K1PF_ECOLI
ID K1PF_ECOLI Reviewed; 312 AA.
AC P0AEW9; P23539;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=1-phosphofructokinase {ECO:0000303|Ref.6};
DE EC=2.7.1.56 {ECO:0000269|PubMed:10833389, ECO:0000269|Ref.6};
DE AltName: Full=Fructose 1-phosphate kinase {ECO:0000303|PubMed:10833389};
DE Short=Fru1PK {ECO:0000303|PubMed:10833389};
GN Name=fruK {ECO:0000303|PubMed:1981619}; Synonyms=fpk;
GN OrderedLocusNames=b2168, JW2155;
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;
RX PubMed=1981619; DOI=10.1098/rspb.1990.0108;
RA Orchard L.M.D., Kornberg H.L.;
RT "Sequence similarities between the gene specifying 1-phosphofructokinase
RT (fruK), genes specifying other kinases in Escherichia coli K12, and lacC of
RT Staphylococcus aureus.";
RL Proc. R. Soc. B 242:87-90(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=K12 / jOD5;
RX DOI=10.1111/j.1574-6968.1985.tb00868.x;
RA Buschmeier B., Hengstenberg W., Deutscher J.;
RT "Purification and properties of 1-phosphofructokinase from Escherichia
RT coli.";
RL FEMS Microbiol. Lett. 29:231-235(1985).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=10833389; DOI=10.1006/prep.2000.1237;
RA Veiga-da-Cunha M., Hoyoux A., Van Schaftingen E., Houyoux A.;
RT "Overexpression and purification of fructose-1-phosphate kinase from
RT Escherichia coli: application to the assay of fructose 1-phosphate.";
RL Protein Expr. Purif. 19:48-52(2000).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of fructose-l-
CC phosphate to fructose-l,6-bisphosphate (Ref.6, PubMed:10833389). Is
CC specific for fructose-l-phosphate (Ref.6). GTP, UTP and CTP can also
CC function as phosphoryl donors showing 60%, 20% and 10% of the activity
CC of ATP (Ref.6). {ECO:0000269|PubMed:10833389, ECO:0000269|Ref.6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:14213, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:138881,
CC ChEBI:CHEBI:456216; EC=2.7.1.56;
CC Evidence={ECO:0000269|PubMed:10833389, ECO:0000269|Ref.6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|Ref.6};
CC Note=Can also use Mn(2+) or Co(2+), with lower efficiency.
CC {ECO:0000269|Ref.6};
CC -!- ACTIVITY REGULATION: Activity is markedly stimulated by KCl
CC (PubMed:10833389). Reversibly inhibited by fructose-1,6- bisphosphate
CC and ADP. Irreversibly inhibited by phenylmethanesulfonyl fluoride
CC (PMSF) (Ref.6). {ECO:0000269|PubMed:10833389, ECO:0000269|Ref.6}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for fructose 1-phosphate {ECO:0000269|Ref.6};
CC KM=0.36 mM for fructose 1-phosphate (in the absence of KCl)
CC {ECO:0000269|PubMed:10833389};
CC KM=0.125 mM for fructose 1-phosphate (in the presence of 50 mM KCl)
CC {ECO:0000269|PubMed:10833389};
CC KM=0.12 mM for ATP {ECO:0000269|Ref.6};
CC KM=0.35 mM for ATP (in the presence of 5 mM KCl)
CC {ECO:0000269|PubMed:10833389};
CC KM=0.6 mM for ATP (in the presence of 50 mM KCl)
CC {ECO:0000269|PubMed:10833389};
CC pH dependence:
CC Optimum pH is 7.8 in 50 mM Tris-HC1 and 8.5 in 50 mM NH(4)HCO(3).
CC {ECO:0000269|Ref.6};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.6}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {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; X53948; CAA37896.1; -; Genomic_DNA.
DR EMBL; U00007; AAA60525.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75229.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15977.1; -; Genomic_DNA.
DR PIR; B37245; B37245.
DR RefSeq; NP_416673.1; NC_000913.3.
DR RefSeq; WP_000091263.1; NZ_STEB01000002.1.
DR AlphaFoldDB; P0AEW9; -.
DR SMR; P0AEW9; -.
DR BioGRID; 4262911; 23.
DR IntAct; P0AEW9; 2.
DR STRING; 511145.b2168; -.
DR jPOST; P0AEW9; -.
DR PaxDb; P0AEW9; -.
DR PRIDE; P0AEW9; -.
DR EnsemblBacteria; AAC75229; AAC75229; b2168.
DR EnsemblBacteria; BAA15977; BAA15977; BAA15977.
DR GeneID; 66673936; -.
DR GeneID; 946676; -.
DR KEGG; ecj:JW2155; -.
DR KEGG; eco:b2168; -.
DR PATRIC; fig|1411691.4.peg.71; -.
DR EchoBASE; EB0333; -.
DR eggNOG; COG1105; Bacteria.
DR HOGENOM; CLU_050013_0_1_6; -.
DR InParanoid; P0AEW9; -.
DR OMA; GETRSNI; -.
DR PhylomeDB; P0AEW9; -.
DR BioCyc; EcoCyc:1-PFK-MON; -.
DR BioCyc; MetaCyc:1-PFK-MON; -.
DR PRO; PR:P0AEW9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008662; F:1-phosphofructokinase activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008443; F:phosphofructokinase activity; IBA:GO_Central.
DR GO; GO:0006001; P:fructose catabolic process; IMP:EcoCyc.
DR CDD; cd01164; FruK_PfkB_like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR022463; 1-PFruKinase.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR017583; Tagatose/fructose_Pkinase.
DR Pfam; PF00294; PfkB; 1.
DR PIRSF; PIRSF000535; 1PFK/6PFK/LacC; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR03168; 1-PFK; 1.
DR TIGRFAMs; TIGR03828; pfkB; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..312
FT /note="1-phosphofructokinase"
FT /id="PRO_0000080076"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 223..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 254..255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
SQ SEQUENCE 312 AA; 33756 MW; 067E5CF7C584FEA8 CRC64;
MSRRVATITL NPAYDLVGFC PEIERGEVNL VKTTGLHAAG KGINVAKVLK DLGIDVTVGG
FLGKDNQDGF QQLFSELGIA NRFQVVQGRT RINVKLTEKD GEVTDFNFSG FEVTPADWER
FVTDSLSWLG QFDMVCVSGS LPSGVSPEAF TDWMTRLRSQ CPCIIFDSSR EALVAGLKAA
PWLVKPNRRE LEIWAGRKLP EMKDVIEAAH ALREQGIAHV VISLGAEGAL WVNASGEWIA
KPPSVDVVST VGAGDSMVGG LIYGLLMRES SEHTLRLATA VAALAVSQSN VGITDRPQLA
AMMARVDLQP FN
