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Protein

Enolase

Gene

eno

Organism
Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15)
Status
Reviewed-Annotation score: Annotation score: 3 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

Pathway:iglycolysis

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-independent phosphoglycerate mutase (gpmI)
  4. Enolase (eno)
  5. Pyruvate kinase (Exig_2211)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei155 – 1551SubstrateUniRule annotation
Binding sitei164 – 1641SubstrateUniRule annotation
Active sitei205 – 2051Proton donorUniRule annotation
Metal bindingi242 – 2421MagnesiumUniRule annotation
Metal bindingi287 – 2871MagnesiumUniRule annotation
Binding sitei287 – 2871SubstrateUniRule annotation
Metal bindingi314 – 3141MagnesiumUniRule annotation
Binding sitei314 – 3141SubstrateUniRule annotation
Active sitei339 – 3391Proton acceptorUniRule annotation
Binding sitei339 – 3391Substrate (covalent); in inhibited formUniRule annotation
Binding sitei390 – 3901SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciESIB262543:GHBP-2474-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:Exig_2393
OrganismiExiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15)
Taxonomic identifieri262543 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillales Family XII. Incertae SedisExiguobacterium
ProteomesiUP000001681 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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430EnolasePRO_1000115864Add
BLAST

Proteomic databases

PRIDEiB1YLD8.

Interactioni

Protein-protein interaction databases

STRINGi262543.Exig_2393.

Structurei

3D structure databases

ProteinModelPortaliB1YLD8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni366 – 3694Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0148.
HOGENOMiHOG000072173.
KOiK01689.
OMAiEFMIIPV.
OrthoDBiEOG65J589.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B1YLD8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMITEIYAR EILDSRGNPT VEVEVYTEDG GFGRALVPSG ASTGEHEAVE
60 70 80 90 100
LRDGDKSRYL GKGVLKAVDN VNEKLAPEII GYDVFDQAGI DKKMIDLDGT
110 120 130 140 150
KNKGNFGANA ILGISMAAAR AAADELGLPL YTYLGGFNAK TLPTPMMNII
160 170 180 190 200
NGGSHADNNV DFQEFMIMPV GAPTFKEALR MGAEIFHALK SVLSGMGLNT
210 220 230 240 250
AVGDEGGFAP NLKSNEEAIT VILEAIEKAG YKAGEDVYLA MDVASSEFYD
260 270 280 290 300
KAAGKYNLAG EGKVLSTEEL VEFYAQLVDK YPIISIEDGC DENDWDGHKL
310 320 330 340 350
LTDRIGHKVQ LVGDDLFVTN TEKLAEGIEK GIANSILIKV NQIGTLTETF
360 370 380 390 400
DAIEMAKKAG YTAVVSHRSG ETEDSTIADI AVATNAGQIK TGSLSRTDRI
410 420 430
AKYNQLLRIE DMLSDVAVYD GIKSFYNLKK
Length:430
Mass (Da):46,328
Last modified:May 20, 2008 - v1
Checksum:iD332A59301988103
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001022 Genomic DNA. Translation: ACB61843.1.
RefSeqiWP_012371259.1. NC_010556.1.

Genome annotation databases

EnsemblBacteriaiACB61843; ACB61843; Exig_2393.
KEGGiesi:Exig_2393.
PATRICi32138418. VBIExiSib53410_2431.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001022 Genomic DNA. Translation: ACB61843.1.
RefSeqiWP_012371259.1. NC_010556.1.

3D structure databases

ProteinModelPortaliB1YLD8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262543.Exig_2393.

Proteomic databases

PRIDEiB1YLD8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACB61843; ACB61843; Exig_2393.
KEGGiesi:Exig_2393.
PATRICi32138418. VBIExiSib53410_2431.

Phylogenomic databases

eggNOGiCOG0148.
HOGENOMiHOG000072173.
KOiK01689.
OMAiEFMIIPV.
OrthoDBiEOG65J589.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BioCyciESIB262543:GHBP-2474-MONOMER.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 17290 / JCM 13490 / 255-15.

Entry informationi

Entry nameiENO_EXIS2
AccessioniPrimary (citable) accession number: B1YLD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: July 22, 2015
This is version 48 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

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 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.