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Protein

Enolase 1

Gene

eno1

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 sitei155SubstrateUniRule annotation1
Binding sitei164SubstrateUniRule annotation1
Active sitei205Proton donorUniRule annotation1
Metal bindingi242MagnesiumUniRule annotation1
Metal bindingi283MagnesiumUniRule annotation1
Binding sitei283SubstrateUniRule annotation1
Metal bindingi310MagnesiumUniRule annotation1
Binding sitei310SubstrateUniRule annotation1
Active sitei335Proton acceptorUniRule annotation1
Binding sitei335Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei386SubstrateUniRule 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 1UniRule annotation (EC:4.2.1.11UniRule annotation)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase 1UniRule annotation
2-phosphoglycerate dehydratase 1UniRule annotation
Gene namesi
Name:eno1UniRule annotation
Ordered Locus Names:SCO3096
ORF Names:SCE41.05c
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_00001339761 – 426Enolase 1Add BLAST426

Proteomic databases

PRIDEiQ9F2Q3.

Interactioni

Protein-protein interaction databases

STRINGi100226.SCO3096.

Structurei

3D structure databases

ProteinModelPortaliQ9F2Q3.
SMRiQ9F2Q3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni362 – 365Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.
HOGENOMiHOG000072174.
InParanoidiQ9F2Q3.
KOiK01689.
OMAiEFMIIPV.
OrthoDBiPOG091H02DK.
PhylomeDBiQ9F2Q3.

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.
IPR034390. Enolase-like_superfamily.
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.
SFLDS00001. 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.

Q9F2Q3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSIDVVVAR EILDSRGNPT VEVEVGLDDG STGRAAVPSG ASTGAFEAIE
60 70 80 90 100
LRDGDPSRYL GKGVEKAVLA VIEQIGPELV GYDATEQRLI DQAMFDLDAT
110 120 130 140 150
DNKGSLGANA ILGVSLAVAH AASEASDLPL FRYLGGPNAH LLPVPMMNIL
160 170 180 190 200
NGGSHADSNV DIQEFMIAPI GAESFSEALR WGAEVYHTLK KVLKNKGLAT
210 220 230 240 250
GLGDEGGFAP NLGSNREALD LILEAIKEAG YTPGEQIALA LDVAASEFYK
260 270 280 290 300
DGSYAFEGKN RSAAEMTEYY AELVEAYPLV SIEDPLFEDD WDGWNTITAK
310 320 330 340 350
LGDKVQLVGD DLFVTNPERL ARGIEENSAN ALLVKVNQIG SLTETLDAVE
360 370 380 390 400
LAQRNGFKCM MSHRSGETED VTIADLAVAT NCGQIKTGAP ARSERVAKYN
410 420
QLLRIEEILD DAAVYAGRSA FPRFKG
Length:426
Mass (Da):45,483
Last modified:March 1, 2001 - v1
Checksum:i63AED7B7A4E15001
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939115 Genomic DNA. Translation: CAC09537.1.
RefSeqiNP_627314.1. NC_003888.3.
WP_003975715.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAC09537; CAC09537; CAC09537.
GeneIDi1098530.
29662158.
KEGGisco:SCO3096.
PATRICifig|100226.15.peg.3158.

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.

Entry informationi

Entry nameiENO1_STRCO
AccessioniPrimary (citable) accession number: Q9F2Q3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: March 1, 2001
Last modified: June 7, 2017
This is version 107 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