ID   PGKH_CHLRE              Reviewed;         461 AA.
AC   P41758;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   24-JAN-2024, entry version 101.
DE   RecName: Full=Phosphoglycerate kinase, chloroplastic;
DE            EC=2.7.2.3;
DE   Flags: Precursor;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=7724671; DOI=10.1104/pp.107.2.393;
RA   Kitayama M., Togasaki R.K.;
RT   "Purification and cDNA isolation of chloroplastic phosphoglycerate kinase
RT   from Chlamydomonas reinhardtii.";
RL   Plant Physiol. 107:393-400(1995).
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; U14912; AAA70082.1; -; mRNA.
DR   PIR; T08041; T08041.
DR   AlphaFoldDB; P41758; -.
DR   SMR; P41758; -.
DR   PaxDb; 3055-EDO98586; -.
DR   ProMEX; P41758; -.
DR   eggNOG; KOG1367; Eukaryota.
DR   UniPathway; UPA00116; -.
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   1: Evidence at protein level;
KW   ATP-binding; Calvin cycle; Chloroplast; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Plastid; Transferase; Transit peptide.
FT   TRANSIT         1..60
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           61..461
FT                   /note="Phosphoglycerate kinase, chloroplastic"
FT                   /id="PRO_0000023890"
FT   BINDING         83..85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         123..126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         357
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         388
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         417..420
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   461 AA;  49008 MW;  BA886FDD9E4DCCB9 CRC64;
     MALSMKMRAN ARVSGRRVAA VAPRVVPFSS ASSSVLRSGF ALRCLWTSAA WAALASVVEA
     VKKSVGDLHK ADLEGKRVFV RADLNVPLDK ATLAITDDTR IRAAVPTLKY LLDNGAKVLL
     TSHLGRPKGG PEDKYRLTPV VARLSELLGK PVTKVDDCIG PEVEKAVGAM KNGELLLLEN
     CRFYKEEEKN EPEFAKKLAA NADLYVNDAF GTAHRAHAST EGVTKFLKPS VAGFLLQKEL
     DYLDGAVSNP KRPFVAIVGG SKVSSKITVI EALMEKCDKI IIGGGMIFTF YKARALKVGS
     SLVEDDKIEL AKKLEEMAKA KGVQLLLPTD VVVADKFDAN ANTQTVPITA IPDGWMGLDI
     GPDSVKTFND ALADAKTVVW NGPMGVFEFP QVRQRTVSIA NTLAGLTPKG CITIIGGGDS
     VAAVEQAGVA EKMSHISTGG GASLELLEGK VLPGVAALDE K
//