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Protein

Enolase

Gene
N/A
Organism
Clostridioides difficile (Peptoclostridium difficile)
Status
Reviewed-Annotation score: Annotation score: 3 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 (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), Phosphoglycerate kinase (pgk), 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), 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), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
  4. Enolase, Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno)
  5. Pyruvate kinase (pyk), Pyruvate kinase (pyk), Pyruvate kinase (pyk), Pyruvate kinase (pyk), Pyruvate kinase (IM33_18340), Pyruvate kinase (pyk), Pyruvate kinase (pyk), Pyruvate kinase (pyk), Pyruvate kinase (pyk), Pyruvate kinase (pyk), 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

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
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
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.

Cross-referencesi

Sequence databases

PIRiA61009.

3D structure databases

ProteinModelPortaliQ7M0V7.
SMRiQ7M0V7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
InterProiView protein in InterPro
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
PfamiView protein in Pfam
PF00113. Enolase_C. 1 hit.
SUPFAMiSSF51604. SSF51604. 1 hit.
ProtoNetiSearch...

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 10, 2017
This is version 57 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.