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 04-NOV-2026, entry version 109. DE RecName: Full=Phosphoglycerate kinase, chloroplastic; DE EC=2.7.2.3 {ECO:0000250|UniProtKB:P00558}; DE Flags: Precursor; Fragment; OS Spinacia oleracea (Spinach). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Caryophyllales; Amaranthaceae; 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 Evidence={ECO:0000250|UniProtKB:P00558}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P00558}; 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}. 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; 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; UP000813463; Unplaced. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. 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; ISS:UniProtKB. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway. DR CDD; cd00318; Phosphoglycerate_kinase; 1. DR FunFam; 3.40.50.1260:FF:000003; Phosphoglycerate kinase; 1. DR FunFam; 3.40.50.1260:FF:000006; 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; Magnesium; Metal-binding; KW Nucleotide-binding; Plastid; Reference proteome; Transferase; KW 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 51 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 52 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 54 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 68 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 90 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 91 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 93 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 94 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 149 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 181 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 182 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 227 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 227 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 229 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 233 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 233 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 251 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 251 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 252 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 252 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 324 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 324 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 349 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 354 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 354 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 355 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 355 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 386 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 386 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 387 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" 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 //