ID   K0PSX6_9HYPH            Unreviewed;       403 AA.
AC   K0PSX6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   29-MAY-2024, entry version 52.
DE   RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01977};
DE            EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01977};
DE   AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01977};
DE   AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01977};
DE            Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01977};
DE   AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01977};
GN   Name=pfp {ECO:0000256|HAMAP-Rule:MF_01977,
GN   ECO:0000313|EMBL:CCM76968.1};
GN   ORFNames=BN77_4011 {ECO:0000313|EMBL:CCM76968.1};
OS   Rhizobium mesoamericanum STM3625.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=1211777 {ECO:0000313|EMBL:CCM76968.1, ECO:0000313|Proteomes:UP000009319};
RN   [1] {ECO:0000313|EMBL:CCM76968.1, ECO:0000313|Proteomes:UP000009319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM3625 {ECO:0000313|EMBL:CCM76968.1,
RC   ECO:0000313|Proteomes:UP000009319};
RX   PubMed=23405314; DOI=10.1128/genomeA.00066-12;
RA   Moulin L., Mornico D., Melkonian R., Klonowska A.;
RT   "Draft Genome Sequence of Rhizobium mesoamericanum STM3625, a Nitrogen-
RT   Fixing Symbiont of Mimosa pudica Isolated in French Guiana (South
RT   America).";
RL   Genome Announc. 1:e00066-e00112(2013).
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_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:0000256|ARBA:ARBA00000628, ECO:0000256|HAMAP-
CC         Rule:MF_01977};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_01977};
CC   -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01977}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-Rule:MF_01977}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01977}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCM76968.1}.
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DR   EMBL; CANI01000028; CCM76968.1; -; Genomic_DNA.
DR   RefSeq; WP_007534747.1; NZ_HF536772.1.
DR   AlphaFoldDB; K0PSX6; -.
DR   STRING; 1211777.BN77_4011; -.
DR   eggNOG; COG0205; Bacteria.
DR   HOGENOM; CLU_643544_0_0_5; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000009319; Unassembled WGS sequence.
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   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   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; PIRSF036484; PPi-PFK_SMc01852; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01977};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_01977};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01977};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01977};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01977};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01977}.
FT   DOMAIN          5..293
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT   BINDING         13
FT                   /ligand="diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:33019"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT   BINDING         122
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT   BINDING         150..152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT   BINDING         195..197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT   BINDING         324..327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
FT   SITE            123
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_01977"
FT   SITE            149
FT                   /note="Important for catalytic activity; stabilizes the
FT                   transition state when the phosphoryl donor is PPi"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01977"
SQ   SEQUENCE   403 AA;  43227 MW;  1DA92E679949581F CRC64;
     MAKQKVAMLT AGGLAPCLSS AVGGLIERYS DVAPDIELIA YRSGYQGVLL GDSITITADM
     REKAPLLHRY GGSPIGNSRV KLTNAADCVK RGLVKEGENP LRVAAERLAN DGVNILHTIG
     GDDTNTTAAD LAAYLAANGY NLTVVGLPKT VDNDVVPIRQ SLGAWTAAEV GAHFFDNVSN
     EQTAAPRTLI IHEVMGRHCG WLTAATARAY LQRTKSYEYV DGLMTNAKMK SIDAVYLPEM
     AFDLDAEAAR LKDVMDRTGH ATVFVSEGAC LDAIVEEREA AGETIKRDAF GHVKIDTINV
     GGWFQKQFAG LISAERSLVQ KSGYFARSAP ANGDDLRLIQ SMTDLAVESA LNKVSGVTGH
     DEAQNGKLRT IEFPRIKGGK AFDISTTWFG EVMDTIGQKY PAA
//