PFP_PORGN
ID PFP_PORGN Reviewed; 549 AA.
AC Q9FAF8; Q7BWB9;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01980};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01980};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01980};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01980};
DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01980};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01980};
GN Name=pfp {ECO:0000255|HAMAP-Rule:MF_01980}; Synonyms=pfk;
OS Porphyromonas gingivalis.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=837;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RA Arimoto T., Ansai T., Takehara T.;
RT "Cloning, expression, and characterization of pyrophosphate-dependent
RT phosphofructokinase gene from Porphyromonas gingivalis.";
RL J. Dent. Health 51:281-292(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC BAA-1703 / FDC 381;
RX PubMed=11886747; DOI=10.1111/j.1574-6968.2002.tb11024.x;
RA Arimoto T., Ansai T., Yu W., Turner A.J., Takehara T.;
RT "Kinetic analysis of PPi-dependent phosphofructokinase from Porphyromonas
RT gingivalis.";
RL FEMS Microbiol. Lett. 207:35-38(2002).
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:0000255|HAMAP-Rule:MF_01980, ECO:0000269|PubMed:11886747,
CC ECO:0000269|Ref.1}.
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:0000255|HAMAP-Rule:MF_01980,
CC ECO:0000269|PubMed:11886747};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01980};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|HAMAP-Rule:MF_01980}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 mM for phosphate {ECO:0000269|PubMed:11886747};
CC KM=1 mM for diphosphate {ECO:0000269|PubMed:11886747};
CC KM=2.2 mM for fructose 6-phosphate {ECO:0000269|PubMed:11886747};
CC KM=0.11 mM for fructose 1,6-bisphosphate
CC {ECO:0000269|PubMed:11886747};
CC Vmax=278 umol/min/mg enzyme for the forward reaction
CC {ECO:0000269|PubMed:11886747};
CC Vmax=190 umol/min/mg enzyme for the reverse reaction
CC {ECO:0000269|PubMed:11886747};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_01980}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01980}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01980}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01980}.
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DR EMBL; AB039836; BAB16715.1; -; Genomic_DNA.
DR RefSeq; WP_004583807.1; NZ_QPGS01000032.1.
DR AlphaFoldDB; Q9FAF8; -.
DR SMR; Q9FAF8; -.
DR BRENDA; 2.7.1.90; 756.
DR SABIO-RK; Q9FAF8; -.
DR UniPathway; UPA00109; UER00182.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; 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; 3.40.50.460; -; 1.
DR HAMAP; MF_01980; Phosphofructokinase_II_Long; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR011183; PfpB_PPi_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
DR TIGRFAMs; TIGR02477; PFKA_PPi; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..549
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000429710"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 78
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 200..202
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 239..240
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 247..249
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 308
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 421..424
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT SITE 173
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:0000255|HAMAP-Rule:MF_01980"
FT SITE 199
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
SQ SEQUENCE 549 AA; 61084 MW; 7396AFA621F33D79 CRC64;
MAKSALHLAR MSYQPKMPAS LQGAVKIIEG KATEAVSDKE EIAAIFPRTY GLPLISFAPG
GERTEYPPTN VGVILSGGQA PGGHNVIAGL FDEMKLLNPD SRLFGFLMGP DGLIEHKYRE
LTAEVIDEYR NTGGFDMIGS GRTKLDKPEQ FEAGLEILRE LDIKALVIIG GDDSNTNACI
LAEYYASIDA GIQVIGCPKT IDGDLKNKQI ETSFGFDTAA KVYSELIGNI QRDCNSARKY
WHFIKLMGRS ASHITLECAL QTHPNICIVS EEVEANNYYL DDVVTYIAET VVRRSEAGMN
FGTVLIPEGL IEFLPAMKRL IKELNEFLSQ NDAEFKLIKR SAQRQYIKNK LSPENSRLYD
SLPVDVARQL IADRDPHGNV QVSLIATEKL LADMTAQKLA EWAEEGRFQG RFSTLTHFFG
YEGRCAMPSN FDANYCYCLG RAASILIAAG KTGYMAAIKN TADPVSEWEA GGVPMTMMMN
MERRSGKMKP VIRKALVDMD GEPYRALREM RREWALSTEY VYPGPIQFFG PEHVCDSPTM
TLRLEKNDR
