ID   KPYC_TOBAC              Reviewed;         508 AA.
AC   Q42954;
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, cytosolic isozyme;
DE            Short=PK;
DE            EC=2.7.1.40;
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].
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: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family.
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DR   EMBL; Z29492; CAA82628.1; -; mRNA.
DR   PIR; S41379; S41379.
DR   HSSP; P14178; 1E0T.
DR   BRENDA; 2.7.1.40; 298.
DR   GO; GO:0005737; C:cytoplasm; 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; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Pyruvate; Transferase.
FT   CHAIN         1    508       Pyruvate kinase, cytosolic isozyme.
FT                                /FTId=PRO_0000112127.
FT   ACT_SITE    238    238       By similarity.
FT   METAL       240    240       Magnesium (Potential).
FT   METAL       261    261       Magnesium (Potential).
FT   METAL       262    262       Magnesium (Potential).
SQ   SEQUENCE   508 AA;  55133 MW;  A8FC5DA9D7CB9989 CRC64;
     MAIENNNNGV NFCTVKRPKT KIVCTLGPAS RSVPMIEKLL RAGMNVARFN FSHGSHDYHQ
     ETIDNLRQAM ESTGILCAVM LDTKGPEIRT GFLKDAKPVQ LKQGQEITIS TDYSIKGDES
     MICMSYKKLA EDVKPQSVIL CADGQITFTV LSCDKENGLD RCRCENTAVL GERKNVNLPG
     VIVDLPTLTD KDKDDILNWG VPNHIDMIAL SFVRKGSDLV EVRKLLGEHA KNILLMSKVE
     NQEGVANFDD ILLNSDAFMV ARGDLGMEIP IEKIFLAQKV MIYKCNIQGK PVVTATQMLE
     SMIKSPRPTR AEATDVANAV LDGTDCVMLS GETAAGAYPD LAVGTMAKIC IEAESTIDYP
     DVFKRIMSNA PVPMSPLESL ASSAVRTANS AKAALILVLT RGGSTAKLVA KYRPGMPILS
     VVVPEIKTDS FDWTCSDESP ARHSLIFRGL VPVLHAGSAR ASHEESTEEA LDFALQHAKT
     KGLCKQGDSV VALHRVGTAS VIKIVTVK
//