ID D6YWC7_WADCW Unreviewed; 548 AA. AC D6YWC7; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 13-SEP-2023, entry version 71. 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=pfkA {ECO:0000313|EMBL:ADI38438.1}; GN Synonyms=pfp {ECO:0000256|HAMAP-Rule:MF_01980}; GN OrderedLocusNames=wcw_1081 {ECO:0000313|EMBL:ADI38438.1}; OS Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044). OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Waddliaceae; Waddlia. OX NCBI_TaxID=716544 {ECO:0000313|EMBL:ADI38438.1, ECO:0000313|Proteomes:UP000001505}; RN [1] {ECO:0000313|EMBL:ADI38438.1, ECO:0000313|Proteomes:UP000001505} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1470 / WSU 86-1044 {ECO:0000313|Proteomes:UP000001505}; RX PubMed=20531937; DOI=10.1371/journal.pone.0010890; RA Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A., RA Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.; RT "The Waddlia genome: a window into chlamydial biology."; RL PLoS ONE 5:E10890-E10890(2010). 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 --------------------------------------------------------------------------- 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; CP001928; ADI38438.1; -; Genomic_DNA. DR RefSeq; WP_013182152.1; NZ_LVEB01000048.1. DR AlphaFoldDB; D6YWC7; -. DR STRING; 716544.wcw_1081; -. DR EnsemblBacteria; ADI38438; ADI38438; wcw_1081. DR KEGG; wch:wcw_1081; -. DR eggNOG; COG0205; Bacteria. DR HOGENOM; CLU_022288_2_0_0; -. DR OMA; SAKKYWH; -. DR OrthoDB; 9802503at2; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000001505; Chromosome. 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; 3.40.50.450; -; 1. DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 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 NCBIfam; TIGR02477; PFKA_PPi; 1. DR PANTHER; PTHR43650; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE; 1. DR PANTHER; PTHR43650:SF1; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE SUBUNIT BETA 2; 1. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF005677; PPi_PFK_PfpB; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; Phosphofructokinase; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001505}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01980}. FT DOMAIN 70..340 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT ACT_SITE 202 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980" FT BINDING 78 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980" FT BINDING 172 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980" FT BINDING 200..202 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 239..240 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01980" FT BINDING 247..249 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 308 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 416..419 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 173 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 199 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 548 AA; 61315 MW; 51FE067DF90C6058 CRC64; MKEHTALEEK RLEYIPKLPA ILHDLRKLKT VNLKNSPGKA SEISDFFPLT IGQTALTFTI DQDHEKTPLK VGVVLSGGQA AGGHNVITGL FDALKELHSK SQLFGFLNGP SGIVNNQTIE LTEEILHSYR NQGGFDLIGA GRTKIETNEQ FQGTLHTVKA LDLDGIVIIG GDDSNTNAAL LAEFFMKEGV RTRVIGVPKT IDGDLKNAYI DLSFGFDTAV KTYSGIIGNI ARDSLSAKKY YFFIKLMGRS ASHIALECAL QTHANYTLIG EEINEEKATF QQITNRLSDV ICRRAELSKH YGVILIPEGL IEFIPEFRTL IAELNEIKID SELSKDERIQ LAMRSISSES LECYKSLPRL IQEQLMLDRD PHGNVQVSKI ETERLFIEAV KQELKRRKEK GEYTGSFNAQ PHFCGYEGRS CLPSNFDSQY CYALGHVAAL LIDANATGYM SCVKNLSRPI EEWQICGIPL TSMIHKEMRK GKLKPVIAKA LVDLQGAPFQ YFKEKRLQWE DEDDYRYPGP VQFFGPSEIT DAVTLTLELS QNTEAILN //