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Protein

Enolase 1

Gene

eno1

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 sitei155SubstrateUniRule annotation1
Binding sitei164SubstrateUniRule annotation1
Active sitei205Proton donorUniRule annotation1
Metal bindingi242MagnesiumUniRule annotation1
Metal bindingi287MagnesiumUniRule annotation1
Binding sitei287SubstrateUniRule annotation1
Metal bindingi314MagnesiumUniRule annotation1
Binding sitei314SubstrateUniRule annotation1
Active sitei339Proton acceptorUniRule annotation1
Binding sitei339Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei390SubstrateUniRule 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 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:LJ_0875
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_00001339011 – 432Enolase 1Add BLAST432

Proteomic databases

PRIDEiQ74K78.

Interactioni

GO - Molecular functioni

  • laminin binding Source: CAFA

Protein-protein interaction databases

STRINGi257314.LJ0875.

Structurei

3D structure databases

ProteinModelPortaliQ74K78.
SMRiQ74K78.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni366 – 369Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.
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.
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.

Q74K78-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVITDIHAR EVLDSRGNPT VEAEVYTELG GFGRAIVPSG ASTGEHEAVE
60 70 80 90 100
LRDGDKSRFL GQGVLTAVEN VNGEIAKAVI GLDVTDQRLI DQTMIDLDGT
110 120 130 140 150
PNKGRLGANA MLAVSLASAR AAADELGLPL YEYLGGPNAH VLPTPMMNVI
160 170 180 190 200
NGGKHADNNV DIQEFMIMPV GAKSLHEAVR MGAETFHTLK SLLQERGEST
210 220 230 240 250
AVGDEGGFAP NLKNNEEPFE ILVEAIQRAG YKPGQDISIA FDCAASEFYN
260 270 280 290 300
KDTKKYVTVA DGREYTAEEW TSLMEDIVDK YPVISIEDPL DENDWEGWKV
310 320 330 340 350
FTERLGDKVQ IVGDDLFVTN TNYLEKGIKM GVANSILIKL NQIGTLTETF
360 370 380 390 400
EAIEMAKEAG YTAVVSHRSG ETEDTTIADL VVATNAGQIK TGSMSRTDRI
410 420 430
AKYNQLMRIE EALGSTAQYK GIHSFYNLHK QF
Length:432
Mass (Da):47,072
Last modified:July 5, 2004 - v1
Checksum:i48F322BE095258C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017198 Genomic DNA. Translation: AAS08696.1.
RefSeqiWP_004897701.1. NC_005362.1.

Genome annotation databases

EnsemblBacteriaiAAS08696; AAS08696; LJ_0875.
KEGGiljo:LJ_0875.

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_LACJO
AccessioniPrimary (citable) accession number: Q74K78
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: July 5, 2004
Last modified: June 7, 2017
This is version 94 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