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 27-MAR-2024, entry version 92.
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; Pseudomonadota; 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; NZ_CP051263.1.
DR AlphaFoldDB; P0AEX0; -.
DR SMR; P0AEX0; -.
DR STRING; 199310.c2703; -.
DR GeneID; 75206421; -.
DR KEGG; ecc:c2703; -.
DR eggNOG; COG1105; Bacteria.
DR HOGENOM; CLU_050013_0_1_6; -.
DR BioCyc; ECOL199310:C2703-MONOMER; -.
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 NCBIfam; TIGR03168; 1-PFK; 1.
DR NCBIfam; TIGR03828; pfkB; 1.
DR PANTHER; PTHR46566:SF5; 1-PHOSPHOFRUCTOKINASE; 1.
DR PANTHER; PTHR46566; 1-PHOSPHOFRUCTOKINASE-RELATED; 1.
DR Pfam; PF00294; PfkB; 1.
DR PIRSF; PIRSF000535; 1PFK/6PFK/LacC; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 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; Reference proteome; 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
//
