ID PFKA_MYCCT Reviewed; 326 AA. AC Q2SSQ6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 106. DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339}; DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_00339}; DE Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339}; DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_00339}; DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_00339}; GN Name=pfkA {ECO:0000255|HAMAP-Rule:MF_00339}; GN OrderedLocusNames=MCAP_0220; OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 OS / NCTC 10154). OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=340047; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=California kid / ATCC 27343 / NCTC 10154; RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O., RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to CC fructose 1,6-bisphosphate by ATP, the first committing step of CC glycolysis. {ECO:0000255|HAMAP-Rule:MF_00339}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6- CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, CC ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00339}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00339}; CC -!- ACTIVITY REGULATION: Allosterically activated by ADP and other CC diphosphonucleosides, and allosterically inhibited by CC phosphoenolpyruvate. {ECO:0000255|HAMAP-Rule:MF_00339}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000255|HAMAP-Rule:MF_00339}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00339}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub- CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00339}. 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; CP000123; ABC01496.1; -; Genomic_DNA. DR RefSeq; WP_011387108.1; NC_007633.1. DR AlphaFoldDB; Q2SSQ6; -. DR SMR; Q2SSQ6; -. DR GeneID; 23778827; -. DR KEGG; mcp:MCAP_0220; -. DR HOGENOM; CLU_020655_0_1_14; -. DR PhylomeDB; Q2SSQ6; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000001928; 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:UniProtKB-KW. 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_00339; Phosphofructokinase_I_B1; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR012003; ATP_PFK_prok-type. DR InterPro; IPR012828; PFKA_ATP_prok. DR InterPro; IPR015912; Phosphofructokinase_CS. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR035966; PKF_sf. DR NCBIfam; TIGR02482; PFKA_ATP; 1. DR PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1. DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000532; ATP_PFK_prok; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; Phosphofructokinase; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 3: Inferred from homology; KW Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Transferase. FT CHAIN 1..326 FT /note="ATP-dependent 6-phosphofructokinase" FT /id="PRO_1000059778" FT ACT_SITE 128 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339" FT BINDING 12 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339" FT BINDING 73..74 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339" FT BINDING 103..106 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339" FT BINDING 104 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339" FT BINDING 126..128 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339" FT BINDING 155 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339" FT BINDING 163 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339" FT BINDING 170..172 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339" FT BINDING 186..188 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339" FT BINDING 214..216 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339" FT BINDING 223 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339" FT BINDING 246 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339" FT BINDING 252..255 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339" SQ SEQUENCE 326 AA; 35179 MW; 558F7448CBFCC949 CRC64; MIKKIGILTS GGDAPGMNNA IAGVVKTASS KGIEVYGIND GYKGLVNGWF EKLNVEKTLD ILSRGGTYLG SARLPEFKEL EVRQKAVANL KKAGIEALVV IGGDGSYMGA QRLTEMGINC IGLPGTIDND IASTDYTIGF HTALNTIVEA VDRIRDTMQS HNRADVVEIM GNGCGDLVTY TAVATGAEIF SPAEDLLTIE QMGQKAKQFR LLGKKSLIIL VSEKLYGISA EEIAEKIQKI SGYETKATVL GHIQRGGRPT AMDRYIAFTA GMFAVEKLAE GKGGLFIGLE NNKLVARDID STLNMKKEDK KPFIKNLREI NGHFSK //