ID A0L8Y2_MAGMM Unreviewed; 405 AA. AC A0L8Y2; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 96. DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01978}; DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01978}; DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01978}; DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01978}; DE Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01978}; DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01978}; GN Name=pfp {ECO:0000256|HAMAP-Rule:MF_01978}; GN OrderedLocusNames=Mmc1_1917 {ECO:0000313|EMBL:ABK44425.1}; OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales; OC Magnetococcaceae; Magnetococcus. OX NCBI_TaxID=156889 {ECO:0000313|EMBL:ABK44425.1, ECO:0000313|Proteomes:UP000002586}; RN [1] {ECO:0000313|Proteomes:UP000002586} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1 RC {ECO:0000313|Proteomes:UP000002586}; RX PubMed=19465526; DOI=10.1128/AEM.02874-08; RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D., RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.; RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic RT coccus strain MC-1."; RL Appl. Environ. Microbiol. 75:4835-4852(2009). RN [2] {ECO:0000313|EMBL:ABK44425.1, ECO:0000313|Proteomes:UP000002586} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1 RC {ECO:0000313|Proteomes:UP000002586}; RX PubMed=22581902; RA Bazylinski D.A., Williams T.J., Lefevre C.T., Berg R.J., Zhang C.L., RA Bowser S.S., Dean A.J., Beveridge T.J.; RT "Magnetococcus marinus gen. nov., sp. nov., a marine, magnetotactic RT bacterium that represents a novel lineage (Magnetococcaceae fam. nov.; RT Magnetococcales ord. nov.) at the base of the Alphaproteobacteria."; RL Int. J. Syst. Evol. Microbiol. 0:0-0(2012). 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:0000256|ARBA:ARBA00003138, ECO:0000256|HAMAP-Rule:MF_01978}. 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:0000256|ARBA:ARBA00000628, ECO:0000256|HAMAP- CC Rule:MF_01978}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP- CC Rule:MF_01978}; CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_01978}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000256|HAMAP-Rule:MF_01978}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01978}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01978}. 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; CP000471; ABK44425.1; -; Genomic_DNA. DR RefSeq; WP_011713569.1; NC_008576.1. DR AlphaFoldDB; A0L8Y2; -. DR STRING; 156889.Mmc1_1917; -. DR KEGG; mgm:Mmc1_1917; -. DR eggNOG; COG0205; Bacteria. DR HOGENOM; CLU_020655_1_1_5; -. DR OrthoDB; 9802503at2; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000002586; 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; 3.40.50.450; -; 1. DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 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. DR PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1. DR PANTHER; PTHR45770:SF11; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF036483; PFK_XF0274; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; Phosphofructokinase; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01978}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01978}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01978}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01978}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01978}; Reference proteome {ECO:0000313|Proteomes:UP000002586}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01978}. FT DOMAIN 5..321 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT ACT_SITE 138 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978" FT BINDING 13 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978" FT BINDING 108 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978" FT BINDING 136..138 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978" FT BINDING 180..182 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978" FT BINDING 237 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978" FT BINDING 295..298 FT /ligand="substrate" FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01978" SQ SEQUENCE 405 AA; 43825 MW; 72304F5D34BBD1D9 CRC64; MKSGKVLIAQ GGGPTAVINQ SLVGAVLEAQ RYAQVDRIYG AVHGVRGIVD ENFMDLSMET AGNLERVAAM PSSALGSTRD KPDRAYCAEM FKVLKAHDIR SFFYCGGNDS SDTVRIVKEF ADEANYEFTA MHIPKTIDND LMANDHTPGF PSAAKFVACA FAGVNMDNRA LPGVYVGVVM GRHAGFLTGA AAMARVFADD GPHLIYVPER TFDMNTFLAD VKSTYDKYGR CIVAVSEGVH DAEGTPIVTK LQENVERDAH GNVQLSGTGA LADLLCDEIK AKLGIKRVRG DTFGYLQRSF LGIVSEVDAR EAREVGQKAV QEALRHNASG TITIKRVGNY ASAYELANVK EVAALTKVMA DNFITTASND VTADFIHYLR PLLGSNPLEH AARLMAPMVE KILHK //