PFKB_ECOLI
ID PFKB_ECOLI Reviewed; 309 AA.
AC P06999; P78065; P78260;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=ATP-dependent 6-phosphofructokinase isozyme 2;
DE Short=ATP-PFK 2;
DE Short=Phosphofructokinase 2;
DE EC=2.7.1.11;
DE AltName: Full=6-phosphofructokinase isozyme II;
DE AltName: Full=Phosphohexokinase 2;
GN Name=pfkB; OrderedLocusNames=b1723, JW5280;
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=6235149; DOI=10.1016/0378-1119(84)90151-3;
RA Daldal F.;
RT "Nucleotide sequence of gene pfkB encoding the minor phosphofructokinase of
RT Escherichia coli K-12.";
RL Gene 28:337-342(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(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 1-38.
RX PubMed=6310120; DOI=10.1016/s0022-2836(83)80019-9;
RA Daldal F.;
RT "Molecular cloning of the gene for phosphofructokinase-2 of Escherichia
RT coli and the nature of a mutation, pfkB1, causing a high level of the
RT enzyme.";
RL J. Mol. Biol. 168:285-305(1983).
RN [6]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF GLU-190, AND
RP ACTIVITY REGULATION.
RX PubMed=16866375; DOI=10.1021/bi060026o;
RA Parducci R.E., Cabrera R., Baez M., Guixe V.;
RT "Evidence for a catalytic Mg2+ ion and effect of phosphate on the activity
RT of Escherichia coli phosphofructokinase-2: regulatory properties of a
RT ribokinase family member.";
RL Biochemistry 45:9291-9299(2006).
RN [8] {ECO:0007744|PDB:3CQD}
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ATP AND
RP ALLOSTERIC INHIBITOR ATP.
RX PubMed=18762190; DOI=10.1016/j.jmb.2008.08.029;
RA Cabrera R., Ambrosio A.L., Garratt R.C., Guixe V., Babul J.;
RT "Crystallographic structure of phosphofructokinase-2 from Escherichia coli
RT in complex with two ATP molecules. Implications for substrate inhibition.";
RL J. Mol. Biol. 383:588-602(2008).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH
RP FRUCTOSE-6-PHOSPHATE.
RX PubMed=21147773; DOI=10.1074/jbc.m110.163162;
RA Cabrera R., Baez M., Pereira H.M., Caniuguir A., Garratt R.C., Babul J.;
RT "The crystal complex of phosphofructokinase-2 of Escherichia coli with
RT fructose-6-phosphate: kinetic and structural analysis of the allosteric ATP
RT inhibition.";
RL J. Biol. Chem. 286:5774-5783(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) IN COMPLEX WITH ADP; ATP;
RP FRUCTOSE-1-6-DIPHOSPHATE AND FRUCTOSE-6-PHOSPHATE.
RA Pereira H.M., Caniuguir A., Baez M., Cabrera R., Garratt R.C., Babul J.;
RT "Structure of E. coli PFK2 in complex with substrates and products.";
RL Submitted (NOV-2011) to the PDB data bank.
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ATP AND DIPHOSPHATE.
RA Pereira H.M., Caniuguir A., Baez M., Cabrera R., Garratt R.C., Babul J.;
RT "Structure of E. coli PFK2 mutant Y23D.";
RL Submitted (NOV-2011) to the PDB data bank.
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH ATP AND POTASSIUM,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=23823238; DOI=10.1016/j.bpj.2013.05.028;
RA Baez M., Cabrera R., Pereira H.M., Blanco A., Villalobos P.,
RA Ramirez-Sarmiento C.A., Caniuguir A., Guixe V., Garratt R.C., Babul J.;
RT "A ribokinase family conserved monovalent cation binding site enhances the
RT MgATP-induced inhibition in E. coli phosphofructokinase-2.";
RL Biophys. J. 105:185-193(2013).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. {ECO:0000269|PubMed:16866375}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:456216; EC=2.7.1.11;
CC Evidence={ECO:0000269|PubMed:16866375, ECO:0000269|PubMed:23823238};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16866375};
CC -!- ACTIVITY REGULATION: Allosterically inhibited by ATP. Allosteric ATP-
CC binding requires the presence of the substrate ATP. Inhibited by
CC monovalent cations with ionic radii larger than Na(+) (e.g. K(+),
CC Cs(+)). The monovalent cations increase the affinity of the allosteric
CC site for ATP. PFK-2 is sensitive to inhibition by fructose 1,6-
CC diphosphate. {ECO:0000269|PubMed:16866375,
CC ECO:0000269|PubMed:23823238}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8 uM for ATP {ECO:0000269|PubMed:23823238};
CC KM=6 uM for fructose 6-phosphate {ECO:0000269|PubMed:23823238};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18762190,
CC ECO:0000269|PubMed:21147773, ECO:0000269|PubMed:23823238,
CC ECO:0000269|Ref.10, ECO:0000269|Ref.11}.
