PFKA_ECOLI
ID PFKA_ECOLI Reviewed; 320 AA.
AC P0A796; P06998; Q2M8L2;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=ATP-dependent 6-phosphofructokinase isozyme 1 {ECO:0000255|HAMAP-Rule:MF_00339};
DE Short=ATP-PFK 1 {ECO:0000255|HAMAP-Rule:MF_00339};
DE Short=Phosphofructokinase 1 {ECO:0000255|HAMAP-Rule:MF_00339};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_00339};
DE AltName: Full=6-phosphofructokinase isozyme I;
DE AltName: Full=Phosphohexokinase 1 {ECO:0000255|HAMAP-Rule:MF_00339};
GN Name=pfkA {ECO:0000255|HAMAP-Rule:MF_00339};
GN OrderedLocusNames=b3916, JW3887;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3158524; DOI=10.1111/j.1432-1033.1985.tb08934.x;
RA Hellinga H.W., Evans P.R.;
RT "Nucleotide sequence and high-level expression of the major Escherichia
RT coli phosphofructokinase.";
RL Eur. J. Biochem. 149:363-373(1985).
RN [2]
RP SEQUENCE REVISION, ACTIVE SITE, AND MUTAGENESIS OF ASP-128 AND ARG-172.
RX PubMed=2953977; DOI=10.1038/327437a0;
RA Hellinga H.W., Evans P.R.;
RT "Mutations in the active site of Escherichia coli phosphofructokinase.";
RL Nature 327:437-439(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
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 PROTEIN SEQUENCE OF 1-8.
RC STRAIN=K12;
RX PubMed=17895580; DOI=10.1266/ggs.82.291;
RA Otsuka Y., Koga M., Iwamoto A., Yonesaki T.;
RT "A role of RnlA in the RNase LS activity from Escherichia coli.";
RL Genes Genet. Syst. 82:291-299(2007).
RN [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM; ADP;
RP FRUCTOSE 1,6-BISPHOSPHATE AND ALLOSTERIC ACTIVATOR, AND ACTIVE SITE.
RX PubMed=2975709; DOI=10.1016/0022-2836(88)90056-3;
RA Shirakihara Y., Evans P.R.;
RT "Crystal structure of the complex of phosphofructokinase from Escherichia
RT coli with its reaction products.";
RL J. Mol. Biol. 204:973-994(1988).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=2527305; DOI=10.1016/0022-2836(89)90246-5;
RA Rypniewski W.R., Evans P.R.;
RT "Crystal structure of unliganded phosphofructokinase from Escherichia
RT coli.";
RL J. Mol. Biol. 207:805-821(1989).
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:0000255|HAMAP-Rule:MF_00339}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00339};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00339,
CC ECO:0000269|PubMed:2975709};
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP and other
CC diphosphonucleosides, and allosterically inhibited by
CC phosphoenolpyruvate. {ECO:0000255|HAMAP-Rule:MF_00339}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_00339}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00339,
CC ECO:0000269|PubMed:2975709}.
CC -!- INTERACTION:
CC P0A796; P12281: moeA; NbExp=2; IntAct=EBI-554405, EBI-554393;
CC P0A796; P0A7I4: prfC; NbExp=2; IntAct=EBI-554405, EBI-556252;
CC P0A796; P37440: ucpA; NbExp=2; IntAct=EBI-554405, EBI-559387;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339,
CC ECO:0000305|PubMed:17895580}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00339}.
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DR EMBL; X02519; CAA26356.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03048.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76898.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77394.1; -; Genomic_DNA.
DR PIR; G65197; KIECFA.
DR RefSeq; NP_418351.1; NC_000913.3.
DR RefSeq; WP_000591795.1; NZ_STEB01000017.1.
DR PDB; 1PFK; X-ray; 2.40 A; A/B=1-320.
DR PDB; 2PFK; X-ray; 2.40 A; A/B/C/D=1-320.
DR PDBsum; 1PFK; -.
DR PDBsum; 2PFK; -.
DR AlphaFoldDB; P0A796; -.
DR SMR; P0A796; -.
DR BioGRID; 4261224; 17.
DR DIP; DIP-35841N; -.
DR IntAct; P0A796; 7.
DR STRING; 511145.b3916; -.
DR SWISS-2DPAGE; P0A796; -.
DR jPOST; P0A796; -.
DR PaxDb; P0A796; -.
DR PRIDE; P0A796; -.
DR EnsemblBacteria; AAC76898; AAC76898; b3916.
DR EnsemblBacteria; BAE77394; BAE77394; BAE77394.
DR GeneID; 66672176; -.
DR GeneID; 948412; -.
DR KEGG; ecj:JW3887; -.
DR KEGG; eco:b3916; -.
DR PATRIC; fig|1411691.4.peg.2789; -.
DR EchoBASE; EB0693; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_0_1_6; -.
DR InParanoid; P0A796; -.
