PFP_DICTH
ID PFP_DICTH Reviewed; 346 AA.
AC Q9KH71;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01976};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01976};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01976};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01976};
DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01976};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01976};
GN Name=pfp {ECO:0000255|HAMAP-Rule:MF_01976};
OS Dictyoglomus thermophilum.
OC Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX NCBI_TaxID=14;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Rt46 B.1;
RX PubMed=10913106; DOI=10.1128/jb.182.16.4661-4666.2000;
RA Ding Y.-H.R., Ronimus R.S., Morgan H.W.;
RT "Sequencing, cloning, and high-level expression of the pfp gene, encoding a
RT ppi-dependent phosphofructokinase from the extremely thermophilic
RT eubacterium Dictyoglomus thermophilum.";
RL J. Bacteriol. 182:4661-4666(2000).
RN [2]
RP PROTEIN SEQUENCE OF 2-22, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=Rt46 B.1;
RX PubMed=10356999; DOI=10.1007/s007920050108;
RA Ding Y.H., Ronimus R.S., Morgan H.W.;
RT "Purification and properties of the pyrophosphate-dependent
RT phosphofructokinase from Dictyoglomus thermophilum Rt46 B.1.";
RL Extremophiles 3:131-137(1999).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the
CC first committing step of glycolysis. Uses inorganic phosphate (PPi) as
CC phosphoryl donor instead of ATP like common ATP-dependent
CC phosphofructokinases (ATP-PFKs), which renders the reaction reversible,
CC and can thus function both in glycolysis and gluconeogenesis.
CC Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-
CC PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
CC {ECO:0000255|HAMAP-Rule:MF_01976, ECO:0000269|PubMed:10356999}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose
CC 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01976};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01976,
CC ECO:0000269|PubMed:10356999};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|HAMAP-Rule:MF_01976,
CC ECO:0000269|PubMed:10356999}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.3 mM for phosphate {ECO:0000269|PubMed:10356999};
CC KM=0.022 mM for diphosphate {ECO:0000269|PubMed:10356999};
CC KM=0.220 mM for tripolyphosphate {ECO:0000269|PubMed:10356999};
CC KM=0.228 mM for fructose 6-phosphate {ECO:0000269|PubMed:10356999};
CC KM=2.9 mM for fructose 1,6-bisphosphate
CC {ECO:0000269|PubMed:10356999};
CC Vmax=4.62 umol/min/mg enzyme for the forward reaction
CC {ECO:0000269|PubMed:10356999};
CC Vmax=0.15 umol/min/mg enzyme for the reverse reaction
CC {ECO:0000269|PubMed:10356999};
CC pH dependence:
CC Optimum pH is 5.7-6.3 for the forward reaction and 7.0-7.5 for the
CC reverse reaction. {ECO:0000269|PubMed:10356999};
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_01976}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10356999}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC Mixed-substrate PFK group III subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01976}.
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DR EMBL; AF268276; AAF80100.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9KH71; -.
DR SMR; Q9KH71; -.
DR PRIDE; Q9KH71; -.
DR SABIO-RK; Q9KH71; -.
DR UniPathway; UPA00109; UER00182.
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:InterPro.
DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.460; -; 1.
DR HAMAP; MF_01976; Phosphofructokinase_III; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR012003; ATP_PFK_prok-type.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR012829; Phosphofructokinase_III.
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; TIGR02483; PFK_mixed; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10356999"
FT CHAIN 2..346
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000112012"
FT ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 13
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 127..129
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 164
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 171..173
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 224
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 269
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 275..278
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT SITE 106
FT /note="Important for catalytic activity and substrate
FT specificity; stabilizes the transition state when the
FT phosphoryl donor is PPi; prevents ATP from binding by
FT mimicking the alpha-phosphate group of ATP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT SITE 126
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
SQ SEQUENCE 346 AA; 37448 MW; 50C03B64BA7927F1 CRC64;
MSKMRIGVLT GGGDCPGLNP AIRGIVMRAL DYGDEVIGLK YGWAGLLKAD TMPLSLEMVE
DILEIGGTIL GSSRTNPFKK EEDVQKCVEN FKKLNLDALI AIGGEDTLGV ASKFSKLGLP
MIGVPKTIDK DLEETDYTLG FDTAVEVVVD AIKRLRDTAR SHARVIVVEI MGRHAGWLAL
YGGLAGGADY ILIPEVEPNL EDLYNHIRKL YARGRNHAVV AIAEGVQLPG FTYQKGQEGM
VDAFGHIRLG GVGNVLAEEI QKNLGIETRA VILSHLQRGG SPSIRDRIMG LLLGKKAVDL
VHEGKSGLFV AVKGNELVPV DITLIEGKTK NVDPAFYESV KTFFNK
