ID   KPYA_TOBAC              Reviewed;         593 AA.
AC   Q40545;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=Pyruvate kinase isozyme A, 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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- TISSUE SPECIFICITY: Highest levels in roots. Also found in stems,
CC       leaves 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; Z28373; CAA82222.1; -; mRNA.
DR   PIR; S51946; S51946.
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         ?    593       Pyruvate kinase isozyme A, chloroplastic.
FT                                /FTId=PRO_0000016663.
FT   ACT_SITE    341    341       By similarity.
FT   METAL       343    343       Magnesium (Potential).
FT   METAL       364    364       Magnesium (Potential).
FT   METAL       365    365       Magnesium (Potential).
SQ   SEQUENCE   593 AA;  65228 MW;  FAF049E193C1D484 CRC64;
     MSQALNFFVS SSSRSPATFT ISRPSVFPST GSLRLLVKKS LRTLVVEASS AAASDLDEPQ
     SSPVLVSENG SGGVLSSATQ EYGRNAAPGT DSSSIEVDTV TEAELKENGF RSTRRTKLIC
     TIGPATCGFE QLERLAEGGM NVARINMCHG TREWHRMVIE RLRRLNEEKG FAVAIMMDTE
     GSEIHMGDLG GASSAKAEDG EIWNFTVRSF DPPLPERTVT VNYDGFAEDV KVGDELLVDG
     GMVRFEVIEK IGPDVKCLCT DPGLLLPRAN LTFWRDGKLV RERNAMLPTI SSKDWLDIDF
     GIAEGVDFIA VSFVKSAEVI KHLKSYIQAR ARDSDISVIA KIESIDSLKN LEEIIQASDG
     AMVARGDLGA QIPLEQVPSE QQKIVQICRQ LNRPVIVASQ LLESMIEYPI PTRAEVADVS
     EAVRQRGDAL MLSGESAMGQ FPEKALTVLR SVSLRIERMW REQKRHEVIE LPSIASSFSD
     SISEEICNSA AKMANNLEVD ALFVYTKNGH MASLLSRCRP DCPIFAFTTT TSVRRRLNLQ
     WGLMPFRLSF SDDMESNLNK TFSLLKARGM IKSGDLIIAV SDMLQSIQVM NVP
//