ID   KPYG_RICCO              Reviewed;         418 AA.
AC   P55964;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 108.
DE   RecName: Full=Pyruvate kinase isozyme G, chloroplastic;
DE            EC=2.7.1.40;
DE   Flags: Fragment;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Baker 296; TISSUE=Seed;
RX   PubMed=7865798; DOI=10.1007/bf00019180;
RA   Blakeley S.D., Gottlob-Mchugh S., Wan J., Crews L., Miki B., Ko K.,
RA   Dennis D.T.;
RT   "Molecular characterization of plastid pyruvate kinase from castor and
RT   tobacco.";
RL   Plant Mol. Biol. 27:79-89(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC         EC=2.7.1.40;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- TISSUE SPECIFICITY: Expressed in developing and germinating endosperm
CC       and in roots.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR   AlphaFoldDB; P55964; -.
DR   SMR; P55964; -.
DR   eggNOG; KOG2323; Eukaryota.
DR   UniPathway; UPA00109; UER00188.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR   Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1.
DR   InterPro; IPR001697; Pyr_Knase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   InterPro; IPR018209; Pyrv_Knase_AS.
DR   InterPro; IPR015793; Pyrv_Knase_brl.
DR   InterPro; IPR015795; Pyrv_Knase_C.
DR   InterPro; IPR036918; Pyrv_Knase_C_sf.
DR   InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR   NCBIfam; TIGR01064; pyruv_kin; 1.
DR   PANTHER; PTHR11817:SF63; PLASTIDIAL PYRUVATE KINASE 3, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR   SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chloroplast; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Plastid; Pyruvate; Transferase.
FT   CHAIN           <1..418
FT                   /note="Pyruvate kinase isozyme G, chloroplastic"
FT                   /id="PRO_0000112126"
FT   BINDING         14
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         15
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         165
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            163
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   418 AA;  46007 MW;  D22531C1B25ECF85 CRC64;
     NAQSHDNVVS IMLDTKGPEV RSGDVPQPML KEGQEFNPTI RRGVSTQDTV SVNYDDFVND
     VVVGDILLVD GGMMSLAVKS KTSDLVKCVV VDGGELKSRR HLNVRGKSAR LPSITDKDWG
     DIKFGVDNQV DFYAVSFVKD AKVVHELKEY LKRCNADIHV IVKIESADSI PNLHSIISAS
     DGAMVARGDL GAELPIEEVP LLQEDIIRRC HSMQKPVIVA TNMLESMINH PTPTRAEVSD
     IAIAVREGAD AVMLSGETAH GKYPLKAVRV MHTVALRTES SSPVNTTPPA QGAYKGHMGE
     MFAFHATIMA NTLNTPIIVF TRTGSMAVLL SHYQPASTIF AFTNEERIKQ RLSLYRGVMP
     IYMEFSSDAE ETFSRALQLL LNKGLLVEGE HVTLVQSGAQ PIWRQESTHH IQVRKVQN
//