ID D4K3T3_9FIRM Unreviewed; 407 AA.
AC D4K3T3;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 62.
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 ORFNames=FP2_05420 {ECO:0000313|EMBL:CBK98176.1};
OS Faecalibacterium prausnitzii L2-6.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=718252 {ECO:0000313|EMBL:CBK98176.1, ECO:0000313|Proteomes:UP000008804};
RN [1] {ECO:0000313|EMBL:CBK98176.1, ECO:0000313|Proteomes:UP000008804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-6 {ECO:0000313|Proteomes:UP000008804};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Faecalibacterium prausnitzii L2/6.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK98176.1, ECO:0000313|Proteomes:UP000008804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-6 {ECO:0000313|Proteomes:UP000008804};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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|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|HAMAP-Rule:MF_01978};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01978}.
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DR EMBL; FP929045; CBK98176.1; -; Genomic_DNA.
DR AlphaFoldDB; D4K3T3; -.
DR STRING; 718252.FP2_05420; -.
DR KEGG; fpr:FP2_05420; -.
DR PATRIC; fig|718252.3.peg.1755; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_1_1_9; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000008804; 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:UP000008804};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01978}.
FT DOMAIN 4..306
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT BINDING 12
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978"
FT BINDING 141..143
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 SITE 114
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 140
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 407 AA; 43781 MW; 8C197F9F05C7C3B8 CRC64;
MARNVIIGQS GGPTAVINSS LAGVYKAACS LGADKVYGMK YGIEGLLKEE LVELNVLLDD
RLSIELLKRT PSSYLGSCRY KLPEPEADST PYVKLFALFD KYDICAVFYI GGNDSMDTIA
KLSRYGAQAG SAVRFIGVPK TIDNDLCLTD HTPGYGSAAK YIATILKEVI RDSSVYDIRS
VTVAEIMGRH AGWLAGAACL AGGDDSDGPD LILLPEVPFD QDKFLARVDA LQRVKPNVII
AASEGVKTAD GTYLCDLVST AGQLDAFGHK AILSGTSRYL SDLIHDKLNC KSRAIEFSTL
QRCASHLASR TDVNEAYAVG GAAAAAAFAG ETGKMIALKR ISEYPYQCIT EAVDVQQVAN
LEKKVPLDWI TPDGMQVTAA FEEYARPLIL DEVTPVYVNG TPRHICL
//
