PGKH_WHEAT
ID PGKH_WHEAT Reviewed; 480 AA.
AC P12782;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Phosphoglycerate kinase, chloroplastic;
DE EC=2.7.2.3;
DE Flags: Precursor;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Chinese Spring; TISSUE=Etiolated shoot;
RX PubMed=7770546; DOI=10.1104/pp.107.4.1483;
RA Jones P.G., Raines C., Lloyd J.C.;
RT "Nucleotide sequence of a wheat chloroplastic Phosphoglycerate kinase
RT gene.";
RL Plant Physiol. 107:1483-1484(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; X15233; CAA33303.1; -; mRNA.
DR EMBL; X73528; CAA51931.1; -; Genomic_DNA.
DR PIR; S05967; TVWTGC.
DR AlphaFoldDB; P12782; -.
DR SMR; P12782; -.
DR STRING; 4565.Traes_1AL_7C91EF27D.1; -.
DR PRIDE; P12782; -.
DR EnsemblPlants; TraesPAR_scaffold_028064_01G000200.1; TraesPAR_scaffold_028064_01G000200.1; TraesPAR_scaffold_028064_01G000200.
DR EnsemblPlants; TraesWEE_scaffold_026409_01G000400.1; TraesWEE_scaffold_026409_01G000400.1; TraesWEE_scaffold_026409_01G000400.
DR Gramene; TraesPAR_scaffold_028064_01G000200.1; TraesPAR_scaffold_028064_01G000200.1; TraesPAR_scaffold_028064_01G000200.
DR Gramene; TraesWEE_scaffold_026409_01G000400.1; TraesWEE_scaffold_026409_01G000400.1; TraesWEE_scaffold_026409_01G000400.
DR eggNOG; KOG1367; Eukaryota.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P12782; baseline and differential.
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; IBA:GO_Central.
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 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; Calvin cycle; Chloroplast; Kinase; Nucleotide-binding;
KW Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..?72
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?73..480
FT /note="Phosphoglycerate kinase, chloroplastic"
FT /id="PRO_0000023894"
FT BINDING 96..98
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 135..138
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 428..431
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 480 AA; 49840 MW; 3EBA1F378DAB16CC CRC64;
MASTAAPPAA LVARRAASAS VAAPLRGAGL AAGCQPARSL AFAAGADPRL AVHVASRCRA
ASAARGTRAV ATMAKKSVGD LTAADLEGKR VLVRADLNVP LDDNQNITDD TRIRAAIPTI
KYLLSNGAKV ILTSHLGRPK GVTPKFSLAP LVPRLSELLG IEVKKAEDVI GPEVEKLVAD
LANGAVLLLE NVRFYKEEEK NDPEFAKKLA SLADLFVNDA FGTAHRAHAS TEGVTKFLKP
SVAGFLLQKE LDYLDGAVSN PKRPFAAIVG GSKVSSKIGV IESLLEKCDI LLLGGGMIFT
FYKAQGLSVG SSLVEEDKLE LATSLLAKAK AKGVSLLLPS DVIIADKFAP DANSQTVPAS
AIPDGWMGLD IGPDSVKTFN DALDTTQTII WNGPMGVFEF DKFAVGTESI AKKLAELSKK
GVTTIIGGGD SVAAVEKVGV ADVMSHISTG GGASLELLEG KELPGVVALD EGVMTRSVTV
