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Protein

Enolase

Gene

eno

Organism
Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Status
Reviewed-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

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. no protein annotated in this organism
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. no protein annotated in this organism
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 sitei154SubstrateUniRule annotation1
Binding sitei163SubstrateUniRule annotation1
Active sitei204Proton donorUniRule annotation1
Metal bindingi241MagnesiumUniRule annotation1
Metal bindingi288MagnesiumUniRule annotation1
Binding sitei288SubstrateUniRule annotation1
Metal bindingi315MagnesiumUniRule annotation1
Binding sitei315SubstrateUniRule annotation1
Active sitei340Proton acceptorUniRule annotation1
Binding sitei340Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei391SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processGlycolysis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciPGIN431947:G1G2V-1954-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:PGN_1743
OrganismiPorphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Taxonomic identifieri431947 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas
Proteomesi

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_10001158971 – 425EnolaseAdd BLAST425

Proteomic databases

PRIDEiB2RLL7

Interactioni

Protein-protein interaction databases

STRINGi431947.PGN_1743

Structurei

3D structure databases

ProteinModelPortaliB2RLL7
SMRiB2RLL7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni367 – 370Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C70 Bacteria
COG0148 LUCA
HOGENOMiHOG000072174
KOiK01689
OMAiEFMIIPV

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
IPR036849 Enolase-like_C_sf
IPR029017 Enolase-like_N
IPR034390 Enolase-like_superfamily
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
SFLDS00001 Enolase, 1 hit
SMARTiView protein in SMART
SM01192 Enolase_C, 1 hit
SM01193 Enolase_N, 1 hit
SUPFAMiSSF51604 SSF51604, 1 hit
TIGRFAMsiTIGR01060 eno, 1 hit
PROSITEiView protein in PROSITE
PS00164 ENOLASE, 1 hit

Sequencei

Sequence statusi: Complete.

B2RLL7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIVKIIGRE ILDSRGNPTV EVDVHLACGI IGRAAVPSGA STGENEAIEL
60 70 80 90 100
RDQDKARYCG KGVLKAVKNV NEVIDPALCG MSVLEQTAID RKLIELDGTK
110 120 130 140 150
TKSNLGANAM LGVSLAVAKA AAAYLDIPLY RYIGGSNTYV LPVPMMNIIN
160 170 180 190 200
GGSHSDAPIA FQEFMIRPVG ACCFREGLRM GAEVFHALKK VLHDRGLSTA
210 220 230 240 250
VGDEGGFAPA LNGTEDAIES ILKAVEAAGY VPGKDITIAM DCASSEFFKD
260 270 280 290 300
GIYDYTKFEG EKGKKRSIDE QVAYLTELVG KYPIDSIEDG MSENDWEGWK
310 320 330 340 350
KLTVALGDKV QLVGDDLFVT NVEFLRRGIA EKCGNSILIK VNQIGTLTET
360 370 380 390 400
LNAIEMAHRH GFTSVTSHRS GETEDTTIAD IAVATNSGQI KTGSLSRTDR
410 420
MAKYNQLLRI EEELGPCAVY GYKKV
Length:425
Mass (Da):45,849
Last modified:July 1, 2008 - v1
Checksum:iDA87A09725858676
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009380 Genomic DNA Translation: BAG34262.1
RefSeqiWP_012458500.1, NZ_CP025930.1

Genome annotation databases

EnsemblBacteriaiBAG34262; BAG34262; PGN_1743
GeneIDi29256903
KEGGipgn:PGN_1743

Similar proteinsi

Entry informationi

Entry nameiENO_PORG3
AccessioniPrimary (citable) accession number: B2RLL7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: May 23, 2018
This is version 65 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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