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 01-MAY-2013, entry version 24.
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:CT332; -.
DR PATRIC; 20380205; VBIChlTra43535_0358.
DR KO; K00873; -.
DR OMA; IVYTESG; -.
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: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; 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; FALSE_NEG.
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
//
