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B8D6N5 (B8D6N5_DESK1) Unreviewed, UniProtKB/TrEMBL

Last modified November 16, 2011. Version 19. 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:DKAM_1440
OrganismDesulfurococcus kamchatkensis (strain 1221n / DSM 18924) [Complete proteome] [HAMAP]
Taxonomic identifier490899 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Desulfurococcus

Protein attributes

Sequence length435 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

Region373 – 3764Substrate binding By similarity HAMAP MF_00318

Sites

Active site2141Proton donor By similarity HAMAP MF_00318
Active site3461Proton acceptor By similarity HAMAP MF_00318
Metal binding2511Magnesium By similarity HAMAP MF_00318
Metal binding2941Magnesium By similarity HAMAP MF_00318
Metal binding3211Magnesium By similarity HAMAP MF_00318
Binding site1621Substrate By similarity HAMAP MF_00318
Binding site1711Substrate By similarity HAMAP MF_00318
Binding site2941Substrate By similarity HAMAP MF_00318
Binding site3211Substrate By similarity HAMAP MF_00318
Binding site3461Substrate (covalent); in inhibited form By similarity HAMAP MF_00318
Binding site3971Substrate By similarity HAMAP MF_00318

Amino acid modifications

Modified residue2881Phosphotyrosine By similarity HAMAP MF_00318

Sequences

Sequence LengthMass (Da)Tools
B8D6N5 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: CBC9474D3972506B

FASTA43547,211
        10         20         30         40         50         60 
MYLEIYDDVY VIKDVKARMI LDSRGNPTVQ VRVVTEGLGI GIANAPSGAS TGKHEAVELR 

        70         80         90        100        110        120 
DGGKEFKGKG VSKAVENVNK VIAPTIIGLN SRHQYEVDGK LIEIDGTPNK ARLGGNAIVA 

       130        140        150        160        170        180 
TSLAVAKAAA STMGVPLYYY LGGRAAELLP VPLLNIINGG VHAGNKLDFQ EFMIVPAGFN 

       190        200        210        220        230        240 
SFHDAIRAAV EVYHELKIVL KNKYGPSAVN VGDEGGYAPP LEKIRDALDL LVEAVKKAGY 

       250        260        270        280        290        300 
EPGGEIAIAL DAASSQFYRE DKGVYVIEGR ELGRNEMLEL YEKLVGDYPI VSIEDPLYEE 

       310        320        330        340        350        360 
DFEGFAEMRR RLGDKILIVG DDLFTTNPAR LSKGIESNAG NAVLVKVNQV GTLSETIEVV 

       370        380        390        400        410        420 
RMAHENRYKA IISHRSGETE DTSIADIAVG LSTGLIKTGA PGRGERTAKY NRLLEIAEEL 

       430 
EKPRYPGFRV FPRKP

« Hide

References

[1]"Complete genome sequence of the anaerobic, protein-degrading hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis."
Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V., Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.
J. Bacteriol. 191:2371-2379(2009) [PubMed: 19114480] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001140 Genomic DNA. Translation: ACL11766.1.
RefSeqYP_002429133.1. NC_011766.1.

3D structure databases

ProteinModelPortalB8D6N5.
ModBaseSearch...

Protein-protein interaction databases

STRINGB8D6N5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7171472.
GenomeReviewsGene locus DKAM_1440 in contig CP001140_GR.
KEGGdka:DKAM_1440.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG726599.
OMAEAWSYFY.
ProtClustDBCLSK2399710.

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 nameB8D6N5_DESK1
AccessionPrimary (citable) accession number: B8D6N5
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: November 16, 2011
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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