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Database: UniProt/TrEMBL
Entry: B7L7Q7_ECO55
LinkDB: B7L7Q7_ECO55
Original site: B7L7Q7_ECO55 
ID   B7L7Q7_ECO55            Unreviewed;       480 AA.
AC   B7L7Q7;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   11-JUN-2014, entry version 42.
DE   RecName: Full=Pyruvate kinase;
DE            EC=2.7.1.40;
GN   Name=pykA; OrderedLocusNames=EC55989_2033;
OS   Escherichia coli (strain 55989 / EAEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55989 / EAEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA   Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA   Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA   Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA   Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA   Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA   Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family.
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DR   EMBL; CU928145; CAU97891.1; -; Genomic_DNA.
DR   RefSeq; YP_002403087.1; NC_011748.1.
DR   ProteinModelPortal; B7L7Q7; -.
DR   STRING; 585055.EC55989_2033; -.
DR   EnsemblBacteria; CAU97891; CAU97891; EC55989_2033.
DR   GeneID; 7148548; -.
DR   KEGG; eck:EC55989_2033; -.
DR   PATRIC; 38477524; VBIEscCol113220_2065.
DR   eggNOG; COG0469; -.
DR   HOGENOM; HOG000021558; -.
DR   KO; K00873; -.
DR   OMA; TPVYFDS; -.
DR   OrthoDB; EOG6GBMB0; -.
DR   BioCyc; ECOL585055:GJOM-2069-MONOMER; -.
DR   UniPathway; UPA00109; UER00188.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.33.10; -; 1.
DR   Gene3D; 3.20.20.60; -; 2.
DR   Gene3D; 3.40.1380.20; -; 1.
DR   InterPro; IPR001697; Pyr_Knase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom.
DR   InterPro; IPR015794; Pyrv_Knase_a/b.
DR   InterPro; IPR018209; Pyrv_Knase_AS.
DR   InterPro; IPR015793; Pyrv_Knase_brl.
DR   InterPro; IPR015795; Pyrv_Knase_C.
DR   InterPro; IPR015806; Pyrv_Knase_insert_dom.
DR   PANTHER; PTHR11817; PTHR11817; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   SUPFAM; SSF50800; SSF50800; 1.
DR   SUPFAM; SSF51621; SSF51621; 2.
DR   SUPFAM; SSF52935; SSF52935; 1.
DR   TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Kinase; Magnesium; Pyruvate;
KW   Transferase.
SQ   SEQUENCE   480 AA;  51385 MW;  30BCC63C9A952868 CRC64;
     MSRRLRRTKI VTTLGPATDR DNNLEKVIAA GANVVRMNFS HGSPEDHKMR ADKVREIAAR
     LGRHVAILGD LQGPKIRVST FKEGKVFLNI GDKFLLDANL GKGEGDKEKV GIDYKGLPAD
     VVPGDILLLD DGRVQLKVLE VQGMKVFTEV TVGGPLSNNK GINKLGGGLS AEALTEKDKA
     DIKTAALIGV DYLAVSFPRC GEDLNYARRL ARDAGCDAKI VAKVERAEAV CSQDAMDDII
     LASDVVMVAR GDLGVEIGDP ELVGIQKALI RRARQLNRAV ITATQMMESM ITNPMPTRAE
     VMDVANAVLD GTDAVMLSAE TAAGQYPSET VAAMARVCLG AEKIPSINVS KHRLDVQFDN
     VEEAIAMSAM YAANHLKGVT AIITMTESGR TALMTSRISS GLPIFAMSRH ERTLNLTALY
     RGVTPVHFDS ANDGVAAASE AVNLLRDKGY LMSGDLVIVT QGDVMSTVGS TNTTRILTVE
//
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