ID A0A431MRQ0_9SPHI Unreviewed; 330 AA. AC A0A431MRQ0; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 03-AUG-2022, entry version 10. 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:RTL59307.1}; GN ORFNames=EKK37_13500 {ECO:0000313|EMBL:RTL59307.1}; OS Sphingobacteriales bacterium. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales. OX NCBI_TaxID=2044944 {ECO:0000313|EMBL:RTL59307.1, ECO:0000313|Proteomes:UP000268352}; RN [1] {ECO:0000313|EMBL:RTL59307.1, ECO:0000313|Proteomes:UP000268352} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AWTP1-9 {ECO:0000313|EMBL:RTL59307.1}; RA Kantor R.S., Miller S.E., Nelson K.L.; RT "The water microbiome through an advanced treatment facility for direct RT potable reuse."; 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|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 -!- 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:RTL59307.1}. 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; RXJG01000004; RTL59307.1; -; Genomic_DNA. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000268352; 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: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 7..283 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT REGION 25..29 FT /note="ADP binding; allosteric activator; shared with FT dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 130..132 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 174..176 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 190..192 FT /note="ADP binding; allosteric activator" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 218..220 FT /note="ADP binding; allosteric activator" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 257..260 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT ACT_SITE 132 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 76..77 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 106..109 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 107 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 159 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 167 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 216 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 227 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 251 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" SQ SEQUENCE 330 AA; 35934 MW; 67C5CCFADD287CC2 CRC64; MTKKVSNIGV LTSGGDSPGM NACIRAVVRT GLYHGLEMFG IMRGYQGMID DDIVPMHSRS VANIIQRGGT ILKTARCKEF FELSGRKKAY ENLKKHGIDG LVIIGGDGSF RGAQKFSHEF DIPCIGLPGT IDKDIAGTDF TIGFDTAVNT AVECIDKIRD TADAHDRLFI IEVMGRDAGY IALHSGIATG AEHILIPERK TDIEAVISSL EEKEKRKKLV NMIVVAEGDD FGGADEVAKV VKERLPMADV RVCILGHIQR GGAPSCIDRL IASRMGYAAV EALLDPTGTH HNHMIGILNN RIHFTPLDKA IKAKQKISDE WMKIVKILAS //