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UniProtKB/Swiss-Prot entry Q9F3P9

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ENO2_STRCO
Primary accession number Q9F3P9
Secondary accession numbers None
Integrated into Swiss-Prot on October 10, 2002
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 49)
Name and origin of the protein
Protein name Enolase 2
Synonyms EC 4.2.1.11
2-phosphoglycerate dehydratase 2
2-phospho-D-glycerate hydro-lyase 2
Gene name
Name: eno2
OrderedLocusNames: SCO7638
ORFNames: SC10F4.11c
From
Streptomyces coelicolor [TaxID: 1902] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Streptomycineae; Streptomycetaceae; Streptomyces.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-471 / A3(2) / M145;
DOI=10.1038/417141a; PubMed=12000953 [NCBI, ExPASy, EBI, Israel, Japan]
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2).";
Nature 417:141-147(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AL939132; CAC16971.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_631678.1; -.
3D structure databases
HSSP Q9NDH8; 1OEP. [HSSP ENTRY / PDB]
ModBase Q9F3P9.
Enzyme and pathway databases
BioCyc SCOE100226:SCO7638-MON; -.
Ontologies
GO
GO:0009986; Cellular component: cell surface (inferred from electronic annotation from HAMAP).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from HAMAP).
GO:0004634; Molecular function: phosphopyruvate hydratase activity (inferred from electronic annotation from HAMAP).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00318; -; 1.
PBIL [Tree]
InterPro IPR000941; Enolase.
Graphical view of domain structure.
PANTHER PTHR11902; Enolase; 1.
Pfam PF00113; Enolase_C; 1.
PF03952; Enolase_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001400; Enolase; 1.
PRINTS PR00148; ENOLASE.
ProDom PD000902; Enolase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01060; eno; 1.
PROSITE PS00164; ENOLASE; 1.
BLOCKS Q9F3P9.
Genome annotation databases
GeneID 1103076; -.
GenomeReviews AL645882_GR; SCO7638.
KEGG sco:SCO7638; -.
NMPDR fig|100226.1.peg.7569; -.
Phylogenomic databases
HOGENOM Q9F3P9; -.
Genome annotation databases
CMR Q9F3P9; SCO7638.
Other
ProtoNet Q9F3P9.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein; Secreted.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   434  434     Enolase 2. PRO_0000133977
REGION   372   375  4     Substrate binding (By similarity). 
ACT_SITE   213   213        Proton donor (By similarity). 
ACT_SITE   345   345        Proton acceptor (By similarity). 
METAL   250   250        Magnesium (By similarity). 
METAL   293   293        Magnesium (By similarity). 
METAL   320   320        Magnesium (By similarity). 
BINDING   163   163        Substrate (By similarity). 
BINDING   172   172        Substrate (By similarity). 
BINDING   293   293        Substrate (By similarity). 
BINDING   320   320        Substrate (By similarity). 
BINDING   345   345        Substrate (covalent); in inhibited form (By similarity). 
BINDING   396   396        Substrate (By similarity). 
MOD_RES   287   287        Phosphotyrosine (By similarity). 
Sequence information
Length: 434 AA [This is the length of the unprocessed precursor] Molecular weight: 45534 Da [This is the MW of the unprocessed precursor] CRC64: 435A1CC0629DC0A0 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSATAVEPAA AIETVTARRI IDSRGNPTVE VDVVLEDGSL GRAAVPSGAS TGAREAVELR 

        70         80         90        100        110        120 
DEDPTRWHGK GVDRAVAHVN GEIAASVRGR DAADQAGLDA ALIALDGTAA KSRLGANALL 

       130        140        150        160        170        180 
GVSLAAAKAA AAARRQPLYR YLGGADAHLL PLPMMNIVNG GAHADNPLDF QEFMIVPVGA 

       190        200        210        220        230        240 
DTFAEAVRMG SEVFHTLRRD LLAAGHSTGV GDEGGFAPAL RTAEEALDFV VAAIERTGYR 

       250        260        270        280        290        300 
AGPDIGLVMD PASSEFFRDG GYDYAGEGVR RSPAEHADHL AGLIDAYPVV SIEDPMAEDD 

       310        320        330        340        350        360 
LDGWRELTDR VGDRCQLTGD DVFCTDEALV REGIRTGVGN SVLVKVNQIG TLTEALATVA 

       370        380        390        400        410        420 
TAHEAGWTVV MSHRSGETED TTIADLAVAT GCGQIKTGSL SRSDRTAKYN RLIRIEEELG 

       430 
ASARFAGRSA LRRV
Q9F3P9 in FASTA format

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