ID   KPYK_SPICI              Reviewed;         192 AA.
AC   P19680; O30600;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   02-SEP-2026, entry version 103.
DE   RecName: Full=Pyruvate kinase;
DE            Short=PK;
DE            EC=2.7.1.40;
DE   Flags: Fragment;
GN   Name=pyk;
OS   Spiroplasma citri.
OC   Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Entomoplasmatales;
OC   Spiroplasmataceae; Spiroplasma.
OX   NCBI_TaxID=2133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27556 / NCPPB 2647 / R8A2;
RX   PubMed=2139649; DOI=10.1128/jb.172.5.2693-2703.1990;
RA   Chevalier C., Saillard C., Bove J.M.;
RT   "Organization and nucleotide sequences of the Spiroplasma citri genes for
RT   ribosomal protein S2, elongation factor Ts, spiralin, phosphofructokinase,
RT   pyruvate kinase, and an unidentified protein.";
RL   J. Bacteriol. 172:2693-2703(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9732535; DOI=10.1007/s002849900377;
RA   Le Dantec L., Bove J.M., Saillard C.;
RT   "Gene organization and transcriptional analysis of the Spiroplasma citri
RT   rpsB/tsf/x operon.";
RL   Curr. Microbiol. 37:269-273(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pyruvate + ATP = phosphoenolpyruvate + ADP + H(+);
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   -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR   EMBL; AF012877; AAB69999.1; -; Genomic_DNA.
DR   PIR; F35270; F35270.
DR   AlphaFoldDB; P19680; -.
DR   SMR; P19680; -.
DR   STRING; 2133.SCITRI_001127; -.
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:UniProtKB-EC.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR001697; Pyr_Knase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_kinase-like_dom_sf.
DR   InterPro; IPR015793; Pyrv_Knase_brl.
DR   PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR   Pfam; PF00224; PK; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Potassium; Pyruvate; Transferase.
FT   CHAIN           1..>192
FT                   /note="Pyruvate kinase"
FT                   /id="PRO_0000112084"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         43..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         43
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        82..192
FT                   /note="HWRIKGLLQKSLNIYHQMNNSLMFSPSFCKFLHYHYTLLLSKKTKKQLLKIV
FT                   KKLKKLQSQHYNLAHGLRETWTSSFCFNERPSIWRLLSSFKQIVTSFKISLVSKVLIKL
FT                   -> RAGIMKGGKQEIVAGATVTIYSLPTEYQNREGTGTEITVSYDMSQDLKVGDVVLVD
FT                   DGKLQLNVTGIKPGIIETKA (in Ref. 2; AAB69999)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         192
SQ   SEQUENCE   192 AA;  22209 MW;  ACF22444BF2CF807 CRC64;
     MDKFNINEKM KRTKIITTIG PSTHSPGAIE ELFKTGMTTI RLNFSHGDHA EQGARIVWAR
     EVSAKIGKPI SVLLDTKGPE IHWRIKGLLQ KSLNIYHQMN NSLMFSPSFC KFLHYHYTLL
     LSKKTKKQLL KIVKKLKKLQ SQHYNLAHGL RETWTSSFCF NERPSIWRLL SSFKQIVTSF
     KISLVSKVLI KL
//