ENO2_CANGA
ID ENO2_CANGA Reviewed; 437 AA.
AC Q6FQY4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Enolase 2;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase 2;
DE AltName: Full=2-phosphoglycerate dehydratase 2;
GN Name=ENO2; OrderedLocusNames=CAGL0I02486g;
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; CR380955; CAG60297.1; -; Genomic_DNA.
DR RefSeq; XP_447360.1; XM_447360.1.
DR AlphaFoldDB; Q6FQY4; -.
DR SMR; Q6FQY4; -.
DR STRING; 5478.XP_447360.1; -.
DR EnsemblFungi; CAG60297; CAG60297; CAGL0I02486g.
DR GeneID; 2889384; -.
DR KEGG; cgr:CAGL0I02486g; -.
DR CGD; CAL0130514; ENO1.
DR VEuPathDB; FungiDB:CAGL0I02486g; -.
DR eggNOG; KOG2670; Eukaryota.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; Q6FQY4; -.
DR OMA; EFMIIPV; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000002428; Chromosome I.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005829; C:cytosol; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; 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..437
FT /note="Enolase 2"
FT /id="PRO_0000134045"
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 437 AA; 46739 MW; D8DAE343A84EB6B1 CRC64;
MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGIHEALEMR DGDKSKWLGK
GVENAVKNVN DVIAPAFVKA NVDIKDQKAV DDLLLSLDGT ANKSKLGANA ILGVSMAAAR
AAAAEKNVPL YQHLADLSDS KTSPFVLPVP FLNVLNGGSH AGGALALQEF MIAPTGAKSF
REAMRIGSEV YHNLKSLTKK RYGSSAGNVG DEGGVAPDIQ TAEEALDLIV DAIKAAGHEG
KVKIGLDCAS SEFFKDGKYD LDFKNPNSDA SKWLSGPQLA DLYHSLVKKY PIVSIEDPFA
EDDWEAWSHF FKTAGVQIVA DDLTVTNPKR IATAIEKKAA DALLLKVNQI GSLSESIKAA
QDSFAAGWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA PARSERLAKL NQLLRIEEEL
GDKAVYAGDN FHHGFKL
