ID A0A7W8BWU3_BORAF Unreviewed; 555 AA. AC A0A7W8BWU3; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 14-DEC-2022, entry version 7. DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01980}; DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01980}; DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01980}; DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01980}; DE Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01980}; DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01980}; GN Name=pfp {ECO:0000256|HAMAP-Rule:MF_01980}; GN ORFNames=HNP63_000824 {ECO:0000313|EMBL:MBB5141413.1}; OS Borreliella afzelii (Borrelia afzelii). OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella. OX NCBI_TaxID=29518 {ECO:0000313|EMBL:MBB5141413.1, ECO:0000313|Proteomes:UP000529652}; RN [1] {ECO:0000313|EMBL:MBB5141413.1, ECO:0000313|Proteomes:UP000529652} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10508 {ECO:0000313|EMBL:MBB5141413.1, RC ECO:0000313|Proteomes:UP000529652}; RA Goeker M.; RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the RT most valuable type-strain genomes for metagenomic binning, comparative RT biology and taxonomic classification."; RL Submitted (AUG-2020) 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_01980}. 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_01980}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_01980}; CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_01980}. 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_01980}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01980}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01980}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01980}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01980}. 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:MBB5141413.1}. 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; JACHGM010000002; MBB5141413.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7W8BWU3; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000529652; 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:0005524; F:ATP binding; IEA:InterPro. 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_01980; Phosphofructokinase_II_Long; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR011183; PfpB_PPi_PFK. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR035966; PKF_sf. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF005677; PPi_PFK_PfpB; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; Phosphofructokinase; 1. DR TIGRFAMs; TIGR02477; PFKA_PPi; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01980}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_01980}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01980}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01980}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01980}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01980}. FT DOMAIN 74..333 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT ACT_SITE 206 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980" FT BINDING 82 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980" FT BINDING 176 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980" FT BINDING 204..206 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980" FT BINDING 243..244 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980" FT BINDING 251..253 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980" FT BINDING 312 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980" FT BINDING 428..431 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980" FT SITE 177 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_01980" FT SITE 203 FT /note="Important for catalytic activity; stabilizes the FT transition state when the phosphoryl donor is PPi" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980" SQ SEQUENCE 555 AA; 62413 MW; C2587592F5557342 CRC64; MNTSLFQQER QKYIPKLPNI LKKDFKNISL VYGEKTEAIQ DRQALKEFFK NTYGLPVVSF AEGESNLSFS KALNIGIILS GGPAPGGHNV ISGVFDAVKK FNANSKLFGF KGGPLGLLEN DKIELTESLV NSYRNTGGFD IVSSGRTKIE TEEHYNKALL VAKENNLNAI IIIGGDDSNT NAAILAEYFK KKGENIQVIG VPKTIDADLK NDHIEISFGF DSATKIYSEM IGNLCRDAMS TKKYWHFVKL MGRSASHVAL ECALKTHPNI CIVSEEVLAK KKTLSEIVDE IVFVILKRSL NGDNFGIVIV PEGVIEFIPE VKSLMLELCN IFDKNESEFK GLNVEKMKEV FVAKLSDYMK EVYLSLPLFI QFELVKSILE RDPHGNFNVS RVPTEKLLIE MVQSRLSDMK KRGEYKGSFI PVDHFFGYEG RSAFPSNFDS DYCYSLGYNA VVLILNGFTG YMSCIRNLNL KPTDWIAGGV PLTMLMNMEE RYGVQKPVIK KALVDLEGRP FKEFVENRDK WALNNLYLYP GPVQYFGSSE IVDEITETLK LELLK //