(data stored in SCRATCH zone)

SWISSPROT: PFKA_GEOSE

ID   PFKA_GEOSE              Reviewed;         319 AA.
AC   P00512;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   11-DEC-2019, entry version 150.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339};
DE            Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_00339};
DE            Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_00339};
DE   AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_00339};
GN   Name=pfkA {ECO:0000255|HAMAP-Rule:MF_00339}; Synonyms=pfk;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2956156; DOI=10.1016/0378-1119(87)90348-9;
RA   French B.A., Chang S.H.;
RT   "Nucleotide sequence of the phosphofructokinase gene from Bacillus
RT   stearothermophilus and comparison with the homologous Escherichia coli
RT   gene.";
RL   Gene 54:65-71(1987).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   PubMed=6447595; DOI=10.1111/j.1432-1033.1980.tb04754.x;
RA   Kolb E., Hudson P.J., Harris J.I.;
RT   "Phosphofructokinase: complete amino-acid sequence of the enzyme from
RT   Bacillus stearothermophilus.";
RL   Eur. J. Biochem. 108:587-597(1980).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 300-319.
RX   PubMed=8436141; DOI=10.1111/j.1432-1033.1993.tb17618.x;
RA   Sakai H., Ohta T.;
RT   "Molecular cloning and nucleotide sequence of the gene for pyruvate kinase
RT   of Bacillus stearothermophilus and the production of the enzyme in
RT   Escherichia coli. Evidence that the genes for phosphofructokinase and
RT   pyruvate kinase constitute an operon.";
RL   Eur. J. Biochem. 211:851-859(1993).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=8136379; DOI=10.1021/bi00177a036;
RA   Byrnes M., Zhu X., Younathan E.S., Chang S.H.;
RT   "Kinetic characteristics of phosphofructokinase from Bacillus
RT   stearothermophilus: MgATP nonallosterically inhibits the enzyme.";
RL   Biochemistry 33:3424-3431(1994).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   PubMed=156307; DOI=10.1038/279500a0;
RA   Evans P.R., Hudson P.J.;
RT   "Structure and control of phosphofructokinase from Bacillus
RT   stearothermophilus.";
RL   Nature 279:500-504(1979).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH MAGNESIUM; ADP AND
RP   FRUCTOSE-6-PHOSPHATE.
RX   PubMed=6115424; DOI=10.1098/rstb.1981.0059;
RA   Evans P.R., Farrants G.W., Hudson P.J.;
RT   "Phosphofructokinase: structure and control.";
RL   Philos. Trans. R. Soc. Lond., B, Biol. Sci. 293:53-62(1981).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ALLOSTERIC INHIBITOR.
RX   PubMed=2136935; DOI=10.1038/343140a0;
RA   Schirmer T., Evans P.R.;
RT   "Structural basis of the allosteric behaviour of phosphofructokinase.";
RL   Nature 343:140-145(1990).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-6-PHOSPHATE.
RX   PubMed=12390023; DOI=10.1021/bi0263412;
RA   Riley-Lovingshimer M.R., Ronning D.R., Sacchettini J.C., Reinhart G.D.;
RT   "Reversible ligand-induced dissociation of a tryptophan-shift mutant of
RT   phosphofructokinase from Bacillus stearothermophilus.";
RL   Biochemistry 41:12967-12974(2002).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS).
RX   PubMed=22212099; DOI=10.1021/bi201548p;
RA   Mosser R., Reddy M.C., Bruning J.B., Sacchettini J.C., Reinhart G.D.;
RT   "Structure of the apo form of Bacillus stearothermophilus
RT   phosphofructokinase.";
RL   Biochemistry 51:769-775(2012).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH PHOSPHOENOLPYRUVIC
RP   ACID.
RX   PubMed=23859543; DOI=10.1021/bi4002503;
RA   Mosser R., Reddy M.C., Bruning J.B., Sacchettini J.C., Reinhart G.D.;
RT   "Redefining the role of the quaternary shift in Bacillus stearothermophilus
RT   phosphofructokinase.";
RL   Biochemistry 52:5421-5429(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:0000255|HAMAP-Rule:MF_00339,
CC       ECO:0000269|PubMed:8136379}.
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, ECO:0000269|PubMed:8136379};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00339,
CC         ECO:0000269|PubMed:6115424};
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP and other
CC       diphosphonucleosides, and allosterically inhibited by
CC       phosphoenolpyruvate. {ECO:0000255|HAMAP-Rule:MF_00339,
CC       ECO:0000269|PubMed:2136935, ECO:0000269|PubMed:23859543,
CC       ECO:0000305|PubMed:8136379}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.07 mM for ATP {ECO:0000269|PubMed:8136379};
CC         KM=0.033 mM for fructose 6-phosphate {ECO:0000269|PubMed:8136379};
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:12390023, ECO:0000269|PubMed:2136935,
CC       ECO:0000269|PubMed:23859543, ECO:0000269|PubMed:6115424}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339}.
CC   -!- MISCELLANEOUS: In the R state the 6-P group of fructose 6-phosphate
CC       (F6P) is bound by His-249 from one chain and Arg-162 and Arg-243 from
CC       an adjacent chain. In the T state a conformation change moves Arg-162
CC       away from the substrate. Glu-161 takes its place, hence repelling the
CC       phosphate of ATP. {ECO:0000305|PubMed:2136935}.
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}.
DR   EMBL; M15643; AAA22656.1; -; Genomic_DNA.
DR   EMBL; D13095; BAA02405.1; -; Genomic_DNA.
DR   PIR; A27474; KIBSFF.
DR   RefSeq; WP_033014452.1; NZ_RCTK01000004.1.
DR   PDB; 1MTO; X-ray; 3.20 A; A/B/C/D/E/F/G/H=1-319.
DR   PDB; 3PFK; X-ray; 2.40 A; A=1-319.
DR   PDB; 3U39; X-ray; 2.79 A; A/B/C/D=1-319.
DR   PDB; 4I36; X-ray; 2.30 A; A/B/C/D=1-319.
DR   PDB; 4I4I; X-ray; 2.49 A; A/B/C/D=1-319.
DR   PDB; 4I7E; X-ray; 2.00 A; A/B/C/D=1-319.
DR   PDB; 4PFK; X-ray; 2.40 A; A=1-319.
DR   PDB; 6PFK; X-ray; 2.60 A; A/B/C/D=1-319.
DR   PDBsum; 1MTO; -.
DR   PDBsum; 3PFK; -.
DR   PDBsum; 3U39; -.
DR   PDBsum; 4I36; -.
DR   PDBsum; 4I4I; -.
DR   PDBsum; 4I7E; -.
DR   PDBsum; 4PFK; -.
DR   PDBsum; 6PFK; -.
DR   SMR; P00512; -.
DR   DrugBank; DB02726; 2-Phosphoglycolic Acid.
DR   DrugBank; DB04493; Fructose-6-Phosphate.
DR   DrugBank; DB09344; Invert sugar.
DR   PRIDE; P00512; -.
DR   BRENDA; 2.7.1.11; 623.
