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B1L7C2 (B1L7C2_KORCO) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 27. Feed History...

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

Protein namesRecommended name:
Enolase HAMAP MF_00318 RuleBase RU000654
EC=4.2.1.11 HAMAP MF_00318 RuleBase RU000654
Alternative name(s):
2-phospho-D-glycerate hydro-lyase HAMAP MF_00318
2-phosphoglycerate dehydratase HAMAP MF_00318
Gene names
Name:eno HAMAP MF_00318
Ordered Locus Names:Kcr_1606
OrganismKorarchaeum cryptofilum (strain OPF8)
Taxonomic identifier374847 [NCBI]
Taxonomic lineageArchaea › Korarchaeota › Candidatus Korarchaeum

Protein attributes

Sequence length421 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 RuleBase RU000654

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer By similarity. HAMAP MF_00318 RuleBase RU000654

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 RuleBase RU000654

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 cell surface By similarity. HAMAP MF_00318

Sequence similarities

Belongs to the enolase family. HAMAP MF_00318 RuleBase RU000654

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region362 – 3654Substrate binding By similarity HAMAP MF_00318

Sites

Active site2071Proton donor By similarity HAMAP MF_00318
Active site3351Proton acceptor By similarity HAMAP MF_00318
Metal binding2421Magnesium By similarity HAMAP MF_00318
Metal binding2831Magnesium By similarity HAMAP MF_00318
Metal binding3101Magnesium By similarity HAMAP MF_00318
Binding site1551Substrate By similarity HAMAP MF_00318
Binding site1641Substrate By similarity HAMAP MF_00318
Binding site2831Substrate By similarity HAMAP MF_00318
Binding site3101Substrate By similarity HAMAP MF_00318
Binding site3351Substrate (covalent); in inhibited form By similarity HAMAP MF_00318
Binding site3861Substrate By similarity HAMAP MF_00318

Amino acid modifications

Modified residue2771Phosphotyrosine By similarity HAMAP MF_00318

Sequences

Sequence LengthMass (Da)Tools
B1L7C2 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 34942210530C4A74

FASTA42145,850
        10         20         30         40         50         60 
MSFRIEDVRA REVLDSRGNP TVEVTVKLEG GGSGRFSVPS GASKGKREAL ELRDGGKWLR 

        70         80         90        100        110        120 
GMGVIKAVRN VNEIIRPSLI GVDASIQPLV DDILIQLDGT PNKSRLGANS ILGASVASAK 

       130        140        150        160        170        180 
ASSDQMGVPL YKYLGGAFSR VLPIPLMNII NGGKHAGNEL AIQEFMIVPV KFKTFKDALF 

       190        200        210        220        230        240 
AGVSVYMELK ALLEERYGRH AVNLGDEGGF APPMKRTEEA LEALVSSIER VGLEGEVKLA 

       250        260        270        280        290        300 
IDCAASNFYA DGKYNIDGAS LTKEELISFY ERIVDEYPIV AIEDPFHEED LDSLSELTKK 

       310        320        330        340        350        360 
LGHRILLVGD DYFVSNERYL RKGIEAKAGN AVLLKVNQIG TLTEAVRTAS LAFRYGYRVI 

       370        380        390        400        410        420 
VSHRSGETND PFISDFSVAL NCGYIKAGAP ARGERVAKYN RLLEIEEELG SVASFSQLDT 


L

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References

[1]"A korarchaeal genome reveals new insights into the evolution of the Archaea."
Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L., Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A., Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G., Richardson P., Keller M., Stetter K.O.
Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008) [PubMed: 18535141] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OPF8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000968 Genomic DNA. Translation: ACB08351.1.
RefSeqYP_001738034.1. NC_010482.1.

3D structure databases

ProteinModelPortalB1L7C2.
SMRB1L7C2. Positions 3-410.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1L7C2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6094882.
GenomeReviewsGene locus Kcr_1606 in contig CP000968_GR.
KEGGkcr:Kcr_1606.

Phylogenomic databases

HOGENOMHBG726599.
OMAGELYKNF.
PhylomeDBB1L7C2.

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 nameB1L7C2_KORCO
AccessionPrimary (citable) accession number: B1L7C2
Entry history
Integrated into UniProtKB/TrEMBL: April 29, 2008
Last sequence update: April 29, 2008
Last modified: December 14, 2011
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info