ID   G7UTD0_PSEUP            Unreviewed;       418 AA.
AC   G7UTD0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01978};
DE            EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01978};
DE   AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01978};
DE   AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01978};
DE            Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01978};
DE   AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01978};
GN   Name=pfp {ECO:0000256|HAMAP-Rule:MF_01978};
GN   OrderedLocusNames=DSC_13660 {ECO:0000313|EMBL:AER57376.1};
OS   Pseudoxanthomonas spadix (strain BD-a59).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER57376.1, ECO:0000313|Proteomes:UP000005870};
RN   [1] {ECO:0000313|EMBL:AER57376.1, ECO:0000313|Proteomes:UP000005870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD-a59 {ECO:0000313|EMBL:AER57376.1,
RC   ECO:0000313|Proteomes:UP000005870};
RX   PubMed=22207748; DOI=10.1128/JB.06436-11;
RA   Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT   "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT   spadix BD-a59.";
RL   J. Bacteriol. 194:544-544(2012).
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:0000256|ARBA:ARBA00003138, ECO:0000256|HAMAP-Rule:MF_01978}.
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:0000256|ARBA:ARBA00000628, ECO:0000256|HAMAP-
CC         Rule:MF_01978};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP-
CC         Rule:MF_01978};
CC   -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_01978}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000256|HAMAP-Rule:MF_01978}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01978}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01978}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       PPi-dependent PFK group II subfamily. Clade 'B2' sub-subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01978}.
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DR   EMBL; CP003093; AER57376.1; -; Genomic_DNA.
DR   RefSeq; WP_014161549.1; NC_016147.2.
DR   AlphaFoldDB; G7UTD0; -.
DR   STRING; 1045855.DSC_13660; -.
DR   KEGG; psd:DSC_13660; -.
DR   eggNOG; COG0205; Bacteria.
DR   HOGENOM; CLU_020655_1_1_6; -.
DR   OrthoDB; 9802503at2; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000005870; Chromosome.
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   Gene3D; 3.40.50.450; -; 1.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 1.
DR   HAMAP; MF_01978; Phosphofructokinase_II_B2; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   InterPro; IPR011404; PPi-PFK.
DR   PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR   PANTHER; PTHR45770:SF11; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF036483; PFK_XF0274; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01978};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01978};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01978};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01978};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01978}; Reference proteome {ECO:0000313|Proteomes:UP000005870};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01978}.
FT   DOMAIN          8..299
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   ACT_SITE        141
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT   BINDING         13
FT                   /ligand="diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:33019"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT   BINDING         111
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT   BINDING         139..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT   BINDING         187..189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT   BINDING         244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT   BINDING         295..298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT   SITE            112
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:0000256|HAMAP-Rule:MF_01978"
FT   SITE            138
FT                   /note="Important for catalytic activity; stabilizes the
FT                   transition state when the phosphoryl donor is PPi"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
SQ   SEQUENCE   418 AA;  44347 MW;  EDA7D3432531F15A CRC64;
     MVQSTLLYAQ SGGVTAVINA TASAVISEAR RRKVKVLAAR NGILGALREE LIDTSRESIS
     AIRALAHTPG GAFGSCRVKL KSLEADRDRY ARLLEVFKAH NVRWFLYNGG NDSADTAWKV
     SQLAQAFDYP LTCVGVPKTI DNDLAVTDTC PGFGSAAKYT AVSVRECALD VAAMAQTSTK
     VFVYEAMGRH AGWLAAAAGL AGAAADEAPH IILFPERAYD QAAFLAQVDK VVKQVGYCVV
     VASEGIRNAD GTFVADAGGA ADAFGHAQLG GVAASLAGTV KASLGYKVHW ALPDYLQRSA
     RHIASKTDWA QAQAVGKAAV QYALKGMNAV MPVIVRSADA PYRWKIAPAP LSKVANHEKT
     MPASFIRKDG FGITANARKY LAPLIKGEAP LPYGADGLPR YVTLKNVAVK KKLPAWED
//