Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Enolase

Gene

eno

Organism
Methanococcus maripaludis (strain C5 / ATCC BAA-1333)
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)
  4. Enolase (eno)
  5. Pyruvate kinase (MmarC5_1803)
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:MmarC5_1242
OrganismiMethanococcus maripaludis (strain C5 / ATCC BAA-1333)
Taxonomic identifieri402880 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
Proteomesi
  • UP000000253 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_00003376231 – 426EnolaseAdd BLAST426

Proteomic databases

PRIDEiA4FZA6.

Interactioni

Protein-protein interaction databases

STRINGi402880.MmarC5_1242.

Structurei

3D structure databases

ProteinModelPortaliA4FZA6.
SMRiA4FZA6.
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.

A4FZA6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDSFDIYEI KARQVLDSRG NPTVEAEVLT AGGGYGHTIV PSGASTGTFE
60 70 80 90 100
AVELRDATEK YGGKSVLNAV SNVNDIIAQE LIGEDARNQR LIDQIMINLD
110 120 130 140 150
GTENKGNLGA NAILAVSLAV AKAAADTASL PLYKYIGGCN AYVMPAPMMN
160 170 180 190 200
VLNGGQHAGN ALDFQEFMIM PVGADSFAEA VRMCAETYQS LKKVVAEKYG
210 220 230 240 250
KDAVNIGDEG GFAPPVKTID EALALLLEGV KRAGYEDEIV FTLDSAASEF
260 270 280 290 300
YDEKSGSYIV AGEKVSTDKL IDIYKEMVAQ YPIVSIEDPL FEEDFEGFTK
310 320 330 340 350
ATKELKGIQI VGDDLFVTNT KRLKKGIEMG ASNSLLLKVN QIGTLSESID
360 370 380 390 400
AANMAFRNGY SLVVSHRSGE SEDSTIADLA VALNSGQIKT GAPARGERTA
410 420
KYNQLIRIEE ELQISKYAGK DFKVPF
Length:426
Mass (Da):45,811
Last modified:May 20, 2008 - v2
Checksum:iE0149C84D29CB4B0
GO

Sequence cautioni

The sequence ABO35540 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000609 Genomic DNA. Translation: ABO35540.1. Different initiation.
RefSeqiWP_011868993.1. NC_009135.1.

Genome annotation databases

EnsemblBacteriaiABO35540; ABO35540; MmarC5_1242.
GeneIDi4929067.
KEGGimmq:MmarC5_1242.

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_METM5
AccessioniPrimary (citable) accession number: A4FZA6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: May 10, 2017
This is version 66 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