ID B7L7Q7_ECO55 Unreviewed; 480 AA.
AC B7L7Q7;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 37.
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; VQVSKHR; -.
DR ProtClustDB; PRK05826; -.
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:EC.
DR GO; GO:0006096; P:glycolysis; 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.
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; PK_B_barrel_like; 1.
DR SUPFAM; SSF52935; Pyruvate_kinase; 1.
DR SUPFAM; SSF51621; Pyrv/PenolPyrv_Kinase_cat; 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
//
