ID   KPYK1_PHOLE             Reviewed;         235 AA.
AC   O30853;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Pyruvate kinase I;
DE            EC=2.7.1.40;
DE   AltName: Full=PK-1;
DE   Flags: Fragment;
GN   Name=pki;
OS   Photobacterium leiognathi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=553611;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25521 / DSM 21260 / CIP 66.5 / NCIMB 2193 / L1;
RX   PubMed=9345300; DOI=10.1006/bbrc.1997.7461;
RA   Lin J.-W., Lu H.-C., Chen H.-Y., Weng S.-F.;
RT   "The pkI gene encoding pyruvate kinase I links to the luxZ gene which
RT   enhances bioluminescence of the lux operon from Photobacterium
RT   leiognathi.";
RL   Biochem. Biophys. Res. Commun. 239:228-234(1997).
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}.
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DR   EMBL; AF019143; AAC45776.1; -; Genomic_DNA.
DR   PIR; PC4418; PC4418.
DR   AlphaFoldDB; O30853; -.
DR   SMR; O30853; -.
DR   STRING; 553611.GCA_001557755_01912; -.
DR   UniPathway; UPA00109; UER00188.
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; 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; IPR015793; Pyrv_Knase_brl.
DR   InterPro; IPR015795; Pyrv_Knase_C.
DR   InterPro; IPR036918; Pyrv_Knase_C_sf.
DR   PANTHER; PTHR11817; PTHR11817; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   SUPFAM; SSF52935; SSF52935; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Potassium; Pyruvate; Transferase.
FT   CHAIN           <1..235
FT                   /note="Pyruvate kinase I"
FT                   /id="PRO_0000112083"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   235 AA;  24734 MW;  F805606C4C8EF4C1 CRC64;
     ASDGIMVARG DLGVEIPVEE VIFAQKMMIE KCNRARKVVI TATQMLDSMI KNPRPTRAEA
     GDVANAIMDG TDAVMLSGES AKGKYPIEAV TIMAQICART DDVVKPELGS RLDSPRLRIT
     EAVCKGAVDT AEKLNAPLII VATEAGKSAR SVRKYFPTAR ILAVTTNTKT AAQLCLSKGV
     TPVVVDSIES TDAFYLRGKE LALETGLGAK GDIVVMVSGA LVASGTTNTA SVHVL