PFP_PROFC
ID PFP_PROFC Reviewed; 404 AA.
AC P29495; D7GDW5; Q08I84;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01977};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01977};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01977};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01977};
DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01977};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01977};
GN Name=pfp {ECO:0000255|HAMAP-Rule:MF_01977}; Synonyms=pfk;
GN OrderedLocusNames=PFREUD_12040;
OS Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM
OS 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Propionibacterium.
OX NCBI_TaxID=754252;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1653240; DOI=10.1016/s0021-9258(18)55336-9;
RA Ladror U.S., Gollapudi L., Tripathi R.L., Latshaw S.P., Kemp R.G.;
RT "Cloning, sequencing, and expression of pyrophosphate-dependent
RT phosphofructokinase from Propionibacterium freudenreichii.";
RL J. Biol. Chem. 266:16550-16555(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1;
RX PubMed=15507000;
RA Meurice G., Deborde C., Jacob D., Falentin H., Boyaval P., Dimova D.;
RT "In silico exploration of the fructose-6-phosphate phosphorylation step in
RT glycolysis: genomic evidence of the coexistence of an atypical ATP-
RT dependent along with a PPi-dependent phosphofructokinase in
RT Propionibacterium freudenreichii subsp. shermanii.";
RL In Silico Biol. 4:517-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1;
RX PubMed=20668525; DOI=10.1371/journal.pone.0011748;
RA Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S.,
RA Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P.,
RA Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., Gaillardin C.,
RA Lortal S.;
RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy
RT actinobacterium with food and probiotic applications.";
RL PLoS ONE 5:E11748-E11748(2010).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP ACTIVITY REGULATION.
RX PubMed=171261; DOI=10.1016/s0021-9258(19)40727-8;
RA O'Brien W.E., Bowien S., Wood H.G.;
RT "Isolation and characterization of a pyrophosphate-dependent
RT phosphofructokinase from Propionibacterium shermanii.";
RL J. Biol. Chem. 250:8690-8695(1975).
RN [5]
RP IDENTIFICATION OF CRITICAL LYSYL RESIDUES.
RX PubMed=1317210; DOI=10.1021/bi00135a011;
RA Green P.C., Latshaw S.P., Ladror U.S., Kemp R.G.;
RT "Identification of critical lysyl residues in the pyrophosphate-dependent
RT phosphofructo-1-kinase of Propionibacterium freudenreichii.";
RL Biochemistry 31:4815-4821(1992).
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_01977, ECO:0000269|PubMed:171261}.
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_01977,
CC ECO:0000269|PubMed:171261};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01977};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|HAMAP-Rule:MF_01977,
CC ECO:0000269|PubMed:171261}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 mM for phosphate {ECO:0000269|PubMed:171261};
CC KM=0.069 mM for diphosphate {ECO:0000269|PubMed:171261};
CC KM=0.1 mM for fructose 6-phosphate {ECO:0000269|PubMed:171261};
CC KM=0.051 mM for fructose 1,6-bisphosphate
CC {ECO:0000269|PubMed:171261};
CC Vmax=258 umol/min/mg enzyme for the forward reaction
CC {ECO:0000269|PubMed:171261};
CC Vmax=232 umol/min/mg enzyme for the reverse reaction
CC {ECO:0000269|PubMed:171261};
CC pH dependence:
CC Optimum pH is 7.5 for the forward reaction and 7.0-7.4 for the
CC reverse reaction. {ECO:0000269|PubMed:171261};
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_01977}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:171261}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01977}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'P' sub-subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01977}.
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DR EMBL; M67447; AAA25675.1; -; Genomic_DNA.
DR EMBL; AJ508922; CAD48602.1; -; Genomic_DNA.
DR EMBL; FN806773; CBL56726.1; -; Genomic_DNA.
DR PIR; A41169; A41169.
DR RefSeq; WP_013161100.1; NC_014215.1.
DR AlphaFoldDB; P29495; -.
DR SMR; P29495; -.
DR STRING; 754252.PFREUD_12040; -.
DR PRIDE; P29495; -.
DR EnsemblBacteria; CBL56726; CBL56726; PFREUD_12040.
DR KEGG; pfr:PFREUD_12040; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_643544_0_0_11; -.
DR OMA; WFAKQFA; -.
DR OrthoDB; 1421302at2; -.
DR BioCyc; PFRE754252:PFREUD_RS05840-MON; -.
DR SABIO-RK; P29495; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000000936; 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 HAMAP; MF_01977; Phosphofructokinase_II_P; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR011405; PPi-PFK_SMc01852.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF036484; PPi-PFK_SMc01852; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..404
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000112013"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 12
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 149..151
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 194..196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT BINDING 323..326
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
FT SITE 122
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_01977"
FT SITE 148
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01977"
SQ SEQUENCE 404 AA; 43246 MW; 2676CD4ADE0D8A55 CRC64;
MVKKVALLTA GGFAPCLSSA IAELIKRYTE VSPETTLIGY RYGYEGLLKG DSLEFSPAVR
AHYDRLFSFG GSPIGNSRVK LTNVKDLVAR GLVASGDDPL KVAADQLIAD GVDVLHTIGG
DDTNTTAADL AAYLAQHDYP LTVVGLPKTI DNDIVPIRQS LGAWTAADEG ARFAANVIAE
HNAAPRELII HEIMGRNCGY LAAETSRRYV AWLDAQQWLP EAGLDRRGWD IHALYVPEAT
IDLDAEAERL RTVMDEVGSV NIFISEGAGV PDIVAQMQAT GQEVPTDAFG HVQLDKINPG
AWFAKQFAER IGAGKTMVQK SGYFSRSAKS NAQDLELIAA TATMAVDAAL AGTPGVVGQD
EEAGDKLSVI DFKRIAGHKP FDITLDWYTQ LLARIGQPAP IAAA