DR   SABIO-RK; P00512; -.
DR   UniPathway; UPA00109; UER00182.
DR   EvolutionaryTrace; P00512; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   CDD; cd00763; Bacterial_PFK; 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;
DR   PRODOM; P00512.
DR   SWISS-2DPAGE; P00512.
KW   3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..319
FT                   /note="ATP-dependent 6-phosphofructokinase"
FT                   /id="PRO_0000111935"
FT   NP_BIND         72..73
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT                   ECO:0000269|PubMed:6115424"
FT   NP_BIND         102..105
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   REGION          21..25
FT                   /note="Allosteric activator ADP binding; shared with
FT                   dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT                   ECO:0000269|PubMed:6115424"
FT   REGION          125..127
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT                   ECO:0000269|PubMed:12390023, ECO:0000269|PubMed:6115424"
FT   REGION          169..171
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT                   ECO:0000269|PubMed:12390023, ECO:0000269|PubMed:6115424"
FT   REGION          185..187
FT                   /note="Allosteric activator ADP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT                   ECO:0000269|PubMed:6115424"
FT   REGION          213..215
FT                   /note="Allosteric activator ADP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT                   ECO:0000269|PubMed:6115424"
FT   REGION          249..252
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT                   ECO:0000269|PubMed:12390023, ECO:0000269|PubMed:6115424"
FT   ACT_SITE        127
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   METAL           103
FT                   /note="Magnesium; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT                   ECO:0000269|PubMed:6115424"
FT   BINDING         11
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         59
FT                   /note="Allosteric activator ADP; shared with dimeric
FT                   partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT                   ECO:0000269|PubMed:6115424"
FT   BINDING         154
FT                   /note="Allosteric activator ADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT                   ECO:0000269|PubMed:6115424"
FT   BINDING         162
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT                   ECO:0000269|PubMed:6115424"
FT   BINDING         211
FT                   /note="Allosteric activator ADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT                   ECO:0000269|PubMed:6115424"
FT   BINDING         222
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT                   ECO:0000269|PubMed:12390023, ECO:0000269|PubMed:6115424"
FT   BINDING         243
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT                   ECO:0000269|PubMed:12390023, ECO:0000269|PubMed:6115424"
FT   CONFLICT        12
FT                   /note="D -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        35..37
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43
FT                   /note="G -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82
FT                   /note="Q -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="E -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="G -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..11
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   HELIX           16..29
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   STRAND          33..37
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   HELIX           40..46
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   STRAND          49..52
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   HELIX           54..57
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   HELIX           74..77
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   HELIX           81..91
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   STRAND          97..102
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   HELIX           103..114
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   STRAND          119..127
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   HELIX           139..153
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   STRAND          159..168
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   HELIX           175..183
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   STRAND          187..190
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   HELIX           198..210
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   STRAND          216..221
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   TURN            222..224
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   HELIX           227..238
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   STRAND          241..246
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   HELIX           248..252
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   HELIX           258..277
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   STRAND          281..287
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   STRAND          290..295
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   HELIX           296..300
FT                   /evidence="ECO:0000244|PDB:4I7E"
FT   HELIX           308..317
FT                   /evidence="ECO:0000244|PDB:4I7E"
SQ   SEQUENCE   319 AA;  34119 MW;  EE968D39BA30712B CRC64;
     MKRIGVLTSG GDSPGMNAAI RSVVRKAIYH GVEVYGVYHG YAGLIAGNIK KLEVGDVGDI
     IHRGGTILYT ARCPEFKTEE GQKKGIEQLK KHGIEGLVVI GGDGSYQGAK KLTEHGFPCV
     GVPGTIDNDI PGTDFTIGFD TALNTVIDAI DKIRDTATSH ERTYVIEVMG RHAGDIALWS
     GLAGGAETIL IPEADYDMND VIARLKRGHE RGKKHSIIIV AEGVGSGVDF GRQIQEATGF
     ETRVTVLGHV QRGGSPTAFD RVLASRLGAR AVELLLEGKG GRCVGIQNNQ LVDHDIAEAL
     ANKHTIDQRM YALSKELSI
//

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