ID   KPYK_CORGL              Reviewed;         475 AA.
AC   Q46078;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 64.
DE   RecName: Full=Pyruvate kinase;
DE            Short=PK;
DE            EC=2.7.1.40;
GN   Name=pyk; OrderedLocusNames=Cgl2089, cg2291;
OS   Corynebacterium glutamicum (Brevibacterium flavum).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1718;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX   MEDLINE=94354663; PubMed=8074528;
RA   Jetten M.S., Gubler M.E., Lee S.H., Sinskey A.J.;
RT   "Structural and functional analysis of pyruvate kinase from
RT   Corynebacterium glutamicum.";
RL   Appl. Environ. Microbiol. 60:2501-2507(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RA   Nakagawa S.;
RT   "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   MEDLINE=22830012; PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
RA   Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
RA   Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
RA   McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
RA   Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
RA   Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence
RT   and its impact on the production of L-aspartate-derived amino acids
RT   and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC   -!- COFACTOR: Magnesium.
CC   -!- COFACTOR: Potassium.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family.
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DR   EMBL; L27126; AAA56793.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB99482.1; -; Genomic_DNA.
DR   EMBL; BX927154; CAF20425.1; ALT_INIT; Genomic_DNA.
DR   PIR; I40840; I40840.
DR   RefSeq; NP_601288.2; -.
DR   RefSeq; YP_226326.1; -.
DR   HSSP; P14178; 1E0T.
DR   World-2DPAGE; 0001:Q46078; -.
DR   PRIDE; Q46078; -.
DR   GeneID; 1020040; -.
DR   GeneID; 3344974; -.
DR   GenomeReviews; BA000036_GR; Cgl2089.
DR   GenomeReviews; BX927147_GR; cg2291.
DR   KEGG; cgb:cg2291; -.
DR   KEGG; cgl:NCgl2008; -.
DR   HOGENOM; Q46078; -.
DR   OMA; Q46078; ATESGYT.
DR   BioCyc; CGLU196627-1:CG2291-MON; -.
DR   BRENDA; 2.7.1.40; 812.
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   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   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Pyruvate; Transferase.
FT   CHAIN         1    475       Pyruvate kinase.
FT                                /FTId=PRO_0000112068.
FT   ACT_SITE    218    218       By similarity.
FT   METAL       220    220       Magnesium (By similarity).
FT   METAL       241    241       Magnesium (By similarity).
FT   METAL       242    242       Magnesium (By similarity).
SQ   SEQUENCE   475 AA;  51471 MW;  4E56A16C570A5386 CRC64;
     MDRRTKIVCT LGPAVASADG ILRLVEDGMD VARLNFSHGD HPDHEQNYKW VREAAEKTGR
     AVGILADLQG PKIRLGRFTD GATVWENGET IRITVDDVEG THDRVSTTYK NLAKDAKPGD
     RLLVDDGKVG LVCVSVEGND VICEVVEGGP VSNNKGVSLP GMDISVPALS EKDIRDLRFA
     LKLGVDFIAL SFVRSPADAE LVHKIMDEEG RRVPVIAKLE KPEAVTSLEP IVLAFDAVMV
     ARGDLGVEVP LEEVPLVQKR AIQIARENAK PVIVATQMLD SMIENSRPTR AEASDVANAV
     LDGADAVMLS GETSVGKDPH NVVRTMSRIV RFAETDGRVP DLTHIPRTKR GVISYSARDI
     AERLNARALV AFTTSGDTAK RVARLHSHLP LLVFTPNEAV RSELALTWGA TTFLCPPVSD
     TDDMMREVDR ALLAMPEYNK GDMMVVVAGS PPGVTGNTNM IHVHLLGDDT RIAKL
//