ID   ENO12_SCHPO             Reviewed;         440 AA.
AC   Q8NKC2; Q8TFF7;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-APR-2003, sequence version 2.
DT   16-JUN-2009, entry version 46.
DE   RecName: Full=Enolase 1-2;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phosphoglycerate dehydratase 1-2;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase 1-2;
GN   Name=eno102; Synonyms=eno1; ORFNames=SPBPB21E7.01c, SPBPB8B6.07c;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC       H(2)O.
CC   -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing
CC       the dimer (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the enolase family.
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DR   EMBL; CU329671; CAD27913.2; -; Genomic_DNA.
DR   RefSeq; NP_001018769.2; -.
DR   HSSP; Q9NDH8; 1OEP.
DR   GeneID; 3361181; -.
DR   KEGG; spo:SPBPB21E7.01c; -.
DR   GeneDB_Spombe; SPBPB21E7.01c; -.
DR   BRENDA; 4.2.1.11; 653.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000941; Enolase.
DR   PANTHER; PTHR11902; Enolase; 1.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   PIRSF; PIRSF001400; Enolase; 1.
DR   PRINTS; PR00148; ENOLASE.
DR   ProDom; PD000902; Enolase; 1.
DR   TIGRFAMs; TIGR01060; eno; 1.
DR   PROSITE; PS00164; ENOLASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium;
KW   Metal-binding.
FT   CHAIN         1    440       Enolase 1-2.
FT                                /FTId=PRO_0000134059.
FT   REGION      373    376       Substrate binding (By similarity).
FT   ACT_SITE    212    212       Proton donor (By similarity).
FT   ACT_SITE    346    346       Proton acceptor (By similarity).
FT   METAL       247    247       Magnesium (By similarity).
FT   METAL       296    296       Magnesium (By similarity).
FT   METAL       321    321       Magnesium (By similarity).
FT   BINDING     160    160       Substrate (By similarity).
FT   BINDING     169    169       Substrate (By similarity).
FT   BINDING     296    296       Substrate (By similarity).
FT   BINDING     321    321       Substrate (By similarity).
FT   BINDING     397    397       Substrate (By similarity).
SQ   SEQUENCE   440 AA;  47867 MW;  E59B1487C8C6B382 CRC64;
     MTTIQKIYSR SIYDSRGNPT VEVELTTELG TFRSMVPSGA STGEWEAKEL RDNDKNKWGG
     KGVTIAVHNV NNIIGPALVK SDIKITDQRG IDEFMIKLDG TNDKSKLGAN SIVGVSMAVA
     RAAAAFLKIP LYEYIGKLAG SKTTECIPVP SFNVLNGGRH AGGDLAFQEF MIMPIKAPTF
     SEGLRWGSEV YHTLKALAKK KYGASAGNVG DEGGIAPDLT TAEEALDLVN EAIKEAGYDG
     KVKIGFDVAA SELYNGKLYD LDFKSEHPKP ENKLDYKKLY EKYSALIEKY PIVFIEDPFS
     EEDWGAFSYM SSKTKVEVIA DDLTVTNVKR LSKAIELKCA NALLVKINQI GSLSETIDAA
     NMAKKAGWGL MVSHRSGETD DSFIAHLAVG LEAGQMKSGA PCRSERLAKY NELLRIEDNL
     GDSAIYAGTR AADYIKSNTL
//