ID   PGKY_WHEAT              Reviewed;         401 AA.
AC   P12783;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Phosphoglycerate kinase, cytosolic;
DE            EC=2.7.2.3;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Mardler; TISSUE=Leaf;
RX   PubMed=2780287; DOI=10.1093/nar/17.16.6569;
RA   Longstaff M., Raines C.A., McMorrow E.M., Bradbeer J.W., Dyer T.A.;
RT   "Wheat phosphoglycerate kinase: evidence for recombination between the
RT   genes for the chloroplastic and cytosolic enzymes.";
RL   Nucleic Acids Res. 17:6569-6580(1989).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; X15232; CAA33302.1; -; mRNA.
DR   PIR; S05966; TVWTGY.
DR   AlphaFoldDB; P12783; -.
DR   SMR; P12783; -.
DR   STRING; 4565.Traes_6DS_CDB16CE3F.1; -.
DR   PRIDE; P12783; -.
DR   EnsemblPlants; TraesCS6B02G187500.2; TraesCS6B02G187500.2; TraesCS6B02G187500.
DR   Gramene; TraesCS6B02G187500.2; TraesCS6B02G187500.2; TraesCS6B02G187500.
DR   eggNOG; KOG1367; Eukaryota.
DR   OMA; SCKFAFG; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P12783; baseline.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; -; 2.
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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..401
FT                   /note="Phosphoglycerate kinase, cytosolic"
FT                   /id="PRO_0000145872"
FT   BINDING         25..27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         64..67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         328
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         357..360
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   401 AA;  42122 MW;  DF35346175CEB3F2 CRC64;
     MATKRSVGTL GEADLKGKKV FVRADLNVPL DDAQKITDDT RIRASIPTIK YLLEKGAKVI
     LASHLGRPKG VTPKFSLKPL VARLSELLGL EVVMAPDCIG EEVEKLAAAL PDGGVLLLEN
     VRFYKEEEKN DPEFAKKLAS VADLYVNDAF GTAHRAHAST EGVTKFLRPS VAGFLMQKEL
     DYLVGAVANP KKPFAAIVGG SKVSSKIGVI ESLLAKVDIL ILGGGMIFTF YKAQGLAVGK
     SLVEEDKLEL ATSLIETAKS KGVKLLLPTD VVVADKFAAD AESKIVPATA IPDGWMGLDV
     GPDSIKTFAE ALDTTKTVIW NGPMGVFEFE KFAAGTDAIA KQLAELTGKG VTTIIGGGDS
     VAAVEKAGLA DKMSHISTGG GASLELLEGK PLPGVLALDE A