ID R0ABP2_9FIRM Unreviewed; 412 AA. AC R0ABP2; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 03-AUG-2022, entry version 41. 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 ORFNames=HMPREF1097_04386 {ECO:0000313|EMBL:ENZ33818.1}; OS Enterocloster bolteae 90B8. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae; OC Enterocloster. OX NCBI_TaxID=997897 {ECO:0000313|EMBL:ENZ33818.1, ECO:0000313|Proteomes:UP000013041}; RN [1] {ECO:0000313|EMBL:ENZ33818.1, ECO:0000313|Proteomes:UP000013041} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=90B8 {ECO:0000313|EMBL:ENZ33818.1, RC ECO:0000313|Proteomes:UP000013041}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Courvalin P., Lambert T., RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Clostridium bolteae 90B8."; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. 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|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|HAMAP-Rule:MF_01978}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-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|ARBA:ARBA00004679, 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01978}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:ENZ33818.1}. 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; AGYG01000029; ENZ33818.1; -; Genomic_DNA. DR RefSeq; WP_002567258.1; NZ_KB851157.1. DR EnsemblBacteria; ENZ33818; ENZ33818; HMPREF1097_04386. DR GeneID; 61859164; -. DR PATRIC; fig|997897.5.peg.4609; -. DR HOGENOM; CLU_020655_1_1_9; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000013041; Unassembled WGS sequence. 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 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01978}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW 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}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01978}. FT DOMAIN 7..328 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT REGION 143..145 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978" FT REGION 191..193 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978" FT ACT_SITE 145 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978" FT BINDING 14 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978" FT BINDING 115 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978" FT BINDING 248 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01978" FT SITE 116 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 142 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 412 AA; 45173 MW; 79A093163F54FB4C CRC64; MGKKRNIIVG QSGGPTSVIN SSLAGVYKTA KERGFHKVYG MLHGIEGLLD EMYVDLSTQI HSDMDIELLK RTPSAFLGSC RYKLPDIHEN PAFYEKIFAI LDKLDIEVFI YIGGNDSMDT IKKLSDYAIV KGHGQKFLGV PKTIDNDLAL TDHTPGFGSA AKYIATSTKE VIRDAMGLSY RRKTITIMEC MGRNAGWLTG STALARTEDC CGPDLIYLPE IPFDIDKFLK KCKDLIQKKP SIVIAVSEGI KVPDGRYVCQ LSGGSDYVDA FGHKQLAGTA DYLAGFLAGE LGCKTRSVEL STLQRSASHV ASRVDINEAF MVGGAAVKAA DEGDTGKMVV IDRVSDDPYM SAAGIYDVHK IANNEKTVPR SWVNKDGSYV TQEFVNYVEP LIQGDYQPFM VNGLPQHLVL KR //