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Protein

Enolase

Gene

eno

Organism
Methanosaeta thermophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT) (Methanothrix thermophila)
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

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-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (apgM), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. no protein annotated in this organism
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 sitei206Proton donorUniRule annotation1
Metal bindingi241MagnesiumUniRule annotation1
Metal bindingi282MagnesiumUniRule annotation1
Binding sitei282SubstrateUniRule annotation1
Metal bindingi308MagnesiumUniRule annotation1
Binding sitei308SubstrateUniRule annotation1
Active sitei333Proton acceptorUniRule annotation1
Binding sitei333Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei384SubstrateUniRule 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:Mthe_0833
OrganismiMethanosaeta thermophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT) (Methanothrix thermophila)
Taxonomic identifieri349307 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosaetaceaeMethanosaeta
Proteomesi
  • UP000000674 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_00002808821 – 420EnolaseAdd BLAST420

Proteomic databases

PRIDEiA0B7E8.

Interactioni

Protein-protein interaction databases

STRINGi349307.Mthe_0833.

Structurei

3D structure databases

ProteinModelPortaliA0B7E8.
SMRiA0B7E8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni360 – 363Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01169. Archaea.
COG0148. LUCA.
HOGENOMiHOG000072173.
KOiK01689.
OMAiEFMIIPV.
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.

A0B7E8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLEIEKIHA REILDSRGNP TVEVDVWTCC GFGRAAVPSG ASTGTYEALE
60 70 80 90 100
LRDGGDRYDG KGVLKAVRNV NEVIGPKLIG MDVIDQRGVD QIMIEMDGTP
110 120 130 140 150
NKSNLGANAI LGVSLAVAKA AASSLGMPLY RYLGGVSATR LPVPSLNVLN
160 170 180 190 200
GGKHAGNDLS IQEFMIEPWG ADSFSEALRM AAETYHALGR ILRGKYGNVA
210 220 230 240 250
TNVGFEGGYA PPISKTRDAL DAIMAALDVT GYTEEIKLGL DSAASSFYLD
260 270 280 290 300
GGYSVDDNRL SPGELIDFYV ELVKTYPIVL IEDPFEENAF EEFAELTKKL
310 320 330 340 350
PDTIIVGDDL YVTNMARIEK GIRMRSTNAL LLKLNQIGTV SEAFDAATLA
360 370 380 390 400
YRNSFKVMVS HRSAETEDSA LADVSVAIGA ELIKTGAPAR SERNAKYNQL
410 420
LRIQEALGSS ASYAGRRRWS
Length:420
Mass (Da):45,276
Last modified:November 28, 2006 - v1
Checksum:i25692E4F80FCD7BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000477 Genomic DNA. Translation: ABK14622.1.

Genome annotation databases

EnsemblBacteriaiABK14622; ABK14622; Mthe_0833.
KEGGimtp:Mthe_0833.

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 nameiENO_METTP
AccessioniPrimary (citable) accession number: A0B7E8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: November 28, 2006
Last modified: June 7, 2017
This is version 72 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