CC -!- INTERACTION:
CC P06999; P06999: pfkB; NbExp=2; IntAct=EBI-6966085, EBI-6966085;
CC -!- MISCELLANEOUS: Only 10% of the activity present in the wild-type strain
CC is phosphofructokinase-2.
CC -!- MISCELLANEOUS: This enzyme is not to be confused with 6-phosphofructo-
CC 2-kinase which is also called phosphofructokinase 2.
CC -!- MISCELLANEOUS: E.coli has two 6-phosphofructokinases enzymes.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; K02500; AAA24321.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74793.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15500.2; -; Genomic_DNA.
DR EMBL; K00128; AAA24320.1; -; Genomic_DNA.
DR PIR; C64931; KIECFB.
DR RefSeq; NP_416237.3; NC_000913.3.
DR RefSeq; WP_000251727.1; NZ_SSZK01000001.1.
DR PDB; 3CQD; X-ray; 1.98 A; A/B=1-309.
DR PDB; 3N1C; X-ray; 2.00 A; A/B/C/D=1-309.
DR PDB; 3UMO; X-ray; 1.70 A; A/B=1-309.
DR PDB; 3UMP; X-ray; 1.85 A; A/B=1-309.
DR PDB; 3UQD; X-ray; 2.14 A; A/B/C/D=1-309.
DR PDB; 3UQE; X-ray; 2.20 A; A/B=1-309.
DR PDBsum; 3CQD; -.
DR PDBsum; 3N1C; -.
DR PDBsum; 3UMO; -.
DR PDBsum; 3UMP; -.
DR PDBsum; 3UQD; -.
DR PDBsum; 3UQE; -.
DR AlphaFoldDB; P06999; -.
DR SMR; P06999; -.
DR BioGRID; 4263076; 25.
DR DIP; DIP-10465N; -.
DR MINT; P06999; -.
DR STRING; 511145.b1723; -.
DR SWISS-2DPAGE; P06999; -.
DR jPOST; P06999; -.
DR PaxDb; P06999; -.
DR PRIDE; P06999; -.
DR EnsemblBacteria; AAC74793; AAC74793; b1723.
DR EnsemblBacteria; BAA15500; BAA15500; BAA15500.
DR GeneID; 946230; -.
DR KEGG; ecj:JW5280; -.
DR KEGG; eco:b1723; -.
DR PATRIC; fig|1411691.4.peg.533; -.
DR EchoBASE; EB0694; -.
DR eggNOG; COG1105; Bacteria.
DR HOGENOM; CLU_050013_0_2_6; -.
DR InParanoid; P06999; -.
DR OMA; QLNEPGP; -.
DR PhylomeDB; P06999; -.
DR BioCyc; EcoCyc:6PFK-2-MON; -.
DR BioCyc; MetaCyc:6PFK-2-MON; -.
DR BRENDA; 2.7.1.11; 2026.
DR SABIO-RK; P06999; -.
DR UniPathway; UPA00109; UER00182.
DR EvolutionaryTrace; P06999; -.
DR PRO; PR:P06999; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003872; F:6-phosphofructokinase activity; 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:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0008443; F:phosphofructokinase activity; IBA:GO_Central.
DR GO; GO:0009024; F:tagatose-6-phosphate kinase activity; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0006096; P:glycolytic process; IMP:EcoCyc.
DR CDD; cd01164; FruK_PfkB_like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
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 PROSITE; PS00583; PFKB_KINASES_1; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Reference proteome; Transferase.
