ID PFKA_MYCPN Reviewed; 328 AA. AC P75476; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 128. DE RecName: Full=Probable ATP-dependent 6-phosphofructokinase; DE Short=ATP-PFK; DE Short=Phosphofructokinase; DE EC=2.7.1.11; DE AltName: Full=Phosphohexokinase; GN Name=pfkA; Synonyms=pfk; OrderedLocusNames=MPN_302; ORFNames=MP534; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) OS (Mycoplasmoides pneumoniae). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129 / Subtype 1; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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:0000250|UniProtKB:P0A796}. 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; CC Evidence={ECO:0000250|UniProtKB:P0A796}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P0A796}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000250|UniProtKB:P0A796}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0A796}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A796}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC {ECO:0000305}. 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; U00089; AAB96182.1; -; Genomic_DNA. DR PIR; S73860; S73860. DR RefSeq; NP_109990.1; NC_000912.1. DR RefSeq; WP_010874659.1; NZ_OU342337.1. DR AlphaFoldDB; P75476; -. DR SMR; P75476; -. DR IntAct; P75476; 2. DR STRING; 272634.MPN_302; -. DR EnsemblBacteria; AAB96182; AAB96182; MPN_302. DR GeneID; 66609051; -. DR KEGG; mpn:MPN_302; -. DR PATRIC; fig|272634.6.peg.326; -. DR HOGENOM; CLU_020655_0_1_14; -. DR OrthoDB; 9802503at2; -. DR BioCyc; MetaCyc:MONOMER-545; -. DR BioCyc; MPNE272634:G1GJ3-472-MONOMER; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:AgBase. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC. 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 InterPro; IPR022953; ATP_PFK. DR InterPro; IPR012003; ATP_PFK_prok-type. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR035966; PKF_sf. 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. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..328 FT /note="Probable ATP-dependent 6-phosphofructokinase" FT /id="PRO_0000111965" FT ACT_SITE 132 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P0A796" FT BINDING 16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0A796" FT BINDING 77..78 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0A796" FT BINDING 107..110 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0A796" FT BINDING 108 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P0A796" FT BINDING 130..132 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P0A796" FT BINDING 167 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P0A796" FT BINDING 174..176 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P0A796" FT BINDING 226 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P0A796" FT BINDING 258..261 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P0A796" SQ SEQUENCE 328 AA; 35989 MW; E29C9F0536766321 CRC64; MSPKTTKKIA ILTSGGDAPG MNATLVYLTR YATSSEIEVF FVKNGYYGLY HDELVPAHQL DLSNSLFSAG TVIGSKRFVE FKELKVREQA AQNLKKRQID YLVVIGGDGS YMGAKLLSEL GVNCYCLPGT IDNDINSSEF TIGFLTALES IKVNVQAVYH TTKSHERVAI VEVMGRHCGD LAIFGALATN ADFVVTPSNK MDLKQLESAV KKILQHQNHC VVIVSENIYG FDGYPSLTAI KQHFDANNMK CNLVSLGHTQ RGFAPTSLEL VQISLMAQHT INLIGQNKVN QVIGNKANVP VNYDFDQAFN MPPVDRSALI AVINKNII //