ID   ENO1_CANAL              Reviewed;         440 AA.
AC   P30575;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-NOV-2008, entry version 59.
DE   RecName: Full=Enolase 1;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phosphoglycerate dehydratase;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
GN   Name=ENO1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 64385 / 1001;
RX   MEDLINE=93239689; PubMed=8478328;
RA   Mason A.B., Buckley H.R., Gorman J.A.;
RT   "Molecular cloning and characterization of the Candida albicans
RT   enolase gene.";
RL   J. Bacteriol. 175:2632-2639(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93015738; PubMed=1400228;
RA   Sundstrom P., Aliaga G.R.;
RT   "Molecular cloning of cDNA and analysis of protein secondary structure
RT   of Candida albicans enolase, an abundant, immunodominant glycolytic
RT   enzyme.";
RL   J. Bacteriol. 174:6789-6799(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KEMH5;
RX   MEDLINE=93366156; PubMed=8359671; DOI=10.1016/0378-1097(93)90189-9;
RA   Franklyn K.M., Warmington J.R.;
RT   "Cloning and nucleotide sequence analysis of the Candida albicans
RT   enolase gene.";
RL   FEMS Microbiol. Lett. 111:101-107(1993).
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC       H(2)O.
CC   -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing
CC       the dimer.
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; L04943; AAB46358.1; -; Genomic_DNA.
DR   EMBL; M93712; AAA34341.1; -; mRNA.
DR   EMBL; L10290; AAA71939.1; -; Unassigned_DNA.
DR   PIR; A40624; A40624.
DR   HSSP; P00924; 4ENL.
DR   SMR; P30575; 5-440.
DR   COMPLUYEAST-2DPAGE; P30575; -.
DR   CGD; CAL0004953; ENO1.
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:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
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   1: Evidence at protein level;
KW   Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding.
FT   CHAIN         1    440       Enolase 1.
FT                                /FTId=PRO_0000134043.
FT   REGION      376    379       Substrate binding (By similarity).
FT   COMPBIAS    118    126       Poly-Ala.
FT   ACT_SITE    213    213       Proton donor (By similarity).
FT   ACT_SITE    349    349       Proton acceptor (By similarity).
FT   METAL       248    248       Magnesium (By similarity).
FT   METAL       297    297       Magnesium (By similarity).
FT   METAL       324    324       Magnesium (By similarity).
FT   BINDING     161    161       Substrate (By similarity).
FT   BINDING     170    170       Substrate (By similarity).
FT   BINDING     297    297       Substrate (By similarity).
FT   BINDING     324    324       Substrate (By similarity).
FT   BINDING     400    400       Substrate (By similarity).
SQ   SEQUENCE   440 AA;  47232 MW;  6621AFD66F275C49 CRC64;
     MSYATKIHAR YVYDSRGNPT VEVDFTTDKG LFRSIVPSGA STGVHEALEL RDGDKSKWLG
     KGVLKAVANV NDIIAPALIK AKIDVVDQAK IDEFLLSLDG TPNKSKLGAN AILGVSLAAA
     NAAAAAQGIP LYKHIANISN AKKGKFVLPV PFQNVLNGGS HAGGALAFQE FMIAPTGVST
     FSEALRIGSE VYHNLKSLTK KKYGQSAGNV GDEGGVAPDI KTPKEALDLI MDAIDKAGYK
     GKVGIAMDVA SSEFYKDGKY DLDFKNPESD PSKWLSGPQL ADLYEQLISE YPIVSIEDPF
     AEDDWDAWVH FFERVGDKIQ IVGDDLTVTN PTRIKTAIEK KAANALLLKV NQIGTLTESI
     QAANDSYAAG WGVMVSHRSG ETEDTFIADL SVGLRSGQIK TGAPARSERL AKLNQILRIE
     EELGSEAIYA GKDFQKASQL
//