KPYK_BUCAI
ID KPYK_BUCAI Reviewed; 480 AA.
AC P57404;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pykA; OrderedLocusNames=BU319;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Allosterically activated by AMP and by several
CC sugar phosphates. Belongs to type II PK (By similarity). {ECO:0000250}.
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; BA000003; BAB13027.1; -; Genomic_DNA.
DR RefSeq; NP_240141.1; NC_002528.1.
DR RefSeq; WP_010896064.1; NC_002528.1.
DR AlphaFoldDB; P57404; -.
DR SMR; P57404; -.
DR STRING; 107806.10038993; -.
DR EnsemblBacteria; BAB13027; BAB13027; BAB13027.
DR KEGG; buc:BU319; -.
DR PATRIC; fig|107806.10.peg.331; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_6; -.
DR OMA; QVPIVQK; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000001806; 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; 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 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Potassium; Pyruvate; Reference proteome;
KW Transferase.
FT CHAIN 1..480
FT /note="Pyruvate kinase"
FT /id="PRO_0000112058"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 38..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 38
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 77
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 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 223
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 480 AA; 52691 MW; 5C955A1A2C561969 CRC64;
MLNRLRRTKI VATLGPSTDI NNNLEKIIRS GVNVLRFNFS HGSKDEHKSR ANQAREIMTR
LNFHIALLGD LQGPKIRISK FIKNNIFLNV GDFFILDANL DQNNGNQERV GIDYKQLPYD
LKVGDVLLLD DGRIQLKVIK STGHEILTKV VIGGILSNNK GINKLGGGLS ADALTEKDKK
DIILATEINV DYLAISFPRC SNDLKQARKL AKEFGSNAKI IAKIERAEAV LNQNTIEDII
LASDAIMIAR GDLGVEIGDS ELAGIQKKLI RTARQLNRIV ITATQMMESM ITNPLPTRAE
VMDVANAVLD GSDAVMLSAE TASGEYPAET VIKMAKICKG AEKVPSINVS RHRIHAKFDD
IEEAIAMSAM YVANHLKGIT AIITMTESGK TALMTSRITS GLPIFALSKN KETLNLASLY
RGVTPIYFNS KNNNFKAANE AIVLLRKRGF LCRGELVIIT QGDIMGKIGK TNTSRILKVV
