PFP_MASBA
ID PFP_MASBA Reviewed; 410 AA.
AC Q9NGP6;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01977};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01977};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01977};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01977};
DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01977};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01977};
OS Mastigamoeba balamuthi (Phreatamoeba balamuthi).
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Mastigamoebidae;
OC Mastigamoeba.
OX NCBI_TaxID=108607;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11673446; DOI=10.1128/jb.183.22.6714-6716.2001;
RA Muller M., Lee J.A., Gordon P., Gaasterland T., Sensen C.W.;
RT "Presence of prokaryotic and eukaryotic species in all subgroups of the
RT PP(i)-dependent group II phosphofructokinase protein family.";
RL J. Bacteriol. 183:6714-6716(2001).
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_01977}.
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_01977};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01977};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|HAMAP-Rule:MF_01977}.
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_01977}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01977}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01977}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'P' sub-subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01977}.
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DR EMBL; AF246209; AAF70463.1; -; mRNA.
DR AlphaFoldDB; Q9NGP6; -.
DR SMR; Q9NGP6; -.
DR VEuPathDB; AmoebaDB:MBAL_010012; -.
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: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 HAMAP; MF_01977; Phosphofructokinase_II_P; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR011405; PPi-PFK_SMc01852.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF036484; PPi-PFK_SMc01852; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..410
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000429705"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 12
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 149..151
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 194..196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 323..326
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT SITE 122
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_01977"
FT SITE 148
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
SQ SEQUENCE 410 AA; 44201 MW; CD362D1D2D41A0D0 CRC64;
MVKTVALLTA GGLAPCLSSA VGGLIERYTE MSPETNIILY LNGYKGLLLG EKVLVTPAMR
LQAHVLHTVG GSCIGNSRVK MANVADCVKR GLVKEGQDPR QVAADQLIKD GVDVLHTIGG
DDTNTAAADL AAYLKAHGYT LRVIGLPKTI DNDIVPVRQS LGAMTAAEQA SRFFQNVVAE
QTANPRVLLV HEVMGRSCGY LTAQAADYYR AQLAHREFAP ELGHTRERYD IHAVYVPEMT
IDLKAEAARL RAVMERVGCV NIFLSEGAGI NDIVAEMTAK GETVPRDPFG HVKIDLINPG
AWFGKQFGGM VGADKVLVQK SGYFSRSAPA NAEDLRLIKG MVDLAVDCAL RGEAGLIGHD
EERNGVLRAI EFERVKGAKA FNIDHPWFTH LLNEIGQPKG AKVSVAHGDE
