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Protein

Enolase 2

Gene

eno2

Organism
Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533)
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. no protein annotated in this organism
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1 (gpmA1), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2 (gpmA2)
  4. Enolase 2 (eno2), Enolase 1 (eno1), Enolase 3 (eno3)
  5. Pyruvate kinase (LJ_1080)
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 bindingi285MagnesiumUniRule annotation1
Binding sitei285SubstrateUniRule annotation1
Metal bindingi312MagnesiumUniRule annotation1
Binding sitei312SubstrateUniRule annotation1
Active sitei337Proton acceptorUniRule annotation1
Binding sitei337Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei388SubstrateUniRule annotation1

GO - Molecular functioni

  • laminin binding Source: CAFA
  • magnesium ion binding Source: InterPro
  • phosphopyruvate hydratase activity Source: UniProtKB-EC

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:LJ_1246
OrganismiLactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533)
Taxonomic identifieri257314 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
Proteomesi
  • UP000000581 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_00001339021 – 428Enolase 2Add BLAST428

Interactioni

GO - Molecular functioni

  • laminin binding Source: CAFA

Protein-protein interaction databases

STRINGi257314.LJ1246.

Structurei

3D structure databases

ProteinModelPortaliQ74J64.
SMRiQ74J64.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni364 – 367Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0148. LUCA.
KOiK01689.
OMAiAEERACN.

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.

Q74J64-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVYVEKVRA LEIFDSRGNP TVEVHAYLSD GTVAKAEVPS GASTGEKEAV
60 70 80 90 100
ELRDGGNRLQ GKGVTQAVTN VNGPINDALK GLSPYNQAEI DRTMIKLDGT
110 120 130 140 150
LNKAKLGANA ILGTSMAIAR AAARSKDEPL YRYLGGCELE MPQTFHNVIN
160 170 180 190 200
GGKHADNGID IQEFMITPVA KNSFRDGFEK IVNTYHALKA VIEEAGFETG
210 220 230 240 250
LGDEGGFAPN LNSSEEALKM LRKAIIKAGY KPRKDIAIAF DAAASSFYNT
260 270 280 290 300
EDGKYHFEGH IWNGEEMLQY YDKLLKEFPE IISCEDPFDE NDWENFEKFT
310 320 330 340 350
AKFGSTHQVV ADDNVCTNPK LVRKAIKDKL CNSILIKLNQ IGTITETLET
360 370 380 390 400
IRLARKNNMT TMVSHRSGET GDTFIADFTV ATNAGQLKSG APARSERVEK
410 420
YNRLLEIENQ IGVENERLNH FPNNVDFD
Length:428
Mass (Da):47,269
Last modified:July 5, 2004 - v1
Checksum:i7521EB6D22E689D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017198 Genomic DNA. Translation: AAS09067.1.
RefSeqiWP_011162075.1. NC_005362.1.

Genome annotation databases

EnsemblBacteriaiAAS09067; AAS09067; LJ_1246.
KEGGiljo:LJ_1246.
PATRICifig|257314.6.peg.1112.

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 nameiENO2_LACJO
AccessioniPrimary (citable) accession number: Q74J64
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: July 5, 2004
Last modified: June 7, 2017
This is version 91 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