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Q31CX3 (ENO_PROM9) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Enolase

EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase
Gene names
Name:eno
Ordered Locus Names:PMT9312_0210
OrganismProchlorococcus marinus (strain MIT 9312) [Complete proteome] [HAMAP]
Taxonomic identifier74546 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis By similarity. HAMAP-Rule MF_00318

Catalytic activity

2-phospho-D-glycerate = phosphoenolpyruvate + H2O. HAMAP-Rule MF_00318

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00318

Enzyme regulation

The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein By similarity. HAMAP-Rule MF_00318

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP-Rule MF_00318

Subcellular location

Cytoplasm By similarity. Secreted By similarity. Cell surface By similarity. 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 By similarity. HAMAP-Rule MF_00318

Sequence similarities

Belongs to the enolase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
Secreted
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcell surface

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

phosphopyruvate hydratase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

phosphopyruvate hydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430Enolase HAMAP-Rule MF_00318
PRO_0000267072

Regions

Region366 – 3694Substrate binding By similarity

Sites

Active site2091Proton donor By similarity
Active site3391Proton acceptor By similarity
Metal binding2461Magnesium By similarity
Metal binding2871Magnesium By similarity
Metal binding3141Magnesium By similarity
Binding site1591Substrate By similarity
Binding site1681Substrate By similarity
Binding site2871Substrate By similarity
Binding site3141Substrate By similarity
Binding site3391Substrate (covalent); in inhibited form By similarity
Binding site3901Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q31CX3 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: D263A14A2578F717

FASTA43046,071
        10         20         30         40         50         60 
MKETIDFLID TIEARQVLDS RGNPTVEAEV FLECGASGRA IVPSGASTGA HEAHELRDGG 

        70         80         90        100        110        120 
SKYMGKGVLN AVNKIHETIS PALCGLSALD QTTVDKLMIE IDGTFNKSNL GANSILAVSL 

       130        140        150        160        170        180 
ATARASANAL DVPLYRYLGD PLSNLLPVPL MNVINGGAHA PNSLDFQEFM LVPHGVQNFS 

       190        200        210        220        230        240 
ESLRMGTEIF HSLKSLLDKK GLSTAVGDEG GFAPNLSSSE EAGDLLLEAI QKAGFIPGEQ 

       250        260        270        280        290        300 
VSLALDAAST EFYSDGIYKY EGKSLNSSEM ISYLSRLVSN YPIVSIEDGL AEDDWEGWSE 

       310        320        330        340        350        360 
LNKELGNKVQ LVGDDLFVTN TERLRKGIME KSANSILIKV NQIGTLTETL EAIELAKTSG 

       370        380        390        400        410        420 
FTSVISHRSG ETEDTTIADL SVATRSGQIK TGSLSRSERI AKYNRLLKIE EELGNQARFA 

       430 
GALGLGPKNI 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000111 Genomic DNA. Translation: ABB49272.1.
RefSeqYP_396708.1. NC_007577.1.

3D structure databases

ProteinModelPortalQ31CX3.
SMRQ31CX3. Positions 8-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING74546.PMT9312_0210.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB49272; ABB49272; PMT9312_0210.
GeneID3764995.
KEGGpmi:PMT9312_0210.
PATRIC23004038. VBIProMar70153_0214.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0148.
HOGENOMHOG000072174.
KOK01689.
OMANLPLYRY.
OrthoDBEOG65J589.
ProtClustDBPRK00077.

Enzyme and pathway databases

BioCycPMAR74546:GHRG-215-MONOMER.
UniPathwayUPA00109; UER00187.

Family and domain databases

HAMAPMF_00318. Enolase.
InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
PANTHERPTHR11902. PTHR11902. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
TIGRFAMsTIGR01060. eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameENO_PROM9
AccessionPrimary (citable) accession number: Q31CX3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 6, 2005
Last modified: February 19, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways