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Q83B44 (ENO_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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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:CBU_1674
OrganismCoxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]
Taxonomic identifier227377 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella ›

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete proteome
Reference 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_0000133877

Regions

Region364 – 3674Substrate binding By similarity

Sites

Active site2071Proton donor By similarity
Active site3371Proton acceptor By similarity
Metal binding2441Magnesium By similarity
Metal binding2851Magnesium By similarity
Metal binding3121Magnesium By similarity
Binding site1571Substrate By similarity
Binding site1661Substrate By similarity
Binding site2851Substrate By similarity
Binding site3121Substrate By similarity
Binding site3371Substrate (covalent); in inhibited form By similarity
Binding site3881Substrate By similarity

Amino acid modifications

Modified residue2791Phosphotyrosine By similarity

Secondary structure

1 ................................................................... 428
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q83B44 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: B58295D02CC2BE61

FASTA42846,626
        10         20         30         40         50         60 
MTATITDINA HEILDSRANP TLEVRVTLSS QAYGCAAVPS GASTGEREAV ELRDNDLERY 

        70         80         90        100        110        120 
GGKGVLQAVE NVNGPIRDAL LGQDPRSQEE IDRIMIELDG TENKANLGAN AILGVSLAVA 

       130        140        150        160        170        180 
YAAANNADLP LYRYLGGDGG PFSMPVPMMN IINGGAHATN NLDFQEFMIV PVGAPTFAEA 

       190        200        210        220        230        240 
LRYGAEVFHA LKKRLVSRGL MSAVGDEGGF APDLPNNEAA FELILEAIED ANYVPGKDIY 

       250        260        270        280        290        300 
LALDAASSEL YQNGRYDFEN NQLTSEEMID RLTEWTKKYP VISIEDGLSE NDWAGWKLLT 

       310        320        330        340        350        360 
ERLENKVQLV GDDIFVTNPD ILEKGIKKNI ANAILVKLNQ IGTLTETLAT VGLAKSNKYG 

       370        380        390        400        410        420 
VIISHRSGET EDTTIADLAV ATDARQIKTG SLCRSDRVAK YNRLLQIERE LNDQAPYAGK 


EAFLFNRK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016828 Genomic DNA. Translation: AAO91170.1.
RefSeqNP_820656.1. NC_002971.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3TQPX-ray2.20A/B1-428[»]
ProteinModelPortalQ83B44.
SMRQ83B44. Positions 3-423.
ModBaseSearch...

Protein-protein interaction databases

STRING227377.CBU_1674.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO91170; AAO91170; CBU_1674.
GeneID1209585.
KEGGcbu:CBU_1674.
PATRIC17932089. VBICoxBur82552_1663.

Phylogenomic databases

eggNOGCOG0148.
HOGENOMHOG000072174.
KOK01689.
OMAEYMIMPL.
ProtClustDBPRK00077.

Enzyme and pathway databases

BioCycCBUR227377:GJ7S-1645-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_COXBU
AccessionPrimary (citable) accession number: Q83B44
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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