KPYK_CHLT2
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 03-AUG-2022, entry version 80.
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; Chlamydiae; 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};
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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 EnsemblBacteria; CAP04026; CAP04026; CTL0586.
DR KEGG; ctb:CTL0586; -.
DR PATRIC; fig|471472.4.peg.631; -.
DR HOGENOM; CLU_015439_0_2_0; -.
DR OMA; QVPIVQK; -.
DR SABIO-RK; B0B7Q0; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000000795; 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 Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.40.1380.20; -; 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 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; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 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
