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Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent) (PPi-dependent phosphofructokinase) (PPi-PFK) (Pyrophosphate-dependent 6-phosphofructose-1-kinase)

 PFP_PROFC               Reviewed;         404 AA.
P29495; D7GDW5; Q08I84;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 98.
RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01977};
EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01977};
AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01977};
AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01977};
Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01977};
AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01977};
Name=pfp {ECO:0000255|HAMAP-Rule:MF_01977}; Synonyms=pfk;
OrderedLocusNames=PFREUD_12040;
Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 /
DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1).
Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
Propionibacterium.
NCBI_TaxID=754252;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=1653240;
Ladror U.S., Gollapudi L., Tripathi R.L., Latshaw S.P., Kemp R.G.;
"Cloning, sequencing, and expression of pyrophosphate-dependent
phosphofructokinase from Propionibacterium freudenreichii.";
J. Biol. Chem. 266:16550-16555(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1;
PubMed=15507000;
Meurice G., Deborde C., Jacob D., Falentin H., Boyaval P., Dimova D.;
"In silico exploration of the fructose-6-phosphate phosphorylation
step in glycolysis: genomic evidence of the coexistence of an atypical
ATP-dependent along with a PPi-dependent phosphofructokinase in
Propionibacterium freudenreichii subsp. shermanii.";
In Silico Biol. 4:517-528(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1;
PubMed=20668525; DOI=10.1371/journal.pone.0011748;
Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S.,
Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P.,
Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F.,
Gaillardin C., Lortal S.;
"The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a
hardy actinobacterium with food and probiotic applications.";
PLoS ONE 5:E11748-E11748(2010).
[4]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
AND ENZYME REGULATION.
PubMed=171261;
O'Brien W.E., Bowien S., Wood H.G.;
"Isolation and characterization of a pyrophosphate-dependent
phosphofructokinase from Propionibacterium shermanii.";
J. Biol. Chem. 250:8690-8695(1975).
[5]
IDENTIFICATION OF CRITICAL LYSYL RESIDUES.
PubMed=1317210; DOI=10.1021/bi00135a011;
Green P.C., Latshaw S.P., Ladror U.S., Kemp R.G.;
"Identification of critical lysyl residues in the pyrophosphate-
dependent phosphofructo-1-kinase of Propionibacterium
freudenreichii.";
Biochemistry 31:4815-4821(1992).
-!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate,
the first committing step of glycolysis. Uses inorganic phosphate
(PPi) as phosphoryl donor instead of ATP like common ATP-dependent
phosphofructokinases (ATP-PFKs), which renders the reaction
reversible, and can thus function both in glycolysis and
gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of
both the forward (ATP-PFK) and reverse (fructose-bisphosphatase
(FBPase)) reactions. {ECO:0000255|HAMAP-Rule:MF_01977,
ECO:0000269|PubMed:171261}.
-!- CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate =
phosphate + D-fructose 1,6-bisphosphate. {ECO:0000255|HAMAP-
Rule:MF_01977, ECO:0000269|PubMed:171261}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_01977};
-!- ENZYME REGULATION: Non-allosteric. {ECO:0000255|HAMAP-
Rule:MF_01977, ECO:0000269|PubMed:171261}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.6 mM for phosphate {ECO:0000269|PubMed:171261};
KM=0.069 mM for diphosphate {ECO:0000269|PubMed:171261};
KM=0.1 mM for fructose 6-phosphate {ECO:0000269|PubMed:171261};
KM=0.051 mM for fructose 1,6-bisphosphate
{ECO:0000269|PubMed:171261};
Vmax=258 umol/min/mg enzyme for the forward reaction
{ECO:0000269|PubMed:171261};
Vmax=232 umol/min/mg enzyme for the reverse reaction
{ECO:0000269|PubMed:171261};
pH dependence:
Optimum pH is 7.5 for the forward reaction and 7.0-7.4 for the
reverse reaction. {ECO:0000269|PubMed:171261};
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 3/4.
{ECO:0000255|HAMAP-Rule:MF_01977}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:171261}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01977}.
-!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
family. PPi-dependent PFK group II subfamily. Clade "P" sub-
subfamily. {ECO:0000255|HAMAP-Rule:MF_01977}.
-----------------------------------------------------------------------
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EMBL; M67447; AAA25675.1; -; Genomic_DNA.
EMBL; AJ508922; CAD48602.1; -; Genomic_DNA.
EMBL; FN806773; CBL56726.1; -; Genomic_DNA.
PIR; A41169; A41169.
RefSeq; WP_013161100.1; NC_014215.1.
ProteinModelPortal; P29495; -.
STRING; 754252.PFREUD_12040; -.
EnsemblBacteria; CBL56726; CBL56726; PFREUD_12040.
GeneID; 29492846; -.
KEGG; pfr:PFREUD_12040; -.
eggNOG; ENOG4107RJF; Bacteria.
eggNOG; COG0205; LUCA.
HOGENOM; HOG000223933; -.
KO; K00895; -.
OMA; GFAPCLS; -.
OrthoDB; POG091H01AC; -.
SABIO-RK; P29495; -.
UniPathway; UPA00109; UER00182.
Proteomes; UP000000936; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003872; F:6-phosphofructokinase activity; IEA:InterPro.
GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
HAMAP; MF_01977; Phosphofructokinase_II_P; 1.
InterPro; IPR022953; ATP_PFK.
InterPro; IPR000023; Phosphofructokinase_dom.
InterPro; IPR035966; PKF_sf.
InterPro; IPR011405; PPi-PFK_SMc01852.
Pfam; PF00365; PFK; 1.
PIRSF; PIRSF036484; PPi-PFK_SMc01852; 1.
PRINTS; PR00476; PHFRCTKINASE.
SUPFAM; SSF53784; SSF53784; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis;
Kinase; Magnesium; Metal-binding; Reference proteome; Transferase.
INIT_MET 1 1 Removed.
CHAIN 2 404 Pyrophosphate--fructose 6-phosphate 1-
phosphotransferase.
/FTId=PRO_0000112013.
REGION 149 151 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01977}.
REGION 194 196 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01977}.
REGION 323 326 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01977}.
ACT_SITE 151 151 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_01977}.
METAL 121 121 Magnesium; catalytic. {ECO:0000255|HAMAP-
Rule:MF_01977}.
BINDING 12 12 Diphosphate; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01977}.
BINDING 266 266 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01977}.
SITE 122 122 Important for catalytic activity and
substrate specificity; stabilizes the
transition state when the phosphoryl
donor is PPi; prevents ATP from binding
by mimicking the alpha-phosphate group of
ATP. {ECO:0000255|HAMAP-Rule:MF_01977}.
SITE 148 148 Important for catalytic activity;
stabilizes the transition state when the
phosphoryl donor is PPi.
{ECO:0000255|HAMAP-Rule:MF_01977}.
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


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