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Protein

Enolase

Gene
N/A
Organism
Clostridioides difficile (Peptoclostridium difficile)
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 (By similarity).By similarity

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.By similarity

Cofactori

Mg2+By similarityNote: Mg2+ is required for catalysis and for stabilizing the dimer.By similarity

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.By similarity

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
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), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
  4. Enolase (eno), Enolase (eno), Enolase, Enolase (eno)
  5. Pyruvate kinase (pyk), Pyruvate kinase (pyk), Pyruvate kinase (IM33_18340), 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
Active sitei25Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processGlycolysis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187

Names & Taxonomyi

Protein namesi
Recommended name:
Enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase
OrganismiClostridioides difficile (Peptoclostridium difficile)
Taxonomic identifieri1496 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceaeClostridioides

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 bacterial cell surface (By similarity).By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000284772‹1 – ›57EnolaseAdd BLAST›57

Proteomic databases

PRIDEiQ7M0V7

Structurei

3D structure databases

ProteinModelPortaliQ7M0V7
SMRiQ7M0V7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni46 – ›48Substrate bindingBy similarity›3

Sequence similaritiesi

Belongs to the enolase family.Sequence analysis

Family and domain databases

Gene3Di3.20.20.120, 1 hit
InterProiView protein in InterPro
IPR036849 Enolase-like_C_sf
IPR020810 Enolase_C
PfamiView protein in Pfam
PF00113 Enolase_C, 1 hit
SUPFAMiSSF51604 SSF51604, 1 hit

Sequencei

Sequence statusi: Fragments.

Q7M0V7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAEVFHSLK KVLGEKGLAS GVGDEGGFAP NLGSNIRRAG YTAVISHRVA

KYNQLLR
Length:57
Mass (Da):6,042
Last modified:December 15, 2003 - v1
Checksum:i9CB0C9F1E449E6A0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11 Publication1
Non-adjacent residuesi38 – 391 Publication2
Non-adjacent residuesi48 – 491 Publication2
Non-terminal residuei57Imported1

Sequence databases

PIRiA61009

Entry informationi

Entry nameiENO_CLODI
AccessioniPrimary (citable) accession number: Q7M0V7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: December 15, 2003
Last modified: May 23, 2018
This is version 61 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

Direct protein sequencing

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