ID D6YWC7_WADCW Unreviewed; 548 AA. AC D6YWC7; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 28-FEB-2018, entry version 52. 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; Chlamydiae; 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, 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_01980}. CC -!- CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate = CC phosphate + D-fructose 1,6-bisphosphate. {ECO:0000256|HAMAP- CC Rule:MF_01980}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01980}; CC -!- ENZYME REGULATION: Non-allosteric. {ECO:0000256|HAMAP- CC 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|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) CC family. PPi-dependent PFK group II subfamily. Clade "Long" sub- CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01980}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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 STRING; 716544.wcw_1081; -. DR EnsemblBacteria; ADI38438; ADI38438; wcw_1081. DR KEGG; wch:wcw_1081; -. DR eggNOG; ENOG4107RJF; Bacteria. DR eggNOG; COG0205; LUCA. DR HOGENOM; HOG000017164; -. DR KO; K00895; -. DR OMA; GGFDMIG; -. DR OrthoDB; POG091H01AC; -. DR BioCyc; WCHO716544:G1GLF-1055-MONOMER; -. 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 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; SSF53784; 1. DR TIGRFAMs; TIGR02477; PFKA_PPi; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001505}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01980}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01980}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01980, ECO:0000313|EMBL:ADI38438.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01980}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01980}; KW Reference proteome {ECO:0000313|Proteomes:UP000001505}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01980, KW ECO:0000313|EMBL:ADI38438.1}. FT DOMAIN 70 312 PFK. {ECO:0000259|Pfam:PF00365}. FT REGION 200 202 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01980}. FT REGION 239 240 Substrate binding; shared with dimeric FT partner. {ECO:0000256|HAMAP-Rule: FT MF_01980}. FT REGION 247 249 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01980}. FT REGION 416 419 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01980}. FT ACT_SITE 202 202 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01980}. FT METAL 172 172 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_01980}. FT BINDING 78 78 Diphosphate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01980}. FT BINDING 308 308 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01980}. FT SITE 173 173 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_01980}. FT SITE 199 199 Important for catalytic activity; FT stabilizes the transition state when the FT phosphoryl donor is PPi. FT {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 //