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UniProtKB/Swiss-Prot entry Q9F2Q3

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

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Entry information
Entry name ENO1_STRCO
Primary accession number Q9F2Q3
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 1
Synonyms EC 4.2.1.11
2-phosphoglycerate dehydratase 1
2-phospho-D-glycerate hydro-lyase 1
Gene name
Name: eno1
OrderedLocusNames: SCO3096
ORFNames: SCE41.05c
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
AL939115; CAC09537.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_627314.1; -.
3D structure databases
HSSP Q9NDH8; 1OEP. [HSSP ENTRY / PDB]
ModBase Q9F2Q3.
Enzyme and pathway databases
BioCyc SCOE100226:SCO3096-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 Q9F2Q3.
Genome annotation databases
GeneID 1098530; -.
GenomeReviews AL645882_GR; SCO3096.
KEGG sco:SCO3096; -.
NMPDR fig|100226.1.peg.3057; -.
Phylogenomic databases
HOGENOM Q9F2Q3; -.
Genome annotation databases
CMR Q9F2Q3; SCO3096.
Other
ProtoNet Q9F2Q3.
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   426  426     Enolase 1. PRO_0000133976
REGION   362   365  4     Substrate binding (By similarity). 
ACT_SITE   205   205        Proton donor (By similarity). 
ACT_SITE   335   335        Proton acceptor (By similarity). 
METAL   242   242        Magnesium (By similarity). 
METAL   283   283        Magnesium (By similarity). 
METAL   310   310        Magnesium (By similarity). 
BINDING   155   155        Substrate (By similarity). 
BINDING   164   164        Substrate (By similarity). 
BINDING   283   283        Substrate (By similarity). 
BINDING   310   310        Substrate (By similarity). 
BINDING   335   335        Substrate (covalent); in inhibited form (By similarity). 
BINDING   386   386        Substrate (By similarity). 
MOD_RES   277   277        Phosphotyrosine (By similarity). 
Sequence information
Length: 426 AA [This is the length of the unprocessed precursor] Molecular weight: 45483 Da [This is the MW of the unprocessed precursor] CRC64: 63AED7B7A4E15001 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MPSIDVVVAR EILDSRGNPT VEVEVGLDDG STGRAAVPSG ASTGAFEAIE LRDGDPSRYL 

        70         80         90        100        110        120 
GKGVEKAVLA VIEQIGPELV GYDATEQRLI DQAMFDLDAT DNKGSLGANA ILGVSLAVAH 

       130        140        150        160        170        180 
AASEASDLPL FRYLGGPNAH LLPVPMMNIL NGGSHADSNV DIQEFMIAPI GAESFSEALR 

       190        200        210        220        230        240 
WGAEVYHTLK KVLKNKGLAT GLGDEGGFAP NLGSNREALD LILEAIKEAG YTPGEQIALA 

       250        260        270        280        290        300 
LDVAASEFYK DGSYAFEGKN RSAAEMTEYY AELVEAYPLV SIEDPLFEDD WDGWNTITAK 

       310        320        330        340        350        360 
LGDKVQLVGD DLFVTNPERL ARGIEENSAN ALLVKVNQIG SLTETLDAVE LAQRNGFKCM 

       370        380        390        400        410        420 
MSHRSGETED VTIADLAVAT NCGQIKTGAP ARSERVAKYN QLLRIEEILD DAAVYAGRSA 


FPRFKG
Q9F2Q3 in FASTA format

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