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Protein

Enolase

Gene

eno

Organism
Pyrobaculum calidifontis (strain JCM 11548 / VA1)
Status
Unreviewed-Annotation score: -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

Activity 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 (Pcal_0029)
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 sitei145SubstrateUniRule annotation1
Binding sitei155SubstrateUniRule annotation1
Active sitei198Proton donorUniRule annotation1
Metal bindingi234MagnesiumUniRule annotation1
Metal bindingi277MagnesiumUniRule annotation1
Binding sitei277SubstrateUniRule annotation1
Metal bindingi303MagnesiumUniRule annotation1
Binding sitei303SubstrateUniRule annotation1
Active sitei328Proton acceptorUniRule annotation1
Binding sitei328Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei379SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyaseUniRule annotationImported
Biological processGlycolysisUniRule annotation
LigandMagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

UniPathwayi
UPA00109;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:Pcal_0022Imported
OrganismiPyrobaculum calidifontis (strain JCM 11548 / VA1)Imported
Taxonomic identifieri410359 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
Proteomesi
  • UP000001431 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

CytoplasmUniRule annotation, SecretedUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi410359.Pcal_0022

Structurei

3D structure databases

ProteinModelPortaliA3MS45
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 124Enolase_NInterPro annotationAdd BLAST122
Domaini129 – 411Enolase_CInterPro annotationAdd BLAST283

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni355 – 358Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01169 Archaea
COG0148 LUCA
HOGENOMiHOG000072173
KOiK01689
OMAiQEFLVVP
OrthoDBiPOG093Z03D9

Family and domain databases

Gene3Di3.20.20.120, 1 hit
3.30.390.10, 1 hit
HAMAPiMF_00318 Enolase, 1 hit
InterProiView protein in InterPro
IPR000941 Enolase
IPR036849 Enolase-like_C_sf
IPR029017 Enolase-like_N
IPR020810 Enolase_C
IPR020809 Enolase_CS
IPR020811 Enolase_N
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
PROSITEiView protein in PROSITE
PS00164 ENOLASE, 1 hit

Sequencei

Sequence statusi: Complete.

A3MS45-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEIKDVAIRK IFTGRGDLTV EVEVATEDFV AKAAAPAGAS RGANEVVYFP
60 70 80 90 100
EEGIDAAIAA FERLVAPEVV GLDVSEPYVV DGKLEEVDGT ARFERIGGAV
110 120 130 140 150
AIATSFASAE AGAASLGLPL FSFIGGAYAR RLPLPLGNVI GGGKHSRGLG
160 170 180 190 200
PDIQEFLAIP LNPPDIFTAI YTNVEIHKRA LKGILKVDAS FTGGKNDEGA
210 220 230 240 250
WTPRISSRTA LRILKETAEE VGKEVGVEVG IGVDVAASSL WNGERYVYKN
260 270 280 290 300
EGVERGPREQ LEFIAKLIEE FDLVYVEDPF HEEDFQSFAE LTDRFRDRLI
310 320 330 340 350
VGDDLFVTNP DRIRHGGRLK AATGVIIKPD QIGTLLRAHT AVSTAREYGL
360 370 380 390 400
KIVVSHRSGD TEYKTLAHVA VGFGAEVIKT GIMGGERTAK LNELIRIGEY
410
LGRWGNISRI R
Length:411
Mass (Da):44,460
Last modified:April 3, 2007 - v1
Checksum:iC785F015F85C33BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000561 Genomic DNA Translation: ABO07462.1

Genome annotation databases

EnsemblBacteriaiABO07462; ABO07462; Pcal_0022
KEGGipcl:Pcal_0022

Similar proteinsi

Entry informationi

Entry nameiA3MS45_PYRCJ
AccessioniPrimary (citable) accession number: A3MS45
Entry historyiIntegrated into UniProtKB/TrEMBL: April 3, 2007
Last sequence update: April 3, 2007
Last modified: September 12, 2018
This is version 78 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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