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UniProtKB/Swiss-Prot entry Q6FQY4

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

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Entry information
Entry name ENO2_CANGA
Primary accession number Q6FQY4
Secondary accession numbers None
Integrated into Swiss-Prot on December 6, 2005
Sequence was last modified on July 19, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 33)
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: CAGL0I02486g
From
Candida glabrata (Yeast) (Torulopsis glabrata) [TaxID: 5478] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; Candida.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
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
CR380955; CAG60297.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_447360.1; -.
3D structure databases
SMR Q6FQY4; 2-437.
ModBase Q6FQY4.
Ontologies
GO
GO:0000015; Cellular component: phosphopyruvate hydratase complex (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004634; Molecular function: phosphopyruvate hydratase activity (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
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.
ProtoNet Q6FQY4.
Genome annotation databases
GeneID 2889384; -.
KEGG cgr:CAGL0I02486g; -.
Phylogenomic databases
HOGENOM Q6FQY4; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   437  437     Enolase 2. PRO_0000134045
REGION   373   376  4     Substrate binding (By similarity). 
ACT_SITE   212   212        Proton donor (By similarity). 
ACT_SITE   346   346        Proton acceptor (By similarity). 
METAL   247   247        Magnesium (By similarity). 
METAL   296   296        Magnesium (By similarity). 
METAL   321   321        Magnesium (By similarity). 
BINDING   160   160        Substrate (By similarity). 
BINDING   169   169        Substrate (By similarity). 
BINDING   296   296        Substrate (By similarity). 
BINDING   321   321        Substrate (By similarity). 
BINDING   397   397        Substrate (By similarity). 
Sequence information
Length: 437 AA [This is the length of the unprocessed precursor] Molecular weight: 46739 Da [This is the MW of the unprocessed precursor] CRC64: D8DAE343A84EB6B1 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGIHEALEMR DGDKSKWLGK 

        70         80         90        100        110        120 
GVENAVKNVN DVIAPAFVKA NVDIKDQKAV DDLLLSLDGT ANKSKLGANA ILGVSMAAAR 

       130        140        150        160        170        180 
AAAAEKNVPL YQHLADLSDS KTSPFVLPVP FLNVLNGGSH AGGALALQEF MIAPTGAKSF 

       190        200        210        220        230        240 
REAMRIGSEV YHNLKSLTKK RYGSSAGNVG DEGGVAPDIQ TAEEALDLIV DAIKAAGHEG 

       250        260        270        280        290        300 
KVKIGLDCAS SEFFKDGKYD LDFKNPNSDA SKWLSGPQLA DLYHSLVKKY PIVSIEDPFA 

       310        320        330        340        350        360 
EDDWEAWSHF FKTAGVQIVA DDLTVTNPKR IATAIEKKAA DALLLKVNQI GSLSESIKAA 

       370        380        390        400        410        420 
QDSFAAGWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA PARSERLAKL NQLLRIEEEL 

       430 
GDKAVYAGDN FHHGFKL
Q6FQY4 in FASTA format

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