ID   C3W301_9GAMM            Unreviewed;       248 AA.
AC   C3W301;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Phosphofructokinase {ECO:0000313|EMBL:ACQ45510.1};
DE   Flags: Fragment;
OS   Ectenagena extenta gill symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=72605 {ECO:0000313|EMBL:ACQ45510.1};
RN   [1] {ECO:0000313|EMBL:ACQ45510.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19289597; DOI=10.1093/molbev/msp049;
RA   Stewart F.J., Young C.R., Cavanaugh C.M.;
RT   "Evidence for homologous recombination in intracellular chemosynthetic clam
RT   symbionts.";
RL   Mol. Biol. Evol. 0:0-0(2009).
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; FJ900022; ACQ45510.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3W301; -.
DR   UniPathway; UPA00109; UER00182.
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   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   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACQ45510.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..244
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACQ45510.1"
FT   NON_TER         248
FT                   /evidence="ECO:0000313|EMBL:ACQ45510.1"
SQ   SEQUENCE   248 AA;  26761 MW;  028E63E427422F0C CRC64;
     ETARKHSNKI GTVYAGKNGI IGALTENLID TSKESSADIK ALKHTPSGGF GSCRYKMKSL
     ETNKAEYERL IEVFKAHNIC YFFYNGGGDS ADTCLKVSQL SESMGYPIQA IHIPKTVDND
     LPITDNSPGF GSVAKYIAVS TMEASFDVAS MAATSTKIFV LEVMGRNAGW IASAGGLVDK
     SIPVVILFPE VGFDEKKFLA KVDKNVKEFG YCTIVVSEGA KWLDGRFLSE QNTHDDFGHA
     QLGGVAPI
//