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Q88YH3 (ENO1_LACPL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Enolase 1
EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase 1
2-phosphoglycerate dehydratase 1
Gene names
Name:eno1
Synonyms:enoA, enoA1
Ordered Locus Names:lp_0792
OrganismLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Taxonomic identifier220668 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length442 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 MF_00318

Catalytic activity

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

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer By similarity.

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 MF_00318

Pathway

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

Subcellular location

Cytoplasm. Secreted. Cell surface. 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 bacterial cell surface By similarity. HAMAP MF_00318

Sequence similarities

Belongs to the enolase family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   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: InterPro

phosphopyruvate hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 442442Enolase 1 HAMAP MF_00318
PRO_0000133906

Regions

Region369 – 3724Substrate binding By similarity

Sites

Active site2051Proton donor By similarity
Active site3421Proton acceptor By similarity
Metal binding2421Magnesium By similarity
Metal binding2901Magnesium By similarity
Metal binding3171Magnesium By similarity
Binding site1551Substrate By similarity
Binding site1641Substrate By similarity
Binding site2901Substrate By similarity
Binding site3171Substrate By similarity
Binding site3421Substrate (covalent); in inhibited form By similarity
Binding site3931Substrate By similarity

Amino acid modifications

Modified residue2841Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q88YH3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: B4FD3E75AA7359D4

FASTA44248,030
        10         20         30         40         50         60 
MSIITDIYAR EVLDSRGNPT VEVELYTESG AFGRGIVPSG ASTGEHEAVE LRDGDKSRFM 

        70         80         90        100        110        120 
GKGVTKAVDN VNKLIAKEIV GYDVTDQRAI DQAMIKLDGT PNKAKLGANA ILGVSIAAAR 

       130        140        150        160        170        180 
AAADELEMPL YNYLGGFNAH VLPTPMMNVI NGGAHANNDV DFQEFMIMPV GASSVKEAIR 

       190        200        210        220        230        240 
MGSETFHNLK AILNERGYST AVGDEGGFAP DLKNNEEPFE ILVEAIERAG YKPGKDIAIA 

       250        260        270        280        290        300 
FDCAASEFYN EETGKYDLKG EGENGQSFTA EEFVDLLDSI VDKYPIVSIE DPLDENNWED 

       310        320        330        340        350        360 
WQMATAKLGK KVQIVGDDLF VTNTDYLAKG IKMGVANSIL IKVNQIGTLT ETVEAIEMAK 

       370        380        390        400        410        420 
EAGYTAIVSH RSGETEDTTI ADLVVAMNAG QIKTGSMSRT ERIAKYNQLM RIEDQLESTS 

       430        440 
EYKGIHGFYN LDEAARNTIT SK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL935263 Genomic DNA. Translation: CCC78252.1.
RefSeqNP_784537.1. NC_004567.1.

3D structure databases

ProteinModelPortalQ88YH3.
SMRQ88YH3. Positions 2-434.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1063808.
GenomeReviewsGene locus lp_0792 in contig AL935263_GR.
KEGGlpl:lp_0792.
NMPDRfig|220668.1.peg.671.
PATRIC22247995. VBILacPla27411_0669.

Phylogenomic databases

HOGENOMHBG726599.
OMAQEYMIMP.
ProtClustDBPRK00077.

Enzyme and pathway databases

BioCycLPLA220668:LP_0792-MONOMER.

Family and domain databases

HAMAPMF_00318. Enolase.
[Tree]
InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
KOK01689.
PANTHERPTHR11902. Enolase. 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 nameENO1_LACPL
AccessionPrimary (citable) accession number: Q88YH3
Secondary accession number(s): F9UM13
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 1, 2003
Last modified: January 25, 2012
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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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