KPYG_TOBAC
ID KPYG_TOBAC Reviewed; 562 AA.
AC Q40546;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Pyruvate kinase isozyme G, chloroplastic;
DE EC=2.7.1.40;
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. Petit Havana SR1; 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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- TISSUE SPECIFICITY: Highest levels in leaves. Also found in stems,
CC roots and flowers.
CC -!- DEVELOPMENTAL STAGE: Most abundantly expressed during the early
CC globular to early cotyledonary stages of embryo development.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR EMBL; Z28374; CAA82223.1; -; mRNA.
DR PIR; S44287; S44287.
DR RefSeq; NP_001313038.1; NM_001326109.1.
DR AlphaFoldDB; Q40546; -.
DR SMR; Q40546; -.
DR STRING; 4097.Q40546; -.
DR PRIDE; Q40546; -.
DR GeneID; 107822892; -.
DR KEGG; nta:107822892; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0009570; C:chloroplast stroma; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.40.1380.20; -; 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 PANTHER; PTHR11817; PTHR11817; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 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; Potassium; Pyruvate; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..562
FT /note="Pyruvate kinase isozyme G, chloroplastic"
FT /id="PRO_0000016664"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 123
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 306
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 562 AA; 61868 MW; D21D50204AA6A66E CRC64;
MATMNLPTGL HVAAKPASLD RLSSAKNVGD LFFSDSRHRK RVNTSNQIMA VQSLEHIHGV
NNNVYANYVN FNVPSSGYSL GQESVYLNSP RKTKIVCTIG PSTSSREMIW KLAEAGMNVA
RLNMSHGDHA SHQRTIDLVK EYNAQFEDKV IAIMLDTKGP EVISGDVPKP ILLKEGQEFN
FSIKRGVSTE DTVSVNYDDF INDVEAGDIL LVDGGMMSLA VKSKTSDIVK CEVIDGGELK
SRRHLNVRGK SATLPSITEK DWDDIKFGVN NQVDFYAVSF VKDAKVVHEL KDYLKSCNAD
IHVIVKIESA DSIPNLHSII SASDGAMVAR GDLGAELPIE EVPLLQEDII RRCQSMQKPV
IVATNMLESM IDHPTPTRAE VSDISIAVRE GADAVMLSGE TAHGKYPLKA VKVMHIVALR
TESSLQKSTS SPSQSAAYKS HMGEMFAFHS SSMANTLSTP IIVFTRTGSM AIILSHNRPS
STVFAFTNNE RVKQRLALYH GVVPIYMEFS SDAEETFSRA IKLLLSKSLV KDGQYVTLVQ
SGAQPIWRRH STHHIQVRKV QS
