ID A0A4V0ZH02_9BACT Unreviewed; 367 AA. AC A0A4V0ZH02; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 29-MAY-2024, entry version 18. DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976}; DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_01976}; DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976}; DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_01976}; GN Name=pfkA {ECO:0000256|HAMAP-Rule:MF_01976}; GN ORFNames=EGM51_06525 {ECO:0000313|EMBL:QBG47064.1}; OS Verrucomicrobia bacterium S94. OC Bacteria; Verrucomicrobiota. OX NCBI_TaxID=2488809 {ECO:0000313|EMBL:QBG47064.1, ECO:0000313|Proteomes:UP000289135}; RN [1] {ECO:0000313|EMBL:QBG47064.1, ECO:0000313|Proteomes:UP000289135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S94 {ECO:0000313|EMBL:QBG47064.1, RC ECO:0000313|Proteomes:UP000289135}; RA Baek K.; RT "Verrucomicrobia bacterium S94."; RL Submitted (NOV-2018) 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:0000256|HAMAP-Rule:MF_01976}. 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:0000256|HAMAP- CC Rule:MF_01976}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_01976}; 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_01976}. CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC Mixed-substrate PFK group III subfamily. {ECO:0000256|HAMAP- CC Rule:MF_01976}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01976}. 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; CP036201; QBG47064.1; -; Genomic_DNA. DR AlphaFoldDB; A0A4V0ZH02; -. DR KEGG; vbs:EGM51_06525; -. DR OrthoDB; 9802503at2; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000289135; Chromosome. DR GO; GO:0005945; C:6-phosphofructokinase complex; IEA:TreeGrafter. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016208; F:AMP binding; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro. DR GO; GO:0070095; F:fructose-6-phosphate binding; IEA:TreeGrafter. DR GO; GO:0042802; F:identical protein binding; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0048029; F:monosaccharide binding; IEA:TreeGrafter. DR GO; GO:0061621; P:canonical glycolysis; IEA:TreeGrafter. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:TreeGrafter. 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_01976; Phosphofructokinase_III; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR012003; ATP_PFK_prok-type. DR InterPro; IPR015912; Phosphofructokinase_CS. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR012829; Phosphofructokinase_III. DR InterPro; IPR035966; PKF_sf. DR PANTHER; PTHR13697:SF52; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 3; 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 ATP-binding {ECO:0000256|HAMAP-Rule:MF_01976}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01976}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_01976}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01976}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01976}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01976}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01976}; KW Reference proteome {ECO:0000313|Proteomes:UP000289135}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01976}. FT DOMAIN 8..312 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT ACT_SITE 137 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 76..77 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 112..115 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 113 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 135..137 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 172 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 179..181 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 232 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 281 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 287..290 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT SITE 114 FT /note="Important for substrate specificity; cannot use PPi FT as phosphoryl donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" SQ SEQUENCE 367 AA; 39111 MW; 39922D1BF34170E2 CRC64; MATKTKTIGI LTSGGDCPGL NAAIRGVAKA ALAQGTKVIG ILDGFRGLVE NRTMTLEDKD VSGILTHGGT FLGSSRDKPH KMPMGEKVLD MTEVAVSNAR KNHIDCLVCL GGNGTQKNAM RLHEAGLDVL TLPKTIDNDV AGTDITFGFD SSMAIATEAI DRLHTTASSH HRAIVCEIMG HKAGWLALGA GIAGGADVIL LPEIPYDLDY IVEHLMARRH HSKRFSIIAI AEGAISKEEA AEGRKKKKPV RKKENGMMLI EEPVASRIAR QIQQAAGIEV RFTSLGHVQR GGSPTATDRL LSTRLGTKAG ELLHDGVYNV MVGLKGERCV AVPLEDVAGR TKVVPAGHPW LKTAVLVDTC LGDKLDF //