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Database: UniProt
Entry: P0CE21
LinkDB: P0CE21
Original site: P0CE21 
ID   KPYK_CHLTR              Reviewed;         485 AA.
AC   P0CE21; O84336; P94685;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   19-MAR-2014, entry version 29.
DE   RecName: Full=Pyruvate kinase;
DE            Short=PK;
DE            EC=2.7.1.40;
GN   Name=pyk; Synonyms=pykF; OrderedLocusNames=CT_332;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V.,
RA   Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans:
RT   Chlamydia trachomatis.";
RL   Science 282:754-759(1998).
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- COFACTOR: Potassium (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; AE001273; AAC67927.1; -; Genomic_DNA.
DR   PIR; G71527; G71527.
DR   RefSeq; NP_219839.1; NC_000117.1.
DR   ProteinModelPortal; P0CE21; -.
DR   EnsemblBacteria; AAC67927; AAC67927; CT_332.
DR   GeneID; 884787; -.
DR   KEGG; ctr:CT_332; -.
DR   PATRIC; 20380205; VBIChlTra43535_0358.
DR   KO; K00873; -.
DR   OMA; NNKGVNF; -.
DR   OrthoDB; EOG6GBMB0; -.
DR   UniPathway; UPA00109; UER00188.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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-like_dom.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom.
DR   InterPro; IPR015794; Pyrv_Knase_a/b.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Potassium; Pyruvate;
KW   Reference proteome; Transferase.
FT   CHAIN         1    485       Pyruvate kinase.
FT                                /FTId=PRO_0000112063.
FT   METAL        35     35       Potassium (By similarity).
FT   METAL        37     37       Potassium (By similarity).
FT   METAL        67     67       Potassium (By similarity).
FT   METAL        68     68       Potassium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       221    221       Magnesium (By similarity).
FT   METAL       245    245       Magnesium (By similarity).
FT   BINDING      33     33       Substrate (By similarity).
FT   BINDING     244    244       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     245    245       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     277    277       Substrate (By similarity).
FT   SITE        219    219       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   485 AA;  53685 MW;  0C638F0605326C55 CRC64;
     MIARTKIICT IGPATNTPEM LEKLLDAGMN VARLNFSHGT HESHGRTIAI LKELREKRQV
     PLAIMLDTKG PEIRLGQVES PIKVQPGDRL TLVSKEILGS KESGVTLYPS CVFPYVRERA
     PVLIDDGYIQ AVVVNAQEHM VEIEFQNSGE IKSNKSLSIK DIDVALPFMT EKDIADLKFG
     VEQELDLIAA SFVRCNEDID SMRKVLESFG RPNMPIIAKI ENHLGVQNFQ EIARAADGIM
     IARGDLGIEL SIVEVPGLQK FMARASRETG RFCITATQML ESMIRNPLPT RAEVSDVANA
     IYDGTSAVML SGETALGAHP VHAVKTMRSI IQETEKTFDY HAFFQLNDKN SALKVSPYLE
     AIGFSGIQIA EKASAKAIIV YTQTGGSPMF LSKYRPYLPI IAVTPNRNVY YRLAVEWGVY
     PMLTLESNRT VWRHQACVYG VEKGILSNYD KILVFSRGAG MQDTNNLTLT TVHDVLSPSL
     DEIVP
//
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