PGK_SCHPO
ID PGK_SCHPO Reviewed; 414 AA.
AC O60101;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk1; ORFNames=SPBC14F5.04c;
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 [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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-75; SER-76; SER-143; SER-172;
RP SER-173; SER-183; SER-253; SER-260; THR-299; SER-328; SER-351; THR-373;
RP SER-387; SER-390; SER-412 AND SER-413, 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)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA19322.1; -; Genomic_DNA.
DR PIR; T39450; T39450.
DR RefSeq; NP_596730.1; NM_001022656.2.
DR AlphaFoldDB; O60101; -.
DR SMR; O60101; -.
DR BioGRID; 276315; 11.
DR IntAct; O60101; 2.
DR MINT; O60101; -.
DR STRING; 4896.SPBC14F5.04c.1; -.
DR iPTMnet; O60101; -.
DR MaxQB; O60101; -.
DR PaxDb; O60101; -.
DR PRIDE; O60101; -.
DR EnsemblFungi; SPBC14F5.04c.1; SPBC14F5.04c.1:pep; SPBC14F5.04c.
DR GeneID; 2539764; -.
DR KEGG; spo:SPBC14F5.04c; -.
DR PomBase; SPBC14F5.04c; pgk1.
DR VEuPathDB; FungiDB:SPBC14F5.04c; -.
DR eggNOG; KOG1367; Eukaryota.
DR HOGENOM; CLU_025427_0_2_1; -.
DR InParanoid; O60101; -.
DR OMA; DMIFDIG; -.
DR PhylomeDB; O60101; -.
DR Reactome; R-SPO-70171; Glycolysis.
DR Reactome; R-SPO-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00185.
DR PRO; PR:O60101; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISO:PomBase.
DR GO; GO:0061621; P:canonical glycolysis; ISO:PomBase.
DR GO; GO:0006094; P:gluconeogenesis; ISO:PomBase.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 3.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..414
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145889"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 63..66
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 370..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 75
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 299
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 373
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 414 AA; 43964 MW; F40D706D5487EB4E CRC64;
MSLSTKLAIT DVDLKGKNVL IRVDFNVPLD GDRITNNARI VGALPTIKYA LEQQPKAVIL
MSHLGRPNGA RVAKYSLKPV AAELSKLLGK PVKFLDDCVG PEVEKACKEA KGGEVILLEN
LRFHIEEEGS AKVDGKKVKA DASAVEAFRK SLTSLGDIFV NDAFGTAHRA HSSMVGVDLP
RVSGFLMKKE LDYFSKALEN PARPFLAILG GAKVADKIQL IDNLLDKVNR LIICGGMAFT
FLKVLNGMKI GDSLFDEAGS KNVESMMAKA KKNNVEVFLP VDFVTADKFD KDAKVGSATA
EEGIPDGWMG LDCGPKSSAK FAEVITTSKT IVWNGPAGVF EFDNFAKGTK SMLDACVKTC
EAGNVVIVGG GDTATVAKKY GKEDALSHVS TGGGASLELL EGKALPGVVA LSSK
