PFP_SPITD
ID PFP_SPITD Reviewed; 554 AA.
AC Q9EZ02; E0RP22;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
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};
GN OrderedLocusNames=STHERM_c17480;
OS Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1).
OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta.
OX NCBI_TaxID=665571;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, COFACTOR, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11382227; DOI=10.1007/s002030100265;
RA Ronimus R., de Heus E., Ruckert A., Morgan H.;
RT "Sequencing, high-level expression and phylogeny of the pyrophosphate-
RT dependent phosphofructokinase from the thermophilic spirochete Spirochaeta
RT thermophila.";
RL Arch. Microbiol. 175:308-312(2001).
RN [2]
RP PROTEIN SEQUENCE OF 1-35, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 49972 / DSM 6192 / RI 19.B1;
RX PubMed=10591850; DOI=10.1007/s002030050777;
RA Ronimus R.S., Morgan H.W., Ding Y.R.;
RT "Phosphofructokinase activities within the order spirochaetales and the
RT characterisation of the pyrophosphate-dependent phosphofructokinase from
RT spirochaeta thermophila.";
RL Arch. Microbiol. 172:401-406(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49972 / DSM 6192 / RI 19.B1;
RX PubMed=20935097; DOI=10.1128/jb.01023-10;
RA Angelov A., Liebl S., Ballschmiter M., Bomeke M., Lehmann R., Liesegang H.,
RA Daniel R., Liebl W.;
RT "Genome sequence of the polysaccharide-degrading, thermophilic anaerobe
RT Spirochaeta thermophila DSM 6192.";
RL J. Bacteriol. 192:6492-6493(2010).
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:10591850}.
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:10591850};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01980,
CC ECO:0000269|PubMed:10591850, ECO:0000269|PubMed:11382227};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|HAMAP-Rule:MF_01980,
CC ECO:0000269|PubMed:10591850}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=400 uM for phosphate {ECO:0000269|PubMed:10591850,
CC ECO:0000269|PubMed:11382227};
CC KM=110 uM for diphosphate {ECO:0000269|PubMed:10591850,
CC ECO:0000269|PubMed:11382227};
CC KM=170 uM for tripolyphosphate {ECO:0000269|PubMed:10591850,
CC ECO:0000269|PubMed:11382227};
CC KM=430 uM for polyphosphate {ECO:0000269|PubMed:10591850,
CC ECO:0000269|PubMed:11382227};
CC KM=240 uM for fructose 6-phosphate {ECO:0000269|PubMed:10591850,
CC ECO:0000269|PubMed:11382227};
CC KM=38 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:10591850,
CC ECO:0000269|PubMed:11382227};
CC Vmax=438 umol/min/mg enzyme for the forward reaction
CC {ECO:0000269|PubMed:10591850, ECO:0000269|PubMed:11382227};
CC Vmax=239 umol/min/mg enzyme for the reverse reaction
CC {ECO:0000269|PubMed:10591850, ECO:0000269|PubMed:11382227};
CC pH dependence:
CC Optimum pH is 5.0-6.0 for the forward reaction and 7.0-7.5 for the
CC reverse reaction. {ECO:0000269|PubMed:10591850,
CC ECO:0000269|PubMed:11382227};
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 ECO:0000269|PubMed:11382227}.
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; AF307859; AAG37271.1; -; Genomic_DNA.
DR EMBL; CP001698; ADN02683.1; -; Genomic_DNA.
DR RefSeq; WP_013314522.1; NC_014484.1.
DR AlphaFoldDB; Q9EZ02; -.
DR SMR; Q9EZ02; -.
DR STRING; 665571.STHERM_c17480; -.
DR PRIDE; Q9EZ02; -.
DR EnsemblBacteria; ADN02683; ADN02683; STHERM_c17480.
DR KEGG; sta:STHERM_c17480; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_022288_0_1_12; -.
DR OMA; SAKKYWH; -.
DR SABIO-RK; Q9EZ02; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000001296; Chromosome.
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; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IDA:UniProtKB.
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; Direct protein sequencing; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Transferase.
FT CHAIN 1..554
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000429056"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 82
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 204..206
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 243..244
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01980"
FT BINDING 251..253
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 312
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 426..429
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 177
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 203
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 554 AA; 61080 MW; 01B1F21B5A72685C CRC64;
MTRISPLQKA RYGYVPKLPP VLQDEIARIQ AELGQPTEAV ADREDLKRLF ANTYGKPIAT
LTRGSNPEAG RRRTVGVILS GGPAPGGHNV ICGLFDALKK ANRESTLIGF KGGPSGILDD
EWIEFTDSLI NQYRNTGGFD IIGSGRTKIE TPEQFAKALE NAKKHGLDAL VIIGGDDSNT
NAALLAEYFV QQGAPIQVIG IPKTIDGDLK NEYIEASFGF DTATKVYAEL IGNIARDAIS
SRKYWHFIRL MGRSASHIAL ECALQTHPNV CIVSEEVREK NMTLSQIVDQ IVDAVVKRAA
KGENFGVVLV PEGLIEFIPE VGALIDELNT LLAKEAEVFN RIDDPRERIS WVKGKLSGNN
QHVFSSLPET IQAQLLMDRD PHGNVQVSRI ETEKLLIEMV SSRLKALKEE GAYKGKFSAL
NHFFGYEARC AFPSNFDADY CYALGFTAFV LIANGLTGYI AAIKNLARPA VEWKPMGIPL
TMMMNMEKRH GKMKPVIRKA LVDLEGAPFK RFATQRDAWA TESAYVFPGA IQYYGPDDVC
NQPTMTLKLE QGLE
