Skip Header

Contribute Send feedback
Read comments (?) or add your own

A3DP05 (A3DP05_STAMF) Unreviewed, UniProtKB/TrEMBL

Last modified November 16, 2011. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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:Smar_1274
OrganismStaphylothermus marinus (strain ATCC 43588 / DSM 3639 / F1) [Complete proteome] [HAMAP]
Taxonomic identifier399550 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Staphylothermus

Protein attributes

Sequence length439 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

Region377 – 3804Substrate binding By similarity HAMAP MF_00318

Sites

Active site2181Proton donor By similarity HAMAP MF_00318
Active site3501Proton acceptor By similarity HAMAP MF_00318
Metal binding2551Magnesium By similarity HAMAP MF_00318
Metal binding2981Magnesium By similarity HAMAP MF_00318
Metal binding3251Magnesium By similarity HAMAP MF_00318
Binding site1661Substrate By similarity HAMAP MF_00318
Binding site1751Substrate By similarity HAMAP MF_00318
Binding site2981Substrate By similarity HAMAP MF_00318
Binding site3251Substrate By similarity HAMAP MF_00318
Binding site3501Substrate (covalent); in inhibited form By similarity HAMAP MF_00318
Binding site4011Substrate By similarity HAMAP MF_00318

Amino acid modifications

Modified residue2921Phosphotyrosine By similarity HAMAP MF_00318

Sequences

Sequence LengthMass (Da)Tools
A3DP05 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: A424FD26217D89FE

FASTA43948,087
        10         20         30         40         50         60 
MTYTTYTTVL DDMFKIKAVR GRYILDSRGN PTVQVKVVTE GLGVGVAAAP SGASTGIHEA 

        70         80         90        100        110        120 
VEVRDGGKEF HGKGVRKAVD NVNTIIAPAI TGMDSRRQVE IDYKMIEIDG TENKSRLGGN 

       130        140        150        160        170        180 
AIIATSLAVA KAAASTMKIP LYYYIGGKQA NILPVPMLNI INGGVHAGNK LDFQEFMIVP 

       190        200        210        220        230        240 
AGFNSFHEAL RAAVETYHEL KRILKEKYGS SAINVGDEGG YAPPLEKIRD ALDLLMEAIK 

       250        260        270        280        290        300 
SAGYSPGKEI ALALDAASSQ FYNKEKKVYV VEGRELTRDQ MIELYEELVN DYPIVSIEDP 

       310        320        330        340        350        360 
LYEEDYDGFA EITKRLGDKV LIVGDDLFTT NPKRLSKGIE VGAANAILVK VNQIGTLTET 

       370        380        390        400        410        420 
MEVVRLAHIH NYRTIISHRS GETEDTTIAD LAVGLNAGLI KTGAPARGER TAKYNRLLEI 

       430 
EEELEKPMYL GFQLFPRKP

« Hide

References

[1]"Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1."
Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H., Kyrpides N.C.
Stand. Genomic Sci. 1:183-188(2009)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota."
Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I., Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A., Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B., Woese C., Bristow J., Kyrpides N.
BMC Genomics 10:145-145(2009) [PubMed: 19341479] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000575 Genomic DNA. Translation: ABN70365.1.
RefSeqYP_001041273.1. NC_009033.1.

3D structure databases

ProteinModelPortalA3DP05.
SMRA3DP05. Positions 10-431.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3DP05.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4906498.
GenomeReviewsGene locus Smar_1274 in contig CP000575_GR.
KEGGsmr:Smar_1274.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04113.
HOGENOMHBG726599.
OMAEAWSYFY.
ProtClustDBCLSK2399710.

Enzyme and pathway databases

BioCycSMAR399550:SMAR_1274-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 nameA3DP05_STAMF
AccessionPrimary (citable) accession number: A3DP05
Entry history
Integrated into UniProtKB/TrEMBL: March 20, 2007
Last sequence update: March 20, 2007
Last modified: November 16, 2011
This is version 34 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