PGKH_CHLRE
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 03-AUG-2022, entry version 95.
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 STRING; 3055.EDO98586; -.
DR PRIDE; P41758; -.
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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
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 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