ID   KPYK2_AGRVI             Reviewed;         482 AA.
AC   Q44473;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Pyruvate kinase;
DE            Short=PK;
DE            EC=2.7.1.40;
GN   Name=ttuE;
OS   Agrobacterium vitis (Rhizobium vitis).
OG   Plasmid pTrAB4.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AB4;
RX   PubMed=7592429; DOI=10.1128/jb.177.22.6518-6526.1995;
RA   Crouzet P., Otten L.;
RT   "Sequence and mutational analysis of a tartrate utilization operon from
RT   Agrobacterium vitis.";
RL   J. Bacteriol. 177:6518-6526(1995).
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   -!- INDUCTION: By tartrate.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR   EMBL; U25634; AAA68700.1; -; Genomic_DNA.
DR   RefSeq; WP_071207358.1; NZ_MBFC02000015.1.
DR   AlphaFoldDB; Q44473; -.
DR   SMR; Q44473; -.
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; 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; IPR018209; Pyrv_Knase_AS.
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.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Plasmid; Potassium; Pyruvate; Transferase.
FT   CHAIN           1..482
FT                   /note="Pyruvate kinase"
FT                   /id="PRO_0000112052"
FT   BINDING         37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         39..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         39
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         41
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         160
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         222
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         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            220
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   482 AA;  51678 MW;  2D2B614589CB46E7 CRC64;
     MFIRNNRRSK IVATVGPASS SPDMLRSLFL AGVDTFRLNF SHGARADHAE VYRNIRALEQ
     EHDAAIAVLQ DLQGPKIRIG VLAHGRLDLA RGSTIGFILG REGGEGMNDI PLPHREIFEV
     AVPGMDLLID DGRIKVRIME VMDGRLVCEV LNGGALSNRK GVNVPGAVLD ISPLTAKDRE
     DLEFGLELGV DWVALSFVQR ARDMIEARSL VGDRAGLIAK IEKPSALDDI EDIVRLSDSV
     MVARGDLGVE IPPEDVPGKQ KEIIRACRLA AKPVIVATQM LDSMVSSPTP TRAEASDVAG
     AIYDGADAVM LSAETATGAY PVEAVEIMNR IIEKTEKHKH YRPILEATEP DVAQSPPHAV
     ATAAANVAVA LGSPVVVAYT SSGTTAARIS RARPALPILA LTPSEQVARR LNMFWGVVGV
     RSQDVHTYEA SLIHAQQAVQ EAKLASPSDH IVIVAGFPFA QQGSTNNLRV VQIAATDNLE
     IA