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Protein

Enolase

Gene

eno

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 3 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-independent phosphoglycerate mutase (apgM)
  4. Enolase (eno)
  5. Pyruvate kinase (PH0570)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei156 – 1561SubstrateUniRule annotation
Binding sitei165 – 1651SubstrateUniRule annotation
Active sitei208 – 2081Proton donorUniRule annotation
Metal bindingi245 – 2451MagnesiumUniRule annotation
Metal bindingi286 – 2861MagnesiumUniRule annotation
Binding sitei286 – 2861SubstrateUniRule annotation
Metal bindingi313 – 3131MagnesiumUniRule annotation
Binding sitei313 – 3131SubstrateUniRule annotation
Active sitei338 – 3381Proton acceptorUniRule annotation
Binding sitei338 – 3381Substrate (covalent); in inhibited formUniRule annotation
Binding sitei389 – 3891SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1949-MONOMER.
UniPathwayiUPA00109; UER00187.

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:PH1942
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428EnolasePRO_0000134032Add
BLAST

Proteomic databases

PRIDEiO59605.

Interactioni

Protein-protein interaction databases

STRINGi70601.PH1942.

Structurei

3D structure databases

ProteinModelPortaliO59605.
SMRiO59605. Positions 1-427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni365 – 3684Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01169. Archaea.
COG0148. LUCA.
HOGENOMiHOG000072173.
KOiK01689.
OMAiEFMIIPV.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase. 1 hit.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O59605-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENPYEITAI VAREILDSRG NPTVEVDVHT PIAMGRAAVP SGASTGTHEA
60 70 80 90 100
VELRDGGKRY HGKGVRRAVE NVNKIIAPEL IGMDVRWQRE IDKLLIELDG
110 120 130 140 150
TENKSNLGAN AILAVSLAVA KAAANSLELP LYQYLGGVNA YVLPVPLSNV
160 170 180 190 200
INGGVHAGNE LDFQEFMIMP IGASSFREAI RWVSETYHVL KRVIMGKYGK
210 220 230 240 250
NAVNVGDEGG FAPPMKEVTE PLDALIKAIE EAGYKPGDEI ALAIDAASSE
260 270 280 290 300
FFKDGKYIVG GKEYTREELL DLYKELVSTY PIVSIEDPFH EEDWEGFVMI
310 320 330 340 350
TNELGKKIQI VGDDLFVTNP RRLKKGIELG AANALLLKVN QIGTLTEAMD
360 370 380 390 400
AAYTAFRAGY SVIVSHRSGE TEDTTIADLA VALNAGQIKT GAPARSDRNA
410 420
KYNQLIRIEE ELEGIAVYAG KNFRKVFF
Length:428
Mass (Da):46,697
Last modified:August 1, 1998 - v1
Checksum:iBA91C397DBEAAC02
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA31069.1.
PIRiF71209.
RefSeqiWP_010886009.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA31069; BAA31069; BAA31069.
GeneIDi1442791.
KEGGipho:PH1942.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA31069.1.
PIRiF71209.
RefSeqiWP_010886009.1. NC_000961.1.

3D structure databases

ProteinModelPortaliO59605.
SMRiO59605. Positions 1-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH1942.

Proteomic databases

PRIDEiO59605.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA31069; BAA31069; BAA31069.
GeneIDi1442791.
KEGGipho:PH1942.

Phylogenomic databases

eggNOGiarCOG01169. Archaea.
COG0148. LUCA.
HOGENOMiHOG000072173.
KOiK01689.
OMAiEFMIIPV.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BioCyciPHOR70601:GJWR-1949-MONOMER.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase. 1 hit.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiENO_PYRHO
AccessioniPrimary (citable) accession number: O59605
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 1, 1998
Last modified: May 11, 2016
This is version 108 of the entry and version 1 of the sequence. [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

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.