ID   PGKH_SPIOL              Reviewed;         433 AA.
AC   P29409;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   08-NOV-2023, entry version 100.
DE   RecName: Full=Phosphoglycerate kinase, chloroplastic;
DE            EC=2.7.2.3;
DE   Flags: Precursor; Fragment;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seedling;
RX   PubMed=8290635; DOI=10.1104/pp.103.4.1449;
RA   Bertsch U., Schlicher T.B., Schroeder I., Soll J.;
RT   "Sequence of mature phosphoglycerate kinase from spinach chloroplasts.";
RL   Plant Physiol. 103:1449-1450(1993).
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 biosynthesis; Calvin cycle.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; X68430; CAA48479.1; -; mRNA.
DR   PIR; S26623; S26623.
DR   AlphaFoldDB; P29409; -.
DR   SMR; P29409; -.
DR   BioCyc; MetaCyc:MONOMER-12711; -.
DR   SABIO-RK; P29409; -.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP001155700; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 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; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 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   2: Evidence at transcript level;
KW   ATP-binding; Calvin cycle; Chloroplast; Kinase; Nucleotide-binding;
KW   Plastid; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         <1..28
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..433
FT                   /note="Phosphoglycerate kinase, chloroplastic"
FT                   /id="PRO_0000023891"
FT   BINDING         52..54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         91..94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         355
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         384..387
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   433 AA;  45573 MW;  D57AE12AA53099F9 CRC64;
     GASFSLHVLS KINSYKSQST KPIRGVASMA KKSVGDLTSA DLKGKKVFVR ADLNVPLDDS
     QNITDDTRIR AAIPTIKHLI NNGAKVILSS HLGRPKGVTP KFSLAPLVPR LSELLGLQVV
     KADDCIGPDV EKLVAELPEG GVLLLENVRF YKEEEKNDPE FAKKLASLAD LYVNDAFGTA
     HRAHASTEGV TKFLKPSVAG FLLQKELDYL VGAVSNPKRP FAAIVGGSKV SSKIGVIESL
     LEKCDILLLG GGMIFTFYKA QGMSVGSSLV EEDKLDLATS LLAKAKEKGV SLLLPTDVVI
     ADKFAADADS KIVPASGIPD GWMGLDIGPD SIKTFSEALD TTQTVIWNGP MGVFEFEKFA
     AGTEAIAKKL EEISKKGATT IIGGGDSVAA VEKVGVAEAM SHISTGGGAS LELLEGKQLP
     GVLALNEADP VPV
//