ENO11_SCHPO
ID ENO11_SCHPO Reviewed; 439 AA.
AC P40370; Q12703; Q9Y7J7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Enolase 1-1;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase 1-1;
DE AltName: Full=2-phosphoglycerate dehydratase 1-1;
GN Name=eno101; Synonyms=eno1; ORFNames=SPBC1815.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7867936; DOI=10.1016/0378-1119(94)00877-u;
RA Jackson J.C., Lopes J.M.;
RT "A cDNA from Schizosaccharomyces pombe encoding a putative enolase.";
RL Gene 154:109-113(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Park S.-K.;
RT "Cloning of enolase gene of S. pombe.";
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX 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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85; SER-249; SER-250;
RP TYR-253; SER-351; THR-353; SER-355 AND SER-421, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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; U13799; AAA70080.1; -; mRNA.
DR EMBL; L37084; AAA51399.2; -; mRNA.
DR EMBL; CU329671; CAB43486.1; -; Genomic_DNA.
DR PIR; JC4036; JC4036.
DR PIR; T39737; T39737.
DR PIR; T45116; T45116.
DR RefSeq; NP_595903.1; NM_001021810.2.
DR AlphaFoldDB; P40370; -.
DR SMR; P40370; -.
DR BioGRID; 276332; 13.
DR IntAct; P40370; 5.
DR MINT; P40370; -.
DR STRING; 4896.SPBC1815.01.1; -.
DR iPTMnet; P40370; -.
DR MaxQB; P40370; -.
DR PaxDb; P40370; -.
DR PRIDE; P40370; -.
DR EnsemblFungi; SPBC1815.01.1; SPBC1815.01.1:pep; SPBC1815.01.
DR GeneID; 2539782; -.
DR KEGG; spo:SPBC1815.01; -.
DR PomBase; SPBC1815.01; eno101.
DR VEuPathDB; FungiDB:SPBC1815.01; -.
DR eggNOG; KOG2670; Eukaryota.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; P40370; -.
DR OMA; EFMIIPV; -.
DR PhylomeDB; P40370; -.
DR Reactome; R-SPO-70171; Glycolysis.
DR Reactome; R-SPO-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00187.
DR PRO; PR:P40370; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; ISM:PomBase.
DR GO; GO:0061621; P:canonical glycolysis; ISM:PomBase.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..439
FT /note="Enolase 1-1"
FT /id="PRO_0000134058"
FT ACT_SITE 211
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 372..375
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 253
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 353
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 13..15
FT /note="DSR -> ALG (in Ref. 1; AAA70080)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="H -> Q (in Ref. 1; AAA70080)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="A -> T (in Ref. 1; AAA70080)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="A -> V (in Ref. 1; AAA70080)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="E -> G (in Ref. 1; AAA70080)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="E -> R (in Ref. 1; AAA70080)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 47436 MW; 4CA257CFF4B456E3 CRC64;
MAIQKVFARQ IYDSRGNPTV EVDLTTETGI HRAIVPSGAS TGIWEALEMR DGDKTKWGGK
GVLKAVGNVN NIIAPAVVKA NLDVTDQKAA DEFLLKLDGT ENKSKLGANA ILGVSMAICR
AGAAQKKLPL WKYIAENFGT KGPYVLPVPS FNVLNGGSHA GGDLAFQEFM ILPTGAPSFS
EAMRWGAETY HTLKSIAKKR YGSSAGNVGD EGGIAPDLQT PQEALDLIVE AINKAGYEGK
IKIGLDVASS EFYVDGKYDL DIKAAKPKPE NKLTYQQLTD LYVELSKKYP IVSIEDPFDQ
DDWSAWTHMK AETDFQIVGD DLTVTNVKRL RTAIDKKCAN ALLLKVNQIG SVTESLNAVR
MSYEAGWGVM VSHRSGETAD TFISHLTVGI GAGQLKSGAP CRSERLAKYN ELLRIEEELG
SEGVYAGAHA GKYIKAAKF