DR OMA; KFAVICV; -.
DR PhylomeDB; P0A796; -.
DR BioCyc; EcoCyc:6PFK-1-MON; -.
DR BioCyc; MetaCyc:6PFK-1-MON; -.
DR BRENDA; 2.7.1.11; 2026.
DR SABIO-RK; P0A796; -.
DR UniPathway; UPA00109; UER00182.
DR EvolutionaryTrace; P0A796; -.
DR PRO; PR:P0A796; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005945; C:6-phosphofructokinase complex; IDA:EcoliWiki.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IDA:EcoCyc.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IMP:EcoliWiki.
DR GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoliWiki.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoliWiki.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0032553; F:ribonucleotide binding; IDA:EcoliWiki.
DR GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR GO; GO:0044275; P:cellular carbohydrate catabolic process; IMP:EcoliWiki.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006007; P:glucose catabolic process; IMP:EcoliWiki.
DR GO; GO:0006096; P:glycolytic process; IDA:EcoliWiki.
DR CDD; cd00763; Bacterial_PFK; 1.
DR Gene3D; 3.40.50.460; -; 1.
DR HAMAP; MF_00339; Phosphofructokinase_I_B1; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR012003; ATP_PFK_prok-type.
DR InterPro; IPR012828; PFKA_ATP_prok.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
DR TIGRFAMs; TIGR02482; PFKA_ATP; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..320
FT /note="ATP-dependent 6-phosphofructokinase isozyme 1"
FT /id="PRO_0000111950"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:2953977, ECO:0000269|PubMed:2975709"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:2975709"
FT BINDING 22..26
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:2975709"
FT BINDING 55..60
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:2975709"
FT BINDING 73..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:2975709"
FT BINDING 103..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:2975709"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:2975709"
FT BINDING 126..128
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:2975709"
FT BINDING 155
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:2975709"
FT BINDING 163
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:2975709"
FT BINDING 170..172
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P00512, ECO:0000255|HAMAP-
FT Rule:MF_00339"
FT BINDING 186..188
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:2975709"
FT BINDING 212
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P00512, ECO:0000255|HAMAP-
FT Rule:MF_00339"
FT BINDING 214..216
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:2975709"
FT BINDING 223
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:2975709"
FT BINDING 244
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:2975709"
FT BINDING 250..253
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:2975709"
FT MUTAGEN 128
FT /note="D->S: 18000-fold reduction of catalytic rate."
FT /evidence="ECO:0000269|PubMed:2953977"
FT MUTAGEN 172
FT /note="R->S: 3.4-fold reduction in turnover numbers."
FT /evidence="ECO:0000269|PubMed:2953977"
FT CONFLICT 74
FT /note="F -> C (in Ref. 1; CAA26356)"
FT /evidence="ECO:0000305"
FT CONFLICT 103..104
FT /note="GD -> DG (in Ref. 1; CAA26356)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="R -> P (in Ref. 1; CAA26356)"
FT /evidence="ECO:0000305"
FT CONFLICT 317..319
FT /note="KKL -> EKM (in Ref. 1; CAA26356)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1PFK"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:1PFK"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1PFK"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:1PFK"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1PFK"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1PFK"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1PFK"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:1PFK"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:1PFK"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:1PFK"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:1PFK"
FT HELIX 140..161
FT /evidence="ECO:0007829|PDB:1PFK"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:1PFK"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:1PFK"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1PFK"
FT HELIX 199..211
FT /evidence="ECO:0007829|PDB:1PFK"
FT STRAND 217..226
FT /evidence="ECO:0007829|PDB:1PFK"
FT HELIX 228..239
FT /evidence="ECO:0007829|PDB:1PFK"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:1PFK"
FT HELIX 249..253
FT /evidence="ECO:0007829|PDB:1PFK"
FT HELIX 259..277
FT /evidence="ECO:0007829|PDB:1PFK"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:1PFK"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:1PFK"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:1PFK"
FT HELIX 310..319
FT /evidence="ECO:0007829|PDB:1PFK"
SQ SEQUENCE 320 AA; 34842 MW; D03D79F6A5536A41 CRC64;
MIKKIGVLTS GGDAPGMNAA IRGVVRSALT EGLEVMGIYD GYLGLYEDRM VQLDRYSVSD
MINRGGTFLG SARFPEFRDE NIRAVAIENL KKRGIDALVV IGGDGSYMGA MRLTEMGFPC
IGLPGTIDND IKGTDYTIGF FTALSTVVEA IDRLRDTSSS HQRISVVEVM GRYCGDLTLA
AAIAGGCEFV VVPEVEFSRE DLVNEIKAGI AKGKKHAIVA ITEHMCDVDE LAHFIEKETG
RETRATVLGH IQRGGSPVPY DRILASRMGA YAIDLLLAGY GGRCVGIQNE QLVHHDIIDA
IENMKRPFKG DWLDCAKKLY
