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   16-JUN-2009, entry version 61.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
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   MEDLINE=95170010; 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: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- COFACTOR: Potassium (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SUBUNIT: Homotetramer (By similarity).
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.
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DR   EMBL; Z28374; CAA82223.1; -; mRNA.
DR   PIR; S44287; S44287.
DR   HSSP; P14178; 1E0T.
DR   BRENDA; 2.7.1.40; 298.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   GO; GO:0004743; F:pyruvate kinase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001697; Pyr_Knase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase_cat.
DR   InterPro; IPR015794; Pyrv_Knase_a/b.
DR   InterPro; IPR018209; Pyrv_Knase_AS.
DR   InterPro; IPR015793; Pyrv_Knase_brl.
DR   Gene3D; G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.
DR   Gene3D; G3DSA:3.40.1380.20; Pyrv_Knase_a/b; 1.
DR   PANTHER; PTHR11817; Pyruvate_kinase; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   ProDom; PD001009; Pyruvate_kinase; 2.
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;
KW   Metal-binding; Nucleotide-binding; Plastid; Pyruvate; Transferase;
KW   Transit peptide.
FT   TRANSIT       1      ?       Chloroplast (Potential).
FT   CHAIN         ?    562       Pyruvate kinase isozyme G, chloroplastic.
FT                                /FTId=PRO_0000016664.
FT   ACT_SITE    306    306       By similarity.
FT   METAL       308    308       Magnesium (Potential).
FT   METAL       329    329       Magnesium (Potential).
FT   METAL       330    330       Magnesium (Potential).
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
//