ID PFP_STRCO Reviewed; 342 AA. AC O08333; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 27-MAR-2024, entry version 148. DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01976}; DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01976}; DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01976}; DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01976}; DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01976}; DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01976}; GN Name=pfkA1 {ECO:0000255|HAMAP-Rule:MF_01976}; GN Synonyms=pfk1, pfkA, pfp; OrderedLocusNames=SCO2119; GN ORFNames=SC6E10.13c; OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group. OX NCBI_TaxID=100226; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A3(2) / 1109; RX PubMed=9055413; DOI=10.1128/aem.63.3.956-961.1997; RA Alves A.M.C.R., Euverink G.J.W., Bibb M.J., Dijkhuizen L.; RT "Identification of ATP-dependent phosphofructokinase as a regulatory step RT in the glycolytic pathway of the actinomycete Streptomyces coelicolor RT A3(2)."; RL Appl. Environ. Microbiol. 63:956-961(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145; RX PubMed=12000953; DOI=10.1038/417141a; RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H., RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor RT A3(2)."; RL Nature 417:141-147(2002). RN [3] RP DISRUPTION PHENOTYPE. RX PubMed=18606812; DOI=10.1074/jbc.m803105200; RA Borodina I., Siebring J., Zhang J., Smith C.P., van Keulen G., RA Dijkhuizen L., Nielsen J.; RT "Antibiotic overproduction in Streptomyces coelicolor A3(2) mediated by RT phosphofructokinase deletion."; RL J. Biol. Chem. 283:25186-25199(2008). 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_01976}. 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_01976}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01976}; CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|HAMAP-Rule:MF_01976}. 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_01976}. CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01976}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}. CC -!- DISRUPTION PHENOTYPE: No effect. {ECO:0000269|PubMed:18606812}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC Mixed-substrate PFK group III subfamily. {ECO:0000255|HAMAP- CC Rule:MF_01976}. CC -!- CAUTION: Was originally characterized as ATP-dependent CC phosphofructokinase (PubMed:9055413). However, inspection of the CC original N-terminal sequence showed that the characterized enzyme was CC not pfkA1 (SCO2119), but pfkA2 (SCO5426) instead, another isozyme in CC S.coelicolor (PubMed:18606812). {ECO:0000305|PubMed:18606812, CC ECO:0000305|PubMed:9055413}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U51728; AAC45135.1; -; Genomic_DNA. DR EMBL; AL939111; CAB51967.1; -; Genomic_DNA. DR PIR; T35500; T35500. DR RefSeq; NP_626376.1; NC_003888.3. DR RefSeq; WP_003976696.1; NZ_VNID01000001.1. DR AlphaFoldDB; O08333; -. DR SMR; O08333; -. DR STRING; 100226.gene:17759717; -. DR PaxDb; 100226-SCO2119; -. DR PATRIC; fig|100226.15.peg.2154; -. DR eggNOG; COG0205; Bacteria. DR HOGENOM; CLU_020655_0_0_11; -. DR InParanoid; O08333; -. DR OrthoDB; 9802503at2; -. DR PhylomeDB; O08333; -. DR BRENDA; 2.7.1.11; 5998. DR SABIO-RK; O08333; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000001973; Chromosome. DR GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central. DR GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central. DR GO; GO:0016208; F:AMP binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central. DR GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central. DR Gene3D; 3.40.50.450; -; 1. DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 1. DR HAMAP; MF_01976; Phosphofructokinase_III; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR012003; ATP_PFK_prok-type. DR InterPro; IPR015912; Phosphofructokinase_CS. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR012829; Phosphofructokinase_III. DR InterPro; IPR035966; PKF_sf. DR NCBIfam; TIGR02483; PFK_mixed; 1. DR PANTHER; PTHR13697:SF52; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 3; 1. DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000532; ATP_PFK_prok; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; Phosphofructokinase; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 3: Inferred from homology; KW Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding; KW Reference proteome; Transferase. FT CHAIN 1..342 FT /note="Pyrophosphate--fructose 6-phosphate 1- FT phosphotransferase" FT /id="PRO_0000111986" FT ACT_SITE 128 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976" FT BINDING 10 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976" FT BINDING 103 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976" FT BINDING 126..128 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976" FT BINDING 163 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976" FT BINDING 170..172 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976" FT BINDING 222 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976" FT BINDING 266 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976" FT BINDING 272..275 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976" FT SITE 104 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_01976" FT SITE 125 FT /note="Important for catalytic activity; stabilizes the FT transition state when the phosphoryl donor is PPi" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976" SQ SEQUENCE 342 AA; 36664 MW; CEEFC7B74092AB34 CRC64; MKVGVLTGGG DCPGLNAVIR AVVRKGVQEY GYDFTGFRDG WRGPLEGDTV PLDIPAVRGI LPRGGTVLGS SRTNPLKQRD GIRRIKDNLA ALGVEALITI GGEDTLGVAT RLADEYGVPC VGVPKTIDND LSATDYTFGF DTAVGIATEA IDRLHTTAES HMRVLVVEVM GRHAGWIALH SGLAGGANVI LIPEQRFDVE QVCSWVTSRF RASYAPIVVV AEGAMPRDGD MVLKDESLDS YGHVRLSGVG EWLAKQIEKR TGNEARTTVL GHVQRGGTPS AFDRWLATRF GLHAVDCVHD GDFGKMVALR GTDIVRVPIA EATARLKTVD PALYEEVGVF FG //