ID A4WBL2_ENT38 Unreviewed; 480 AA.
AC A4WBL2;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 01-MAY-2013, entry version 54.
DE RecName: Full=Pyruvate kinase;
DE EC=2.7.1.40;
GN OrderedLocusNames=Ent638_2423;
OS Enterobacter sp. (strain 638).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Enterobacter sp. 638.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000653; ABP61092.1; -; Genomic_DNA.
DR RefSeq; YP_001177143.1; NC_009436.1.
DR ProteinModelPortal; A4WBL2; -.
DR STRING; 399742.Ent638_2423; -.
DR EnsemblBacteria; ABP61092; ABP61092; Ent638_2423.
DR GeneID; 5110925; -.
DR KEGG; ent:Ent638_2423; -.
DR PATRIC; 20414483; VBIEntSp101211_2569.
DR eggNOG; COG0469; -.
DR HOGENOM; HOG000021558; -.
DR KO; K00873; -.
DR OMA; VQVSKHR; -.
DR ProtClustDB; PRK05826; -.
DR BioCyc; ESP399742:GJ0E-2471-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; 51483 MW; 3B64D43A7625E8F6 CRC64;
MSRRLRRTKI VTTLGPATDR DNNLEKIIAA GANVVRMNFS HGTPEDHKLR ADKVREIAAK
LGRHVAILGD LQGPKIRVST FKEGKVFLNI GDKFLLDANL GKGEGDKERV GIDYKGLPAD
VVPGDILLLD DGRVQLKVLE VQGMKVFTEV TVGGPLSNNK GINKLGGGLS AEALTEKDKA
DIITAAQIGV DYLAVSFPRC GEDLNYARRL ARDAGCDAKI VAKVERAEAV CSQDAMDDVI
LASDVVMVAR GDLGVEIGDP ELVGIQKALI RRARQLNRSV ITATQMMESM ITNPMPTRAE
VMDVANAVLD GTDAVMLSAE TAAGQYPAET VAAMARVCLG AEKIPSINVS KHRLDIQFDN
VEEAISMSAM YAANHLKGVT AIITMTESGR TALMTSRISS GLPIFAMSRH ERTLNLTTLY
RGVTPVYFDS TSEGVAAAND AVNLLRDKGY LVSGDIVIVT QGDVMSTIGS TNTTRVMTVE
//