ID R0ABP2_9FIRM Unreviewed; 412 AA. AC R0ABP2; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 11-NOV-2015, entry version 15. 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 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 [Clostridium] bolteae 90B8. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=997897 {ECO:0000313|EMBL:ENZ33818.1}; RN [1] {ECO:0000313|EMBL:ENZ33818.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=90B8 {ECO:0000313|EMBL:ENZ33818.1}; 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., RA Wortman J., 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, CC the first committing step of glycolysis. Uses inorganic phosphate CC (PPi) as phosphoryl donor instead of ATP like common ATP-dependent CC phosphofructokinases (ATP-PFKs), which renders the reaction CC reversible, and can thus function both in glycolysis and CC gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of CC both the forward (ATP-PFK) and reverse (fructose-bisphosphatase CC (FBPase)) reactions. {ECO:0000256|HAMAP-Rule:MF_01978}. CC -!- CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate = CC phosphate + D-fructose 1,6-bisphosphate. {ECO:0000256|HAMAP- CC Rule:MF_01978}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01978}; CC -!- ENZYME REGULATION: Non-allosteric. {ECO:0000256|HAMAP- CC 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) CC family. PPi-dependent PFK group II subfamily. Clade "B2" sub- CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01978}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 ProteinModelPortal; R0ABP2; -. DR EnsemblBacteria; ENZ33818; ENZ33818; HMPREF1097_04386. DR UniPathway; UPA00109; UER00182. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-HAMAP. 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 HAMAP; MF_01978; Phosphofructokinase_II_B2; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR000023; Phosphofructokinase_dom. 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|HAMAP-Rule:MF_01978}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01978, ECO:0000313|EMBL:ENZ33818.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01978}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01978}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01978}. FT REGION 143 145 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01978}. FT REGION 191 193 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01978}. FT ACT_SITE 145 145 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01978}. FT METAL 115 115 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_01978}. FT BINDING 14 14 Diphosphate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01978}. FT BINDING 248 248 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01978}. FT SITE 116 116 Important for catalytic activity and FT substrate specificity; stabilizes the FT transition state when the phosphoryl FT donor is PPi; prevents ATP from binding FT by mimicking the alpha-phosphate group of FT ATP. {ECO:0000256|HAMAP-Rule:MF_01978}. FT SITE 142 142 Important for catalytic activity; FT stabilizes the transition state when the FT phosphoryl donor is PPi. FT {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 //