitei344Proton acceptorUniRule annotation1
Binding sitei344Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei395SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processGlycolysis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187

Protein family/group databases

MoonProtiQ1JML5

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:MGAS9429_Spy0609
OrganismiStreptococcus pyogenes serotype M12 (strain MGAS9429)
Taxonomic identifieri370551 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000002433 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Secreted UniRule annotation
  • Cell surface UniRule annotation
  • 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.UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002671171 – 435EnolaseAdd BLAST435

Structurei

3D structure databases

ProteinModelPortaliQ1JML5
SMRiQ1JML5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni371 – 374Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

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.

Q1JML5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIITDVYAR EVLDSRGNPT LEVEVYTESG AFGRGMVPSG ASTGEHEAVE
60 70 80 90 100
LRDGDKSRYL GLGTQKAVDN VNNIIAEAII GYDVRDQQAI DRAMITLDGT
110 120 130 140 150
PNKGKLGANA ILGVSIAVAR AAADYLEVPL YTYLGGFNTK VLPTPMMNII
160 170 180 190 200
NGGSHSDAPI AFQEFMIMPV GAPTFKEGLR WGAEVFHALK KILKERGLVT
210 220 230 240 250
AVGDEGGFAP KFEGTEDGVE TILKAIEAAG YEAGENGIMI GFDCASSEFY
260 270 280 290 300
DKERKVYDYT KFEGEGAAVR TSAEQVDYLE ELVNKYPIIT IEDGMDENDW
310 320 330 340 350
DGWKVLTERL GKRVQLVGDD FFVTNTEYLA RGIKENAANS ILIKVNQIGT
360 370 380 390 400
LTETFEAIEM AKEAGYTAVV SHRSGETEDS TIADIAVATN AGQIKTGSLS
410 420 430
RTDRIAKYNQ LLRIEDQLGE VAQYKGIKSF YNLKK
Length:435
Mass (Da):47,386
Last modified:June 13, 2006 - v1
Checksum:i05C2B6BCA4EF1267
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000259 Genomic DNA Translation: ABF31797.1
RefSeqiWP_002990448.1, NC_008021.1

Genome annotation databases

EnsemblBacteriaiABF31797; ABF31797; MGAS9429_Spy0609
KEGGispk:MGAS9429_Spy0609

Similar proteinsi

Entry informationi

Entry nameiENO_STRPC
AccessioniPrimary (citable) accession number: Q1JML5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 13, 2006
Last modified: April 25, 2018
This is version 90 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

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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