KPYK2_ECOLI
ID KPYK2_ECOLI Reviewed; 480 AA.
AC P21599;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Pyruvate kinase II;
DE EC=2.7.1.40;
DE AltName: Full=PK-2;
GN Name=pykA; OrderedLocusNames=b1854, JW1843;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Bledig S.A., Fotheringham I.G., Hunter M.G.;
RL Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 319-480.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=1732206; DOI=10.1128/jb.174.3.702-710.1992;
RA Karow M.L., Georgopoulos C.;
RT "Isolation and characterization of the Escherichia coli msbB gene, a
RT multicopy suppressor of null mutations in the high-temperature requirement
RT gene htrB.";
RL J. Bacteriol. 174:702-710(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 323-480.
RC STRAIN=K12;
RA Engel H., Smink A.J., Keck W.;
RL Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 2-44.
RX PubMed=1859631; DOI=10.1515/bchm3.1991.372.1.91;
RA Valentini G., Stoppini M., Speranza M.L., Malcovati M., Ferri G.;
RT "Bacterial pyruvate kinases have a shorter N-terminal domain.";
RL Biol. Chem. Hoppe-Seyler 372:91-93(1991).
RN [8]
RP PROTEIN SEQUENCE OF 64-77; 83-107; 251-272 AND 337-353.
RX PubMed=8439398; DOI=10.1515/bchm3.1993.374.1-6.69;
RA Valentini G., Stoppini M., Iadarola P., Malcovati M., Ferri G.,
RA Speranza M.L.;
RT "Divergent binding sites in pyruvate kinases I and II from Escherichia
RT coli.";
RL Biol. Chem. Hoppe-Seyler 374:69-74(1993).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-351, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
CC -!- FUNCTION: Catalyzes the formation of pyruvate in the last step of
CC glycolysis, it is irreversible under physiological conditions. The
CC reaction is critical for the control of metabolic flux in the second
CC part of glycolysis. {ECO:0000305}.
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 PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18159;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC -!- ACTIVITY REGULATION: Allosterically activated by AMP and by several
CC sugar phosphates. Belongs to type II PK.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5.
CC -!- SUBUNIT: Homotetramer.
CC -!- INTERACTION:
CC P21599; P23930: lnt; NbExp=3; IntAct=EBI-368956, EBI-556569;
CC P21599; P19642: malX; NbExp=4; IntAct=EBI-368956, EBI-556578;
CC P21599; P21599: pykA; NbExp=3; IntAct=EBI-368956, EBI-368956;
CC P21599; P08390: usg; NbExp=3; IntAct=EBI-368956, EBI-548921;
CC P21599; P52052: yggR; NbExp=4; IntAct=EBI-368956, EBI-552531;
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA96707.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M63703; AAA24473.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74924.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15662.1; -; Genomic_DNA.
DR EMBL; M77039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M87660; AAA96707.1; ALT_FRAME; Genomic_DNA.
DR PIR; S29790; S29790.
DR RefSeq; NP_416368.1; NC_000913.3.
DR RefSeq; WP_000091148.1; NZ_SSZK01000001.1.
DR PDB; 6K0K; X-ray; 2.68 A; A/B/C/D=1-480.
DR PDBsum; 6K0K; -.
DR AlphaFoldDB; P21599; -.
DR SMR; P21599; -.
DR BioGRID; 4263205; 27.
DR BioGRID; 850874; 5.
DR DIP; DIP-10622N; -.
DR IntAct; P21599; 18.
DR STRING; 511145.b1854; -.
DR iPTMnet; P21599; -.
DR jPOST; P21599; -.
DR PaxDb; P21599; -.
DR PRIDE; P21599; -.
DR EnsemblBacteria; AAC74924; AAC74924; b1854.
DR EnsemblBacteria; BAA15662; BAA15662; BAA15662.
DR GeneID; 66674256; -.
DR GeneID; 946527; -.
DR KEGG; ecj:JW1843; -.
DR KEGG; eco:b1854; -.
DR PATRIC; fig|511145.12.peg.1933; -.
DR EchoBASE; EB0796; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_8_0_6; -.
DR InParanoid; P21599; -.
DR OMA; QVPIVQK; -.
DR PhylomeDB; P21599; -.
DR BioCyc; EcoCyc:PKII-MON; -.
DR BioCyc; MetaCyc:PKII-MON; -.
DR UniPathway; UPA00109; UER00188.
DR PRO; PR:P21599; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1902912; C:pyruvate kinase complex; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IDA:EcoCyc.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR CDD; cd00288; Pyruvate_Kinase; 1.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; ATP-binding;
KW Direct protein sequencing; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1859631"
FT CHAIN 2..480
FT /note="Pyruvate kinase II"
FT /id="PRO_0000112073"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
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|UniProtKB:P30613"
FT BINDING 40
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 70
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
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 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT SITE 223
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00549"
FT MOD_RES 351
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT CONFLICT 20
FT /note="R -> C (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="S -> G (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="A -> R (in Ref. 6; AAA96707)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="Missing (in Ref. 6; AAA96707)"
FT /evidence="ECO:0000305"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 44..61
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:6K0K"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 176..188
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 233..241
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 259..275
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 298..310
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 327..342
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 361..375
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 390..396
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 423..427
FT /evidence="ECO:0007829|PDB:6K0K"
FT HELIX 434..448
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:6K0K"
FT STRAND 473..478
FT /evidence="ECO:0007829|PDB:6K0K"
SQ SEQUENCE 480 AA; 51357 MW; C37F004C374D27E9 CRC64;
MSRRLRRTKI VTTLGPATDR DNNLEKVIAA GANVVRMNFS HGSPEDHKMR ADKVREIAAK
LGRHVAILGD LQGPKIRVST FKEGKVFLNI GDKFLLDANL GKGEGDKEKV GIDYKGLPAD
VVPGDILLLD DGRVQLKVLE VQGMKVFTEV TVGGPLSNNK GINKLGGGLS AEALTEKDKA
DIKTAALIGV DYLAVSFPRC GEDLNYARRL ARDAGCDAKI VAKVERAEAV CSQDAMDDII
LASDVVMVAR GDLGVEIGDP ELVGIQKALI RRARQLNRAV ITATQMMESM ITNPMPTRAE
VMDVANAVLD GTDAVMLSAE TAAGQYPSET VAAMARVCLG AEKIPSINVS KHRLDVQFDN
VEEAIAMSAM YAANHLKGVT AIITMTESGR TALMTSRISS GLPIFAMSRH ERTLNLTALY
RGVTPVHFDS ANDGVAAASE AVNLLRDKGY LMSGDLVIVT QGDVMSTVGS TNTTRILTVE
