ID   K1PF_ECOL6              Reviewed;         312 AA.
AC   P0AEX0; P23539;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=1-phosphofructokinase {ECO:0000250|UniProtKB:P0AEW9};
DE            EC=2.7.1.56 {ECO:0000250|UniProtKB:P0AEW9};
DE   AltName: Full=Fructose 1-phosphate kinase {ECO:0000250|UniProtKB:P0AEW9};
DE            Short=Fru1PK {ECO:0000250|UniProtKB:P0AEW9};
GN   Name=fruK; OrderedLocusNames=c2703;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of fructose-l-
CC       phosphate to fructose-l,6-bisphosphate. {ECO:0000250|UniProtKB:P0AEW9}.
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:0000250|UniProtKB:P0AEW9};
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000305}.
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DR   EMBL; AE014075; AAN81157.1; -; Genomic_DNA.
DR   RefSeq; WP_000091263.1; NC_004431.1.
DR   AlphaFoldDB; P0AEX0; -.
DR   SMR; P0AEX0; -.
DR   STRING; 199310.c2703; -.
DR   EnsemblBacteria; AAN81157; AAN81157; c2703.
DR   GeneID; 66673936; -.
DR   KEGG; ecc:c2703; -.
DR   eggNOG; COG1105; Bacteria.
DR   HOGENOM; CLU_050013_0_1_6; -.
DR   OMA; GETRSNI; -.
DR   BioCyc; ECOL199310:C2703-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0008662; F:1-phosphofructokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..312
FT                   /note="1-phosphofructokinase"
FT                   /id="PRO_0000080078"
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