ID A0A3N2DLH2_9ENTR Unreviewed; 320 AA. AC A0A3N2DLH2; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 07-OCT-2020, entry version 8. 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 ORFNames=EC848_4567 {ECO:0000313|EMBL:ROS00631.1}; OS Enterobacter sp. BIGb0359. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=2485133 {ECO:0000313|EMBL:ROS00631.1, ECO:0000313|Proteomes:UP000281546}; RN [1] {ECO:0000313|EMBL:ROS00631.1, ECO:0000313|Proteomes:UP000281546} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BIGb0359 {ECO:0000313|EMBL:ROS00631.1, RC ECO:0000313|Proteomes:UP000281546}; RA Samuel B.; RT "Genomic analyses of the natural microbiome of Caenorhabditis elegans."; 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 -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the CC first committing step of glycolysis. Uses inorganic phosphate (PPi) as CC phosphoryl donor instead of ATP like common ATP-dependent CC phosphofructokinases (ATP-PFKs), which renders the reaction reversible, CC and can thus function both in glycolysis and gluconeogenesis. CC Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- CC PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. CC {ECO:0000256|ARBA:ARBA00003138}. 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 -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose CC 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; CC Evidence={ECO:0000256|ARBA:ARBA00000628}; 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: 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:ROS00631.1}. 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; RKHS01000009; ROS00631.1; -; Genomic_DNA. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000281546; 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:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR CDD; cd00763; Bacterial_PFK; 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 ECO:0000313|EMBL:ROS00631.1}; 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 4..276 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT NP_BIND 73..74 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT NP_BIND 103..106 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 22..26 FT /note="Allosteric activator ADP binding; shared with FT dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 55..60 FT /note="Allosteric activator ADP binding; shared with FT dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 126..128 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 170..172 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 186..188 FT /note="Allosteric activator ADP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 214..216 FT /note="Allosteric activator ADP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 250..253 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT ACT_SITE 128 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT METAL 104 FT /note="Magnesium; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 12 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 155 FT /note="Allosteric activator ADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 163 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 212 FT /note="Allosteric activator ADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 223 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 244 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" SQ SEQUENCE 320 AA; 35005 MW; D15012D3F7858BD9 CRC64; MIKKIGVLTS GGDAPGMNAA IRGVVRSALA EGLEVFGIYD GYLGLYEDRM VQLDRYSVSD MINRGGTFLG SARFPEFRDD KVREIAIENM KKRGLDALVV IGGDGSYMGA KRLTEMGFPC IGLPGTIDND IKGTDYTIGY FTALGTVVEA IDRLRDTSSS HQRISIVEVM GRYCGDLTLA AAIAGGCEFV VVPEVEFSRE DLVAEIKAGI AKGKKHAIVA ITEHICDVDE LARFIETETK RETRSTVLGH IQRGGSPVPY DRILASRMGA YAIELLQQGY GGRCVGIQNE KLVHHDIIDA IENMKRPFKG DWLDCAKKLY //