ID A0A0W8I0Z1_9MICO Unreviewed; 339 AA. AC A0A0W8I0Z1; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 14-DEC-2022, entry version 30. 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=AVL62_12570 {ECO:0000313|EMBL:KUG51080.1}; OS Serinicoccus chungangensis. OC Bacteria; Actinobacteria; Micrococcales; Ornithinimicrobiaceae; OC Serinicoccus. OX NCBI_TaxID=767452 {ECO:0000313|EMBL:KUG51080.1, ECO:0000313|Proteomes:UP000054837}; RN [1] {ECO:0000313|EMBL:KUG51080.1, ECO:0000313|Proteomes:UP000054837} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CD08_5 {ECO:0000313|EMBL:KUG51080.1, RC ECO:0000313|Proteomes:UP000054837}; RA Chander A.M., Kaur G., Nair G.R., Dhawan D.K., Kochhar R.K., Mayilraj S., RA Bhadada S.K.; RT "Serinicoccus chungangenesis strain CD08_5 genome sequencing and RT assembly."; RL Submitted (DEC-2015) 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|ARBA:ARBA00004496, CC 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KUG51080.1}. 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; LQBL01000033; KUG51080.1; -; Genomic_DNA. DR RefSeq; WP_058892625.1; NZ_LQBL01000033.1. DR AlphaFoldDB; A0A0W8I0Z1; -. DR STRING; 767452.AVL62_12570; -. DR EnsemblBacteria; KUG51080; KUG51080; AVL62_12570. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000054837; Unassembled WGS sequence. 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:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro. 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_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 Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000532; ATP_PFK_prok; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; Phosphofructokinase; 1. DR TIGRFAMs; TIGR02483; PFK_mixed; 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:UP000054837}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01976}. FT DOMAIN 2..293 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT ACT_SITE 126 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 10 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 72..73 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 101..104 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 102 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 124..126 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 161 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 168..170 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 220 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 263 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 269..272 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 103 FT /note="Important for substrate specificity; cannot use PPi FT as phosphoryl donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" SQ SEQUENCE 339 AA; 36186 MW; 7CA5BB9EB35269A9 CRC64; MKIGLLTSGG DCPGLNAVIR GVVLKGDRIY EHEFVGIKDG FRGLVEDDIV PLPRKRVRGL SKVGGTILGT SRISPIRTGG IDRVKEVMDK HEIDALVAIG GEGTLTVARM FHDEGINVVG VPKTIDNDLS ATDRTFGFDT AVSIATESID RLRTTGEAHS RCMVVEVMGR HVGWIALHAG IASGAHAILI PEVPVSSDQL CQWVQNAMDR GRAPTIVVAE GFTFAGAEQV ASDRVDGFGR PLLGGIGEAV TRAIEEHTGI ETRNTTLGHL QRGGVPSSYD RVLATRFGTA AIDSVSAKKW GTMVALSGMD IVNVNLRDAT SELKLVPRDQ WDEAAIMFG //