ID   G2J0Q6_PSEUL            Unreviewed;       391 AA.
AC   G2J0Q6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=6-phosphofructokinase {ECO:0000313|EMBL:BAK76045.1};
GN   OrderedLocusNames=NH8B_1219 {ECO:0000313|EMBL:BAK76045.1};
OS   Pseudogulbenkiania sp. (strain NH8B).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Pseudogulbenkiania.
OX   NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK76045.1, ECO:0000313|Proteomes:UP000001274};
RN   [1] {ECO:0000313|Proteomes:UP000001274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274};
RX   PubMed=22038961; DOI=10.1128/JB.06127-11;
RA   Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.;
RT   "Complete genome sequence of the denitrifying and N(2)O-reducing bacterium
RT   Pseudogulbenkiania sp. strain NH8B.";
RL   J. Bacteriol. 193:6395-6396(2011).
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}.
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};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       {ECO:0000256|ARBA:ARBA00038478}.
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DR   EMBL; AP012224; BAK76045.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2J0Q6; -.
DR   STRING; 748280.NH8B_1219; -.
DR   KEGG; pse:NH8B_1219; -.
DR   eggNOG; COG0205; Bacteria.
DR   HOGENOM; CLU_020655_1_1_4; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000001274; Chromosome.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; 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; 3.40.50.450; -; 1.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
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   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAK76045.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001274};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..303
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
SQ   SEQUENCE   391 AA;  41827 MW;  149EA1CA4DD481B9 CRC64;
     MVNASAQGVI EAARHAGVSL CAARHGLTGL RQGELLDLDA VPQRQWQLLS TLPGTCFGSS
     REMLPPYDSA PETWHQLHDV LRGAGIGTVL LNGGNGSMAT ALRLTEFGLR LGYPLRVIGI
     PKTIDNDLVA THFSPGYPSA AKYLAASVRE LALDVSSLGP GRVMLLETMG RNAGWLAAGC
     AAAARHPGDA PHLLLLPEVP YRPERLLDAL DTCLRQHGHA VLVVAEGVRD DNGVLLAEQP
     YTPGSPFQQL GGAAQRVASY LAQQRGLHVH AAVADCLQRA ARHLVSALDL RLAQAAGRTA
     LEWALRGQSG VMVGLRPARG QEDWEMAAVA LADVADAERL LPASYIGADG FSVSPDFLDY
     LRPLLQGEDW PPFADGLPSY PSLEWPILRW Q
//