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Protein

Enolase

Gene

eno

Organism
Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)
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. Glyceraldehyde-3-phosphate dehydrogenase (gap)
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (apgM), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. Pyruvate kinase (Mevan_0916)
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 sitei157SubstrateUniRule annotation1
Binding sitei166SubstrateUniRule annotation1
Active sitei209Proton donorUniRule annotation1
Metal bindingi244MagnesiumUniRule annotation1
Metal bindingi287MagnesiumUniRule annotation1
Binding sitei287SubstrateUniRule annotation1
Metal bindingi313MagnesiumUniRule annotation1
Binding sitei313SubstrateUniRule annotation1
Active sitei338Proton acceptorUniRule annotation1
Binding sitei338Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei389SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processGlycolysis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

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:Mevan_1383
OrganismiMethanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)
Taxonomic identifieri406327 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
Proteomesi
  • UP000001107 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_00003376251 – 426EnolaseAdd BLAST426

Proteomic databases

PRIDEiA6US08.

Interactioni

Protein-protein interaction databases

STRINGi406327.Mevan_1383.

Structurei

3D structure databases

ProteinModelPortaliA6US08.
SMRiA6US08.
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

eggNOGiarCOG01169. Archaea.
COG0148. LUCA.
HOGENOMiHOG000072174.
KOiK01689.
OrthoDBiPOG093Z03D9.

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.

A6US08-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNSFDIYEI KARQVLDSRG NPTIEAEVLT AGRGYGHAIV PSGASTGTFE
60 70 80 90 100
AVELRDLGKK YGGKGVLNAV GNVNEIIAPE LIGEDSRNQR LIDNIMINLD
110 120 130 140 150
GTENKANLGA NAILAVSMAV ARAAADTSSL PLYKYLGGCN SYIMPVPMMN
160 170 180 190 200
VLNGGKHAGN ALDFQEFMIM PIGADSFSDA VRMCAETYQS LKKVISEKYG
210 220 230 240 250
KDAVNIGDEG GFAPPVKTID EAFSVLLEGV KRAGYENEIV FTLDSAASEF
260 270 280 290 300
YDEKTNSYVV LGESLSTDKL IEIYKDMVSK YPIVSIEDPL FEGDFEGFKE
310 320 330 340 350
ITKELKGIQI IGDDIFVTNT NRLKKGIEMN AANALLLKVN QIGTISESID
360 370 380 390 400
AANLASRNGY GVIVSHRSGE TEDSIISDLT VALNSGQIKT GAPARGERTA
410 420
KYNQLIRIEE ELQISKYAGK NFKIPF
Length:426
Mass (Da):46,118
Last modified:May 20, 2008 - v2
Checksum:i5E584AE497DA3AE7
GO

Sequence cautioni

The sequence ABR55280 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000742 Genomic DNA. Translation: ABR55280.1. Different initiation.
RefSeqiWP_012066194.1. NC_009634.1.

Genome annotation databases

EnsemblBacteriaiABR55280; ABR55280; Mevan_1383.
GeneIDi5324765.
KEGGimvn:Mevan_1383.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000742 Genomic DNA. Translation: ABR55280.1. Different initiation.
RefSeqiWP_012066194.1. NC_009634.1.

3D structure databases

ProteinModelPortaliA6US08.
SMRiA6US08.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi406327.Mevan_1383.

Proteomic databases

PRIDEiA6US08.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABR55280; ABR55280; Mevan_1383.
GeneIDi5324765.
KEGGimvn:Mevan_1383.

Phylogenomic databases

eggNOGiarCOG01169. Archaea.
COG0148. LUCA.
HOGENOMiHOG000072174.
KOiK01689.
OrthoDBiPOG093Z03D9.

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 nameiENO_METVS
AccessioniPrimary (citable) accession number: A6US08
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: May 10, 2017
This is version 65 of the entry and version 2 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

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.