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 24-JAN-2024, entry version 151. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 284812.O60101; -. DR iPTMnet; O60101; -. DR MaxQB; O60101; -. DR PaxDb; 4896-SPBC14F5-04c-1; -. 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd00318; Phosphoglycerate_kinase; 1. DR Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 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; PHOSPHOGLYCERATE KINASE; 1. DR PANTHER; PTHR11406:SF0; PHOSPHOGLYCERATE KINASE; 1. DR Pfam; PF00162; PGK; 1. DR PIRSF; PIRSF000724; Pgk; 1. DR PRINTS; PR00477; PHGLYCKINASE. DR SUPFAM; SSF53748; Phosphoglycerate kinase; 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 //