ID A0A7U7EYV4_STAAU Unreviewed; 322 AA. AC A0A7U7EYV4; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 19-JAN-2022, entry version 3. DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339}; DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_00339}; DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339}; DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_00339}; DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_00339}; GN Name=pfkA {ECO:0000256|HAMAP-Rule:MF_00339, GN ECO:0000313|EMBL:CCJ22986.1}; GN ORFNames=SAI7S6_1012400 {ECO:0000313|EMBL:CCJ22986.1}; OS Staphylococcus aureus subsp. aureus ST228. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=1074919 {ECO:0000313|EMBL:CCJ22986.1, ECO:0000313|Proteomes:UP000032744}; RN [1] {ECO:0000313|EMBL:CCJ22986.1, ECO:0000313|Proteomes:UP000032744} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST228/18412 {ECO:0000313|Proteomes:UP000032744}; RX PubMed=22720005; DOI=10.1371/journal.pone.0038969; RA Vogel V., Falquet L., Calderon-Copete S.P., Basset P., Blanc D.S.; RT "Short term evolution of a highly transmissible methicillin-resistant RT Staphylococcus aureus clone (ST228) in a tertiary care hospital."; RL PLoS ONE 7:e38969-e38969(2012). 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:0000256|ARBA:ARBA00002659, ECO:0000256|HAMAP- CC 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; CC Evidence={ECO:0000256|ARBA:ARBA00000432, ECO:0000256|HAMAP- CC Rule:MF_00339}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_00339}; CC -!- ACTIVITY REGULATION: Allosterically activated by ADP and other CC diphosphonucleosides, and allosterically inhibited by CC phosphoenolpyruvate. {ECO:0000256|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:0000256|ARBA:ARBA00004679, ECO:0000256|HAMAP-Rule:MF_00339}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00339}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|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:0000256|HAMAP-Rule:MF_00339}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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; HE579071; CCJ22986.1; -; Genomic_DNA. DR RefSeq; WP_000717561.1; NC_020568.1. DR SMR; A0A7U7EYV4; -. DR KEGG; sauj:SAI2T2_1012400; -. DR KEGG; sauk:SAI3T3_1012380; -. DR KEGG; sauq:SAI4T8_1012390; -. DR KEGG; saut:SAI1T1_2012380; -. DR KEGG; sauv:SAI7S6_1012400; -. DR KEGG; sauw:SAI5S5_1012350; -. DR KEGG; saux:SAI6T6_1012360; -. DR KEGG; sauy:SAI8T7_1012390; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000032744; 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; 3.40.50.460; -; 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 Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000532; ATP_PFK_prok; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; SSF53784; 1. DR TIGRFAMs; TIGR02482; PFKA_ATP; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 3: Inferred from homology; KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533, ECO:0000256|HAMAP- KW Rule:MF_00339}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00339}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00339}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_00339}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00339}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00339}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00339}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00339}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00339}. FT DOMAIN 3..277 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT NP_BIND 72..73 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT NP_BIND 102..105 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 21..25 FT /note="ADP binding; allosteric activator; shared with FT dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 127..129 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 171..173 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 187..189 FT /note="ADP binding; allosteric activator" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 215..217 FT /note="ADP binding; allosteric activator" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 251..254 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT ACT_SITE 129 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT METAL 103 FT /note="Magnesium; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 11 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 156 FT /note="ADP; allosteric activator" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 164 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 213 FT /note="ADP; allosteric activator" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 224 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 245 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" SQ SEQUENCE 322 AA; 34840 MW; 1FAE41C0BA7CA7F1 CRC64; MKKIAVLTSG GDSPGMNAAV RAVVRTAIYN EIEVYGVYHG YQGLLNDDIH KLELGSVGDT IQRGGTFLYS ARCPEFKEQE VRKVAIENLR KRGIEGLVVI GGDGSYRGAQ RISEECKEIQ TIGIPGTIDN DINGTDFTIG FDTALNTIIG LVDKIRDTAS SHARTFIIEA MGRDCGDLAL WAGLSVGAET IVVPEVKTDI KEIADKIEQG IKRGKKHSIV LVAEGCMTAQ DCQKELSQYI NVDNRVSVLG HVQRGGSPTG ADRVLASRLG GYAVDLLMQG ETAKGVGIKN NKIVATSFDE IFDGKDHKFD YSLYELANKL SI //