FT CHAIN 1..309
FT /note="ATP-dependent 6-phosphofructokinase isozyme 2"
FT /id="PRO_0000080083"
FT ACT_SITE 256
FT /evidence="ECO:0000250"
FT BINDING 12..14
FT /ligand="substrate"
FT BINDING 27..29
FT /ligand="substrate"
FT BINDING 27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="substrate; ligand shared between dimeric
FT partners"
FT /evidence="ECO:0000269|PubMed:18762190,
FT ECO:0000269|PubMed:23823238, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.11, ECO:0007744|PDB:3CQD"
FT BINDING 27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="allosteric inhibitor; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000269|PubMed:18762190,
FT ECO:0007744|PDB:3CQD"
FT BINDING 39..43
FT /ligand="substrate"
FT BINDING 90..92
FT /ligand="substrate"
FT BINDING 139
FT /ligand="substrate"
FT BINDING 185..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="substrate; ligand shared between dimeric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:18762190,
FT ECO:0000269|PubMed:23823238, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.11, ECO:0007744|PDB:3CQD"
FT BINDING 187..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="allosteric inhibitor; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:18762190,
FT ECO:0007744|PDB:3CQD"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 224..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="substrate; ligand shared between dimeric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:18762190,
FT ECO:0000269|PubMed:23823238, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.11, ECO:0007744|PDB:3CQD"
FT BINDING 248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="substrate; ligand shared between dimeric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:18762190,
FT ECO:0000269|PubMed:23823238, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.11, ECO:0007744|PDB:3CQD"
FT BINDING 250
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:23823238"
FT BINDING 252
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:23823238"
FT BINDING 256
FT /ligand="substrate"
FT BINDING 280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="substrate; ligand shared between dimeric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:18762190,
FT ECO:0000269|PubMed:23823238, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.11, ECO:0007744|PDB:3CQD"
FT BINDING 284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="substrate; ligand shared between dimeric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:18762190,
FT ECO:0000269|PubMed:23823238, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.11, ECO:0007744|PDB:3CQD"
FT BINDING 286
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:23823238"
FT BINDING 289
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:23823238"
FT BINDING 291
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:23823238"
FT BINDING 293
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:23823238"
FT MUTAGEN 190
FT /note="E->Q: Causes a 50-fold decrease in the kcat value
FT and a 15-fold increment in the apparent KM for ATP."
FT /evidence="ECO:0000269|PubMed:16866375"
FT CONFLICT 26..38
FT /note="GKLRCTAPVFEPG -> ENCAVPHRCSNP (in Ref. 1; AAA24321
FT and 5; AAA24320)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..171
FT /note="AAQKQGIRCIVDSSGEA -> LRKNKGSAASSTVLGQG (in Ref. 1;
FT AAA24321)"
FT /evidence="ECO:0000305"
FT CONFLICT 245..246
FT /note="PV -> AL (in Ref. 1; AAA24321)"
FT /evidence="ECO:0000305"
FT CONFLICT 257..258
FT /note="SM -> RL (in Ref. 1; AAA24321)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:3UMO"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:3UMO"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:3UMO"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:3UMO"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:3UMO"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:3UMO"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:3UMO"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:3UMO"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:3UMO"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:3UMO"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3UMO"
FT HELIX 115..125
FT /evidence="ECO:0007829|PDB:3UMO"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:3UMO"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:3UMO"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:3UMO"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:3UMO"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:3CQD"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:3UMO"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:3UMO"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:3UMO"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3UMO"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:3UMO"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:3UMO"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:3UMO"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:3UMO"
FT HELIX 254..267
FT /evidence="ECO:0007829|PDB:3UMO"
FT HELIX 272..286
FT /evidence="ECO:0007829|PDB:3UMO"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:3CQD"
FT HELIX 297..307
FT /evidence="ECO:0007829|PDB:3UMO"
SQ SEQUENCE 309 AA; 32456 MW; A93BEBE0D5801309 CRC64;
MVRIYTLTLA PSLDSATITP QIYPEGKLRC TAPVFEPGGG GINVARAIAH LGGSATAIFP
AGGATGEHLV SLLADENVPV ATVEAKDWTR QNLHVHVEAS GEQYRFVMPG AALNEDEFRQ
LEEQVLEIES GAILVISGSL PPGVKLEKLT QLISAAQKQG IRCIVDSSGE ALSAALAIGN
IELVKPNQKE LSALVNRELT QPDDVRKAAQ EIVNSGKAKR VVVSLGPQGA LGVDSENCIQ
VVPPPVKSQS TVGAGDSMVG AMTLKLAENA SLEEMVRFGV AAGSAATLNQ GTRLCSHDDT
QKIYAYLSR
