PFP_RHORT
ID PFP_RHORT Reviewed; 404 AA.
AC Q2RNU4;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01978};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01978};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01978};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01978};
DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01978};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01978};
GN Name=pfp {ECO:0000255|HAMAP-Rule:MF_01978}; OrderedLocusNames=Rru_A3407;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBUNIT.
RX PubMed=6446207;
RA Pfleiderer C., Klemme J.H.;
RT "Pyrophosphate-dependent D-fructose-6-phosphate-phosphotransferase in
RT Rhodospirillaceae.";
RL Z. Naturforsch. C Biosci. 35:229-238(1980).
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_01978, ECO:0000269|PubMed:6446207}.
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_01978,
CC ECO:0000269|PubMed:6446207};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01978,
CC ECO:0000269|PubMed:6446207};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|HAMAP-Rule:MF_01978}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.82 mM for phosphate {ECO:0000269|PubMed:6446207};
CC KM=0.025 mM for diphosphate {ECO:0000269|PubMed:6446207};
CC KM=0.38 mM for fructose 6-phosphate {ECO:0000269|PubMed:6446207};
CC KM=0.02 mM for fructose 1,6-bisphosphate
CC {ECO:0000269|PubMed:6446207};
CC Vmax=20 umol/min/mg enzyme for the forward reaction
CC {ECO:0000269|PubMed:6446207};
CC Vmax=24.2 umol/min/mg enzyme for the reverse reaction
CC {ECO:0000269|PubMed:6446207};
CC pH dependence:
CC Optimum pH is 7.2 for the forward reaction and 8.6 for the revesre
CC reaction. {ECO:0000269|PubMed:6446207};
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_01978}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01978,
CC ECO:0000269|PubMed:6446207}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01978}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'B2' sub-subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01978}.
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DR EMBL; CP000230; ABC24201.1; -; Genomic_DNA.
DR RefSeq; WP_011391154.1; NC_007643.1.
DR RefSeq; YP_428488.1; NC_007643.1.
DR AlphaFoldDB; Q2RNU4; -.
DR SMR; Q2RNU4; -.
DR STRING; 269796.Rru_A3407; -.
DR PRIDE; Q2RNU4; -.
DR EnsemblBacteria; ABC24201; ABC24201; Rru_A3407.
DR KEGG; rru:Rru_A3407; -.
DR PATRIC; fig|269796.9.peg.3523; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_1_1_5; -.
DR OMA; AHDIGYF; -.
DR OrthoDB; 1421302at2; -.
DR PhylomeDB; Q2RNU4; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000001929; 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 Gene3D; 3.40.50.460; -; 1.
DR HAMAP; MF_01978; Phosphofructokinase_II_B2; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR011404; PPi-PFK_XF0274.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF036483; PFK_XF0274; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..404
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000429698"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 13
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 136..138
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 180..182
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 295..298
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT SITE 109
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_01978"
FT SITE 135
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
SQ SEQUENCE 404 AA; 44156 MW; F8415CB2671A1939 CRC64;
MFKGKVVVAQ GGGPTAVINQ SMVGAVLESR KFRNVELVYG AVHGVRGIVD EHFLDLTQET
THNLEMVAET PSSALGSTRE KPDLKYCQEI FKVLKAHEIG YFFYIGGNDS SDTVRIVSEE
AAKADYGLRC IHIPKTIDND LVVNDHTPGF PSAARFVAQA FSGVNLDNQA LPGVYIGVVM
GRHAGFLTAA SALGKKFQDD GPHLIYLPER TFDVDTFVSD VKEVYDRTGR CIVAVSEGIH
DASGEPIITK LAEEVERDAH GNVQLSGTGA LADLLVSVVK KKSGIKRVRG DTLGYLQRSF
VGCVSDVDQR EAREVGEKAV QYAMWGQTNG SVTIHRTGFY SVDYQLTPLL DVAGKTRTMP
DSFIAANGHD VTTDFLMYLR PLLGRGMPDA YRLRDNRVAK VLNR
