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Protein

Enolase 2

Gene

eno2

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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. Glyceraldehyde-3-phosphate dehydrogenase (gap)
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
  4. Enolase 2 (eno2), Enolase 1 (eno1)
  5. Pyruvate kinase (SCO5423), Pyruvate kinase (SCO2014)
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 sitei163SubstrateUniRule annotation1
Binding sitei172SubstrateUniRule annotation1
Active sitei213Proton donorUniRule annotation1
Metal bindingi250MagnesiumUniRule annotation1
Metal bindingi293MagnesiumUniRule annotation1
Binding sitei293SubstrateUniRule annotation1
Metal bindingi320MagnesiumUniRule annotation1
Binding sitei320SubstrateUniRule annotation1
Active sitei345Proton acceptorUniRule annotation1
Binding sitei345Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei396SubstrateUniRule annotation1

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 2UniRule annotation (EC:4.2.1.11UniRule annotation)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase 2UniRule annotation
2-phosphoglycerate dehydratase 2UniRule annotation
Gene namesi
Name:eno2UniRule annotation
Ordered Locus Names:SCO7638
ORF Names:SC10F4.11c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 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_00001339771 – 434Enolase 2Add BLAST434

Proteomic databases

PRIDEiQ9F3P9.

Interactioni

Protein-protein interaction databases

STRINGi100226.SCO7638.

Structurei

3D structure databases

ProteinModelPortaliQ9F3P9.
SMRiQ9F3P9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni372 – 375Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0148. LUCA.
HOGENOMiHOG000072174.
InParanoidiQ9F3P9.
KOiK01689.
OMAiWHGKGVD.
OrthoDBiPOG091H02DK.
PhylomeDBiQ9F3P9.

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.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
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.
SMARTiView protein in SMART
SM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiView protein in PROSITE
PS00164. ENOLASE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9F3P9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSATAVEPAA AIETVTARRI IDSRGNPTVE VDVVLEDGSL GRAAVPSGAS
60 70 80 90 100
TGAREAVELR DEDPTRWHGK GVDRAVAHVN GEIAASVRGR DAADQAGLDA
110 120 130 140 150
ALIALDGTAA KSRLGANALL GVSLAAAKAA AAARRQPLYR YLGGADAHLL
160 170 180 190 200
PLPMMNIVNG GAHADNPLDF QEFMIVPVGA DTFAEAVRMG SEVFHTLRRD
210 220 230 240 250
LLAAGHSTGV GDEGGFAPAL RTAEEALDFV VAAIERTGYR AGPDIGLVMD
260 270 280 290 300
PASSEFFRDG GYDYAGEGVR RSPAEHADHL AGLIDAYPVV SIEDPMAEDD
310 320 330 340 350
LDGWRELTDR VGDRCQLTGD DVFCTDEALV REGIRTGVGN SVLVKVNQIG
360 370 380 390 400
TLTEALATVA TAHEAGWTVV MSHRSGETED TTIADLAVAT GCGQIKTGSL
410 420 430
SRSDRTAKYN RLIRIEEELG ASARFAGRSA LRRV
Length:434
Mass (Da):45,534
Last modified:March 1, 2001 - v1
Checksum:i435A1CC0629DC0A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939132 Genomic DNA. Translation: CAC16971.1.
RefSeqiNP_631678.1. NC_003888.3.
WP_011031794.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAC16971; CAC16971; CAC16971.
GeneIDi1103076.
KEGGisco:SCO7638.
PATRICi23745231. VBIStrCoe124346_7758.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939132 Genomic DNA. Translation: CAC16971.1.
RefSeqiNP_631678.1. NC_003888.3.
WP_011031794.1. NC_003888.3.

3D structure databases

ProteinModelPortaliQ9F3P9.
SMRiQ9F3P9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO7638.

Proteomic databases

PRIDEiQ9F3P9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC16971; CAC16971; CAC16971.
GeneIDi1103076.
KEGGisco:SCO7638.
PATRICi23745231. VBIStrCoe124346_7758.

Phylogenomic databases

eggNOGiCOG0148. LUCA.
HOGENOMiHOG000072174.
InParanoidiQ9F3P9.
KOiK01689.
OMAiWHGKGVD.
OrthoDBiPOG091H02DK.
PhylomeDBiQ9F3P9.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.

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.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
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.
SMARTiView protein in SMART
SM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiView protein in PROSITE
PS00164. ENOLASE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiENO2_STRCO
AccessioniPrimary (citable) accession number: Q9F3P9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: March 1, 2001
Last modified: March 15, 2017
This is version 105 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, Reference proteome

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.