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A0PW55 (ENO_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:MUL_4631
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium ›

Protein attributes

Sequence length428 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. 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-Rule MF_00318

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP-Rule 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-Rule 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
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: 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: HAMAP

phosphopyruvate hydratase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Enolase HAMAP-Rule MF_00318
PRO_0000280866

Regions

Region361 – 3644Substrate binding By similarity

Sites

Active site2041Proton donor By similarity
Active site3341Proton acceptor By similarity
Metal binding2411Magnesium By similarity
Metal binding2821Magnesium By similarity
Metal binding3091Magnesium By similarity
Binding site1541Substrate By similarity
Binding site1631Substrate By similarity
Binding site2821Substrate By similarity
Binding site3091Substrate By similarity
Binding site3341Substrate (covalent); in inhibited form By similarity
Binding site3851Substrate By similarity

Amino acid modifications

Modified residue2761Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PW55 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 58A29D49E5EBF57F

FASTA42844,736
        10         20         30         40         50         60 
MPIIEQVGAR EILDSRGNPT VEVEVALIDG TFARAAVPSG ASTGEHEAVE LRDGGDRYGG 

        70         80         90        100        110        120 
KGVKKAVEAV LDEIGPAVIG LNADDQRLVD QALVDLDGTP DKSRLGGNSI LGVSLAVAKA 

       130        140        150        160        170        180 
ASESAELPLF RYIGGPNAHI LPVPMMNILN GGAHADTGVD IQEFMVAPIG APSFSEALRW 

       190        200        210        220        230        240 
GAEVYHALKA VLKKAGLSTG LGDEGGFAPD VASTTAALDL ISQAIEAAGF KPGVDVALAL 

       250        260        270        280        290        300 
DAAANEFHAD GSYTFEGTPR TAAQMTEFYA GLLGSYPVVS IEDPLYENDW DGWAALTAEI 

       310        320        330        340        350        360 
GDRVQIVGDD VFVTNPERLE EGIDRGVANA LLVKVNQIGT LTETLDAVAL AHHSGYRTMI 

       370        380        390        400        410        420 
SHRSGETEDT IIADLAVAVG SGQIKTGAPA RSERVAKYNQ LLRIEEALGD AARYAGDLAF 


PRFVADPK

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000325 Genomic DNA. Translation: ABL06574.1.
RefSeqYP_908045.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PW55.
SMRA0PW55. Positions 3-425.
ModBaseSearch...

Protein-protein interaction databases

STRING362242.MUL_4631.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL06574; ABL06574; MUL_4631.
GeneID4550802.
KEGGmul:MUL_4631.
PATRIC18177111. VBIMycUlc37413_5355.

Organism-specific databases

GenoListMUL_4631.
CMRSearch...

Phylogenomic databases

eggNOGCOG0148.
HOGENOMHOG000072173.
KOK01689.
OMAFHEEDFQ.
ProtClustDBPRK00077.

Enzyme and pathway databases

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_MYCUA
AccessionPrimary (citable) accession number: A0PW55
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: January 9, 2007
Last modified: May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Recent format changes

Overview of recent format changes

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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