ENO1_CANGA
ID ENO1_CANGA Reviewed; 438 AA.
AC Q6FTW6;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Enolase 1;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase 1;
DE AltName: Full=2-phosphoglycerate dehydratase 1;
GN Name=ENO1; OrderedLocusNames=CAGL0F08261g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.
CC {ECO:0000250};
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; CR380952; CAG59252.1; -; Genomic_DNA.
DR RefSeq; XP_446328.1; XM_446328.1.
DR AlphaFoldDB; Q6FTW6; -.
DR SMR; Q6FTW6; -.
DR STRING; 5478.XP_446328.1; -.
DR PRIDE; Q6FTW6; -.
DR EnsemblFungi; CAG59252; CAG59252; CAGL0F08261g.
DR GeneID; 2887972; -.
DR KEGG; cgr:CAGL0F08261g; -.
DR CGD; CAL0131204; CAGL0F08261g.
DR VEuPathDB; FungiDB:CAGL0F08261g; -.
DR eggNOG; KOG2670; Eukaryota.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; Q6FTW6; -.
DR OMA; KHADNGI; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..438
FT /note="Enolase 1"
FT /id="PRO_0000134044"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 346
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 373..376
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 438 AA; 47282 MW; A5C39636C234E43E CRC64;
MSVTKVHART VYDSRGNPTV EVEVYTKDGM FRAIVPSGAS TGSHEALELR DGDKSKWEGK
GVTKAVSNVN DIIGPKLIES KLDVKDQKAI DEFMIKLDGT KNKSKLGANA ILGVSLAVAR
AGAAAKGVPL YQHIAELADM KKEPYVIPCP FFNVLNGGVH AGGNLALQEF LIAPVGAESF
HEALRLGSEV YHKLKALAKK RIGSSAGNVG DEGGIAPSLS TPFEALDLIY DAIKEAGHEG
KVKIAMDPAS SEFFQGDKYD LDFKNPHPDA KNKLSGAQLG DYYKTILEKY PIVSLEDPFA
EDDWEAWTNF FPKAGVQIIA DDLTVTNPER IQTAIDKKTA DCLLLKVNQI GSLTESINSA
KLAYGAGWGV QVSHRSGETE DTFIADLVVG LRTGQIKSGS LARSERLAKW NQILRIEEEL
GASNTIFAGA KFHKGQLL
