ID PFP_THEMA Reviewed; 419 AA.
AC Q9WYC5; G4FHK3;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01979};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01979};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01979};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01979};
DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01979};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01979};
GN Name=pfp {ECO:0000255|HAMAP-Rule:MF_01979}; OrderedLocusNames=TM_0289;
GN ORFNames=THEMA_03280, Tmari_0287;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485;
RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H.,
RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y.,
RA Zengler K.;
RT "The genome organization of Thermotoga maritima reflects its lifestyle.";
RL PLoS Genet. 9:E1003485-E1003485(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RG DOE Joint Genome Institute;
RA Noll K.M., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=11133978; DOI=10.1128/jb.183.2.791-794.2001;
RA Ding Y.R., Ronimus R.S., Morgan H.W.;
RT "Thermotoga maritima phosphofructokinases: expression and characterization
RT of two unique enzymes.";
RL J. Bacteriol. 183:791-794(2001).
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_01979, ECO:0000269|PubMed:11133978}.
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_01979,
CC ECO:0000269|PubMed:11133978};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01979,
CC ECO:0000269|PubMed:11133978};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01979,
CC ECO:0000269|PubMed:11133978};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01979,
CC ECO:0000269|PubMed:11133978};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01979,
CC ECO:0000269|PubMed:11133978};
CC Note=Mg(2+) can be partially replaced by Co(2+), Mn(2+) and Ni(2+).
CC {ECO:0000255|HAMAP-Rule:MF_01979, ECO:0000269|PubMed:11133978};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|HAMAP-Rule:MF_01979,
CC ECO:0000269|PubMed:11133978}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.067 mM for diphosphate {ECO:0000269|PubMed:11133978};
CC KM=0.01 mM for tripolyphosphate {ECO:0000269|PubMed:11133978};
CC KM=0.0038 mM for polyphosphate {ECO:0000269|PubMed:11133978};
CC KM=0.98 mM for fructose 6-phosphate {ECO:0000269|PubMed:11133978};
CC Vmax=203 umol/min/mg enzyme with diphosphate as substrate
CC {ECO:0000269|PubMed:11133978};
CC Vmax=249 umol/min/mg enzyme with triphosphate as substrate
CC {ECO:0000269|PubMed:11133978};
CC Vmax=319 umol/min/mg enzyme with polyphosphate as substrate
CC {ECO:0000269|PubMed:11133978};
CC pH dependence:
CC Optimum pH is 5.6-5.8 for the forward reaction, and 5.6-6.8 for the
CC reverse reaction. {ECO:0000269|PubMed:11133978};
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_01979}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01979,
CC ECO:0000269|PubMed:11133978}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01979}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'Short' sub-subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01979}.
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DR EMBL; AE000512; AAD35377.1; -; Genomic_DNA.
DR EMBL; CP004077; AGL49213.1; -; Genomic_DNA.
DR EMBL; CP007013; AHD17947.1; -; Genomic_DNA.
DR PIR; G72396; G72396.
DR RefSeq; NP_228101.1; NC_000853.1.
DR RefSeq; WP_004083005.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WYC5; -.
DR SMR; Q9WYC5; -.
DR STRING; 243274.TM_0289; -.
DR PaxDb; 243274-THEMA_03280; -.
DR EnsemblBacteria; AAD35377; AAD35377; TM_0289.
DR KEGG; tma:TM0289; -.
DR KEGG; tmi:THEMA_03280; -.
DR KEGG; tmm:Tmari_0287; -.
DR KEGG; tmw:THMA_0296; -.
DR PATRIC; fig|243274.17.peg.286; -.
DR eggNOG; COG0205; Bacteria.
DR InParanoid; Q9WYC5; -.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000008183; 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:0008443; F:phosphofructokinase activity; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0009749; P:response to glucose; IBA:GO_Central.
DR Gene3D; 3.40.50.450; -; 1.
DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 1.
DR HAMAP; MF_01979; Phosphofructokinase_II_Short; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR011403; PPi-PFK_TM0289.
DR NCBIfam; NF041103; PFKA_PPi_Ttgales; 1.
DR PANTHER; PTHR43650; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR43650:SF1; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE SUBUNIT BETA 1; 1.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF036482; PPi_PFK_TM0289; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..419
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000429700"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 12
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 132..134
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 178..180
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 300..303
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT SITE 108
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_01979"
FT SITE 131
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
SQ SEQUENCE 419 AA; 46465 MW; 4E3FBC75A8410CEC CRC64;
MAERLGILVG GGPAPGINSV ISSVTIEAIN NGLEVIGIYD GFKHLVEGKT NMVKKLSIED
VSRIHIEGGS ILRTSRVNPA KSEETLEKTV QTLKKLGIKY LVTIGGDDTA FSASKVCERS
KGEIKVVHVP KTIDNDLPLP ENMPTFGFET ARHVATELVY NLMQDSRTTN RWYFVAMMGR
EAGHLALGVG KAASATITII PEEFKEGVTL EEVCDVLDGA ILKRKLMGRD DGVAVIGEGI
AEKMDPEELA NIPGVIVEKD PHGHLRLAEI PLATILKRAI ERRYAERGER IHIVDVTIGY
ELRSARPIPF DIVYTRTLGY GAVRFLLGDY SDLPGGMVCV VGGRIKILPF DAFMDPKTGR
TKVRVVDVRS EDYRVARKYM IRLEKKDLED PETLEKLAKL AKMEPEEFKK KYWHTTELP
//
