ID   KPYK_BUCAP              Reviewed;         481 AA.
AC   Q8K9M3;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 44.
DE   RecName: Full=Pyruvate kinase;
DE            Short=PK;
DE            EC=2.7.1.40;
GN   Name=pykA; OrderedLocusNames=BUsg_311;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- COFACTOR: Potassium (By similarity).
CC   -!- ENZYME REGULATION: Allosterically activated by AMP and by several
CC       sugar phosphates. Belongs to type II PK (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family.
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DR   EMBL; AE013218; AAM67865.1; -; Genomic_DNA.
DR   RefSeq; NP_660654.1; -.
DR   HSSP; P14178; 1E0T.
DR   GeneID; 1005515; -.
DR   GenomeReviews; AE013218_GR; BUsg_311.
DR   KEGG; bas:BUsg311; -.
DR   HOGENOM; Q8K9M3; -.
DR   OMA; Q8K9M3; RMIKLAR.
DR   BioCyc; BAPH198804:BUSG311-MON; -.
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   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Pyruvate; Transferase.
FT   CHAIN         1    481       Pyruvate kinase.
FT                                /FTId=PRO_0000112059.
FT   ACT_SITE    223    223       By similarity.
FT   METAL       225    225       Magnesium (By similarity).
FT   METAL       249    249       Magnesium (By similarity).
FT   METAL       250    250       Magnesium (By similarity).
SQ   SEQUENCE   481 AA;  52632 MW;  8A11ECA79EAB8A3B CRC64;
     MLNRVRRTKI VATLGPSTDK ANNLEKIILS GANVLRLNFS HGSSEEHKKR AKKAKEIMFK
     LNCHIALLGD LQGPKIRISK FKKNSIFLKV NDVFILDANL NEKNGNNERV GIDYKKLPND
     LNVNDILLLD DGRIQLKVIK IEKCAIFTKV IIGGILSNNK GINKLGGGLS ADALTEKDKK
     DIILASEIDV DYLAVSFPRC ADDLIKAREL LKKSGSNAQI IAKIERAEAV FDQNAIENII
     LSSDAIMIAR GDLGVEIGDA ELVGIQKKLI RTARKLNKVA ITATQMMESM ILNPLPTRAE
     VMDVANAVLD GSDAVMLSAE TASGKYPSET VISMAKVCKG AEKVPSINVS RHRLNVEFQS
     IEEAIAMSSM YAANHLKGIT AIITMTESGK TALMTSRITS GLPIFALSKH KKTLNLTALY
     RGVIPIYFDS DKDGVEAANE AIILLCKKKF LFNNDLVIVT QGDIMGKIGK TNTSRILRVT
     Y
//