PGKH_TOBAC
ID PGKH_TOBAC Reviewed; 481 AA.
AC Q42961;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Phosphoglycerate kinase, chloroplastic;
DE EC=2.7.2.3;
DE Flags: Precursor;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Samsun; TISSUE=Leaf;
RA Rao S.K., Bringloe D.H., Dyer T.A., Raines C.A., Bradbeer J.W.;
RT "Nucleotide sequences of cDNAs encoding the chloroplastic and cytosolic
RT phosphoglycerate kinases from tobacco.";
RL (er) Plant Gene Register PGR95-090(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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; Z48977; CAA88841.1; -; mRNA.
DR PIR; T03660; T03660.
DR AlphaFoldDB; Q42961; -.
DR SMR; Q42961; -.
DR STRING; 4097.Q42961; -.
DR PRIDE; Q42961; -.
DR ProMEX; Q42961; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000084051; 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; 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; -; 3.
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..75
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 76..481
FT /note="Phosphoglycerate kinase, chloroplastic"
FT /id="PRO_0000023892"
FT BINDING 99..101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 138..141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 431..434
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 481 AA; 50177 MW; 7AA497C747D0716D CRC64;
MASATASHTL CGIPATSSST TNKAIAPSSA RFLAKTPLRR LGFAGAAADS LFTNHVATKL
RSLKSSSKPI RGVASMAKKS VGDLTAAELK GKKVFVRADL NVPLDDNQNI TDDTRIRAAV
PTIKHLMANG AKVILSSHLG RPKGVTPKYS LAPLVPRLSE LLGIQVVKVE DCIGPEVEKL
VASLPEGGVL LLENVRFYKE EEKNEPEFAK KLASLADLYV NDAFGTAHRA HASTEGVTKF
LKPSVAGFLL QKELDYLVGA VSNPKRPFAA IVGGSKVSSK IGVIESLLEK CDILLLGGGM
IFTFYKAQGL SVGSSLVEED KLELATSLLE KAKAKGVSLL LPSDVVIADK FAPDANSKIV
PASAIPDGWM GLDIGPDSVK TFNDALDTTK TVIWNGPMGV FEFDKFAVGT EAIAKKLADL
SGKGVTTIIG GGDSVAAVEK VGVASVMSHI STGGGASLEL LEGKVLPGVI ALDEADAPVA
V