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Protein

Enolase

Gene

eno

Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
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. Glyceraldehyde-3-phosphate dehydrogenase 1 (gapA), Glyceraldehyde-3-phosphate dehydrogenase 2 (gapB)
  2. Phosphoglycerate kinase 2 (pgk2), Phosphoglycerate kinase 1 (pgk1)
  3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2 (gpmI2), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1 (gpmI1), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (apgM)
  4. Enolase (eno)
  5. Pyruvate kinase (pyk)
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 sitei166SubstrateUniRule annotation1
Binding sitei175SubstrateUniRule annotation1
Active sitei218Proton donorUniRule annotation1
Metal bindingi254MagnesiumUniRule annotation1
Metal bindingi295MagnesiumUniRule annotation1
Binding sitei295SubstrateUniRule annotation1
Metal bindingi321MagnesiumUniRule annotation1
Binding sitei321SubstrateUniRule annotation1
Active sitei346Proton acceptorUniRule annotation1
Binding sitei346Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei397SubstrateUniRule 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:MA_1672
OrganismiMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Taxonomic identifieri188937 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
Proteomesi
  • UP000002487 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_00001340231 – 429EnolaseAdd BLAST429

Proteomic databases

PRIDEiQ8TQ79.

Interactioni

Protein-protein interaction databases

STRINGi188937.MA1672.

Structurei

3D structure databases

ProteinModelPortaliQ8TQ79.
SMRiQ8TQ79.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni373 – 376Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01169. Archaea.
COG0148. LUCA.
InParanoidiQ8TQ79.
KOiK01689.
OMAiEFMIIPV.
OrthoDBiPOG093Z03D9.
PhylomeDBiQ8TQ79.

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.

Q8TQ79-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMSYIGLQQD SGEYKIQKIH AREILDSRGN PTIEVDVFTP KGFGRASVPS
60 70 80 90 100
GASTGTNEAL ELRDADPNRY GGKGVLTAVK NVNTIIQKEL LGLDVRNQRE
110 120 130 140 150
IDELMIELDE TENKSNLGAN SILGVSMAVA KAAADSLNMP LYRYFGGSNA
160 170 180 190 200
FTLPVPTMNV LNGGKHAGNE LAIQEFMIQP KGAETFYEAL QIGAEIYHVL
210 220 230 240 250
GKYLEKKYGR SSTNVGYEGG YAPKMSESTE ALDALVQAIE EAGYTESEVT
260 270 280 290 300
IGLDAAATEF YEEEFYNIDG KKLAAPELLD YYVELVNSYP ILSIEDPFYE
310 320 330 340 350
EAFEDFEALT NELWDTIIVG DDLFVTNIER LSRGVDMGAA NALLLKVNQI
360 370 380 390 400
GSISEAFDAA SMASRNGYTV IVSHRSAETE DTTISDLAVA IGAEMIKTGA
410 420
PARGERTAKY NQLLRIEEDL GEVAHYVQL
Length:429
Mass (Da):46,875
Last modified:June 1, 2002 - v1
Checksum:iC5125FC71B24F248
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010299 Genomic DNA. Translation: AAM05080.1.

Genome annotation databases

EnsemblBacteriaiAAM05080; AAM05080; MA_1672.
KEGGimac:MA_1672.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010299 Genomic DNA. Translation: AAM05080.1.

3D structure databases

ProteinModelPortaliQ8TQ79.
SMRiQ8TQ79.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi188937.MA1672.

Proteomic databases

PRIDEiQ8TQ79.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM05080; AAM05080; MA_1672.
KEGGimac:MA_1672.

Phylogenomic databases

eggNOGiarCOG01169. Archaea.
COG0148. LUCA.
InParanoidiQ8TQ79.
KOiK01689.
OMAiEFMIIPV.
OrthoDBiPOG093Z03D9.
PhylomeDBiQ8TQ79.

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_METAC
AccessioniPrimary (citable) accession number: Q8TQ79
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 1, 2002
Last modified: April 12, 2017
This is version 108 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.