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Q60173 (ENO_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:MJ0232
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length423 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 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 archaeal cell surface By similarity. HAMAP MF_00318

Sequence similarities

Belongs to the enolase family.

Sequence caution

The sequence AAB98220.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
Secreted
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical term3D-structure
Complete 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 – 423423Enolase HAMAP MF_00318
PRO_0000134024

Regions

Region362 – 3654Substrate binding By similarity

Sites

Active site2091Proton donor By similarity
Active site3351Proton acceptor By similarity
Metal binding2441Magnesium By similarity
Metal binding2851Magnesium By similarity
Metal binding3101Magnesium By similarity
Binding site1571Substrate By similarity
Binding site1661Substrate By similarity
Binding site2851Substrate By similarity
Binding site3101Substrate By similarity
Binding site3351Substrate (covalent); in inhibited form By similarity
Binding site3861Substrate By similarity

Secondary structure

1 ......................................................................... 423
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q60173 [UniParc].

Last modified February 21, 2001. Version 2.
Checksum: 9C9BB163E64BF577

FASTA42346,298
        10         20         30         40         50         60 
MDERFEIKDI VAREVIDSRG NPTVEVEVIT KGNGYGSAIV PSGASTGTHE ALELRDKEKR 

        70         80         90        100        110        120 
FGGKGVLMAV ENVNSIIRPE ILGYDARMQR EIDTIMIELD GTPNKSRLGA NAILAVSLAV 

       130        140        150        160        170        180 
AKAAAATAKI PLYKYLGGFN SYVMPVPMMN VINGGKHAGN DLDLQEFMIM PVGATSISEA 

       190        200        210        220        230        240 
VRMGSEVYHV LKNVILEKYG KNAVNVGDEG GFAPPLKTSR EALDLLTESV KKAGYEDEVV 

       250        260        270        280        290        300 
FALDAAASEF YKDGYYYVEG KKLTREELLD YYKALVDEYP IVSIEDPFHE EDFEGFAMIT 

       310        320        330        340        350        360 
KELDIQIVGD DLFVTNVERL RKGIEMKAAN ALLLKVNQIG TLSEAVDAAQ LAFRNGYGVV 

       370        380        390        400        410        420 
VSHRSGETED TTIADLSVAL NSGQIKTGAP ARGERTAKYN QLIRIEQELG LSKYAGRNFR 


CPF

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L77117 Genomic DNA. Translation: AAB98220.1. Different initiation.
PIRA64329.
RefSeqNP_247203.1. NC_000909.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PA6X-ray1.85A/B1-423[»]
ProteinModelPortalQ60173.
SMRQ60173. Positions 1-423.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1451085.
GenomeReviewsGene locus MJ0232 in contig L77117_GR.
KEGGmja:MJ_0232.
NMPDRfig|243232.1.peg.240.
TIGRMJ0232.

Phylogenomic databases

HOGENOMHBG726599.
OMAGELYKNF.
ProtClustDBPRK00077.

Enzyme and pathway databases

BioCycMJAN243232:MJ_0232-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 nameENO_METJA
AccessionPrimary (citable) accession number: Q60173
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 21, 2001
Last modified: November 16, 2011
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Methanococcus jannaschii

Methanococcus jannaschii: 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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