ENO1_CANAL
ID ENO1_CANAL Reviewed; 440 AA.
AC P30575; A0A1D8PEA6; Q59QC3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Enolase 1;
DE EC=4.2.1.11 {ECO:0000269|PubMed:1400228};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=2-phosphoglycerate dehydratase;
GN Name=ENO1; OrderedLocusNames=CAALFM_C108500CA;
GN ORFNames=CaO19.395, CaO19.8025;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 64385 / 1001;
RX PubMed=8478328; DOI=10.1128/jb.175.9.2632-2639.1993;
RA Mason A.B., Buckley H.R., Gorman J.A.;
RT "Molecular cloning and characterization of the Candida albicans enolase
RT gene.";
RL J. Bacteriol. 175:2632-2639(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RX PubMed=1400228; DOI=10.1128/jb.174.21.6789-6799.1992;
RA Sundstrom P., Aliaga G.R.;
RT "Molecular cloning of cDNA and analysis of protein secondary structure of
RT Candida albicans enolase, an abundant, immunodominant glycolytic enzyme.";
RL J. Bacteriol. 174:6789-6799(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KEMH5;
RX PubMed=8359671; DOI=10.1111/j.1574-6968.1993.tb06368.x;
RA Franklyn K.M., Warmington J.R.;
RT "Cloning and nucleotide sequence analysis of the Candida albicans enolase
RT gene.";
RL FEMS Microbiol. Lett. 111:101-107(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11;
CC Evidence={ECO:0000269|PubMed:1400228};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; L04943; AAB46358.1; -; Genomic_DNA.
DR EMBL; M93712; AAA34341.1; -; mRNA.
DR EMBL; L10290; AAA71939.1; -; Genomic_DNA.
DR EMBL; CP017623; AOW26488.1; -; Genomic_DNA.
DR PIR; A40624; A40624.
DR RefSeq; XP_711883.1; XM_706790.2.
DR AlphaFoldDB; P30575; -.
DR SMR; P30575; -.
DR BioGRID; 1229577; 5.
DR STRING; 237561.P30575; -.
DR Allergome; 785; Cand a Enolase.
DR MoonDB; P30575; Curated.
DR MoonProt; P30575; -.
DR COMPLUYEAST-2DPAGE; P30575; -.
DR PRIDE; P30575; -.
DR ABCD; P30575; 3 sequenced antibodies.
DR GeneID; 3646493; -.
DR KEGG; cal:CAALFM_C108500CA; -.
DR CGD; CAL0000185645; ENO1.
DR VEuPathDB; FungiDB:C1_08500C_A; -.
DR eggNOG; KOG2670; Eukaryota.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; P30575; -.
DR OMA; EFMIIPV; -.
DR OrthoDB; 773373at2759; -.
DR UniPathway; UPA00109; UER00187.
DR PRO; PR:P30575; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005829; C:cytosol; IDA:CGD.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:CAFA.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0016020; C:membrane; IDA:CGD.
DR GO; GO:0005634; C:nucleus; IDA:CGD.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; ISS:CGD.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0030985; F:high molecular weight kininogen binding; IDA:CGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:CGD.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IDA:CGD.
DR GO; GO:0044409; P:entry into host; IPI:CGD.
DR GO; GO:0042730; P:fibrinolysis; IPI:CAFA.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IMP:CGD.
DR GO; GO:0006094; P:gluconeogenesis; ISS:CGD.
DR GO; GO:0006096; P:glycolytic process; IMP:CGD.
DR GO; GO:0044416; P:induction by symbiont of host defense response; IDA:CGD.
DR CDD; cd03313; enolase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR HAMAP; MF_00318; Enolase; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; PTHR11902; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR SFLD; SFLDF00002; enolase; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..440
FT /note="Enolase 1"
FT /id="PRO_0000134043"
FT ACT_SITE 213
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 376..379
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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
