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Protein

Enolase

Gene

eno

Organism
Prochlorococcus marinus (strain MIT 9312)
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 (PMT9312_0888)
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 sitei159 – 1591SubstrateUniRule annotation
Binding sitei168 – 1681SubstrateUniRule annotation
Active sitei209 – 2091Proton donorUniRule annotation
Metal bindingi246 – 2461MagnesiumUniRule 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

BioCyciPMAR74546:GHRG-215-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:PMT9312_0210
OrganismiProchlorococcus marinus (strain MIT 9312)
Taxonomic identifieri74546 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000002715 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_0000267072Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi74546.PMT9312_0210.

Structurei

3D structure databases

ProteinModelPortaliQ31CX3.
SMRiQ31CX3. Positions 8-423.
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.
HOGENOMiHOG000072174.
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.

Q31CX3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKETIDFLID TIEARQVLDS RGNPTVEAEV FLECGASGRA IVPSGASTGA
60 70 80 90 100
HEAHELRDGG SKYMGKGVLN AVNKIHETIS PALCGLSALD QTTVDKLMIE
110 120 130 140 150
IDGTFNKSNL GANSILAVSL ATARASANAL DVPLYRYLGD PLSNLLPVPL
160 170 180 190 200
MNVINGGAHA PNSLDFQEFM LVPHGVQNFS ESLRMGTEIF HSLKSLLDKK
210 220 230 240 250
GLSTAVGDEG GFAPNLSSSE EAGDLLLEAI QKAGFIPGEQ VSLALDAAST
260 270 280 290 300
EFYSDGIYKY EGKSLNSSEM ISYLSRLVSN YPIVSIEDGL AEDDWEGWSE
310 320 330 340 350
LNKELGNKVQ LVGDDLFVTN TERLRKGIME KSANSILIKV NQIGTLTETL
360 370 380 390 400
EAIELAKTSG FTSVISHRSG ETEDTTIADL SVATRSGQIK TGSLSRSERI
410 420 430
AKYNRLLKIE EELGNQARFA GALGLGPKNI
Length:430
Mass (Da):46,071
Last modified:December 6, 2005 - v1
Checksum:iD263A14A2578F717
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000111 Genomic DNA. Translation: ABB49272.1.
RefSeqiWP_011375776.1. NC_007577.1.

Genome annotation databases

EnsemblBacteriaiABB49272; ABB49272; PMT9312_0210.
KEGGipmi:PMT9312_0210.
PATRICi23004038. VBIProMar70153_0214.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000111 Genomic DNA. Translation: ABB49272.1.
RefSeqiWP_011375776.1. NC_007577.1.

3D structure databases

ProteinModelPortaliQ31CX3.
SMRiQ31CX3. Positions 8-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi74546.PMT9312_0210.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB49272; ABB49272; PMT9312_0210.
KEGGipmi:PMT9312_0210.
PATRICi23004038. VBIProMar70153_0214.

Phylogenomic databases

eggNOGiCOG0148.
HOGENOMiHOG000072174.
KOiK01689.
OMAiEFMIIPV.
OrthoDBiEOG65J589.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BioCyciPMAR74546:GHRG-215-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. "Complete sequence of Prochlorococcus marinus str. MIT 9312."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MIT 9312.

Entry informationi

Entry nameiENO_PROM9
AccessioniPrimary (citable) accession number: Q31CX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 6, 2005
Last modified: July 22, 2015
This is version 77 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

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.