ID KPYK_CHLT2 Reviewed; 485 AA. AC B0B7Q0; O84336; P94685; DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 87. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; Synonyms=pykF; OrderedLocusNames=CTL0586; OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B). OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=471472; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10411734; DOI=10.1046/j.1365-2958.1999.01464.x; RA Iliffe-Lee E.R., McClarty G.; RT "Glucose metabolism in Chlamydia trachomatis: the 'energy parasite' RT hypothesis revisited."; RL Mol. Microbiol. 33:177-187(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=434/Bu / ATCC VR-902B; RX PubMed=18032721; DOI=10.1101/gr.7020108; RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P., RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D., RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.; RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma RT venereum isolates."; RL Genome Res. 18:161-171(2008). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate; CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; CC EC=2.7.1.40; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB41226.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U83196; AAB41226.1; ALT_INIT; Genomic_DNA. DR EMBL; AM884176; CAP04026.1; -; Genomic_DNA. DR RefSeq; WP_009873733.1; NC_010287.1. DR RefSeq; YP_001654661.1; NC_010287.1. DR AlphaFoldDB; B0B7Q0; -. DR SMR; B0B7Q0; -. DR KEGG; ctb:CTL0586; -. DR PATRIC; fig|471472.4.peg.631; -. DR HOGENOM; CLU_015439_0_2_0; -. DR SABIO-RK; B0B7Q0; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP001154402; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1. DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1. DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1. DR InterPro; IPR001697; Pyr_Knase. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf. DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf. DR InterPro; IPR015793; Pyrv_Knase_brl. DR InterPro; IPR015795; Pyrv_Knase_C. DR InterPro; IPR036918; Pyrv_Knase_C_sf. DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf. DR NCBIfam; TIGR01064; pyruv_kin; 1. DR PANTHER; PTHR11817; PYRUVATE KINASE; 1. DR PANTHER; PTHR11817:SF132; PYRUVATE KINASE 1; 1. DR Pfam; PF00224; PK; 1. DR Pfam; PF02887; PK_C; 1. DR PRINTS; PR01050; PYRUVTKNASE. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1. DR SUPFAM; SSF52935; PK C-terminal domain-like; 1. PE 3: Inferred from homology; KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Potassium; Pyruvate; Transferase. FT CHAIN 1..485 FT /note="Pyruvate kinase" FT /id="PRO_0000391804" FT BINDING 33 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 35..38 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 35 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 37 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 67 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 68 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 74 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 155 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 221 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 244 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 245 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 245 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 277 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 219 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT CONFLICT 104..113 FT /note="GVTLYPSCVF -> ALLFIQVVYS (in Ref. 1; AAB41226)" FT /evidence="ECO:0000305" FT CONFLICT 362..366 FT /note="IGFSG -> NWVFW (in Ref. 1; AAB41226)" FT /evidence="ECO:0000305" SQ SEQUENCE 485 AA; 53631 MW; 37001F8B1F40FF4C 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 SGETASGAHP VHAVKTMRSI IQETEKTFDY HAFFQLNDKN SALKVSPYLE AIGFSGIQIA EKASAKAIIV YTQTGGSPMF LSKYRPYLPI IAVTPNRNVY YRLAVEWGVY PMLTLESNRT VWRHQACVYG VEKGILSNYD KILVFSRGAG MQDTNNLTLT TVHDALSPSL DEIVP //