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Protein

Enolase 3

Gene

eno3

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 bindingi286MagnesiumUniRule annotation1
Binding sitei286SubstrateUniRule annotation1
Metal bindingi313MagnesiumUniRule annotation1
Binding sitei313SubstrateUniRule annotation1
Active sitei338Proton acceptorUniRule annotation1
Binding sitei338Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei389SubstrateUniRule 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 3UniRule annotation (EC:4.2.1.11UniRule annotation)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase 3UniRule annotation
2-phosphoglycerate dehydratase 3UniRule annotation
Gene namesi
Name:eno3UniRule annotation
Ordered Locus Names:LJ_1416
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_00001339031 – 428Enolase 3Add BLAST428

Interactioni

GO - Molecular functioni

  • laminin binding Source: CAFA

Protein-protein interaction databases

STRINGi257314.LJ1416.

Structurei

3D structure databases

ProteinModelPortaliQ74IV0.
SMRiQ74IV0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni365 – 368Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0148. LUCA.
KOiK01689.
OMAiFKDAMRI.

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.

Q74IV0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKSVIENVH ALEIFDSRGN PTVEVFVTLS NGVVGKAEVP SGASTGENEA
60 70 80 90 100
VELRDGGSRL GGKGVMNAVN NVNTEINDAL KGLDPHDQPN IDATMIALDG
110 120 130 140 150
TPNKGRLGAN AILGVSMATA AAAAKDNHQP LYRYLGGTDL EMPQTFHNVI
160 170 180 190 200
NGGEHADNGI DIQEFMITPV AKTSFRDGFE KIVNVYHTLK KVLEDMGYET
210 220 230 240 250
GLGDEGGFAP NMKNSEEALK ALHESIIKAG YKPGEDIAIA CDCAASYFYN
260 270 280 290 300
KEDGKYHLEG KVLTDEELAD YYDKLLDEFP ELISMEDPYD ENDVEGMVKF
310 320 330 340 350
TQSHKDRIQI VLDDFICTNP KLLNKAIHEG AGNASLIKLN QIGTVTETLE
360 370 380 390 400
TIRLSRKNGY NTMISHRSGE TGDTFIADFA VAVNGGQLKT GAPARSERVE
410 420
KYNRLLEIEE ELGKGERLAF FPDNVDLD
Length:428
Mass (Da):46,633
Last modified:July 5, 2004 - v1
Checksum:i4FBDCFED4CE39049
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017198 Genomic DNA. Translation: AAS09182.1.
RefSeqiWP_004897160.1. NC_005362.1.

Genome annotation databases

EnsemblBacteriaiAAS09182; AAS09182; LJ_1416.
GeneIDi2743679.
KEGGiljo:LJ_1416.
PATRICi22239105. VBILacJoh1832_1230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017198 Genomic DNA. Translation: AAS09182.1.
RefSeqiWP_004897160.1. NC_005362.1.

3D structure databases

ProteinModelPortaliQ74IV0.
SMRiQ74IV0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi257314.LJ1416.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS09182; AAS09182; LJ_1416.
GeneIDi2743679.
KEGGiljo:LJ_1416.
PATRICi22239105. VBILacJoh1832_1230.

Phylogenomic databases

eggNOGiCOG0148. LUCA.
KOiK01689.
OMAiFKDAMRI.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.

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.
ProtoNetiSearch...

Entry informationi

Entry nameiENO3_LACJO
AccessioniPrimary (citable) accession number: Q74IV0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: July 5, 2004
Last modified: May 10, 2017
This is version 92 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

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.