ID B7WS18_COMTK Unreviewed; 351 AA. AC B7WS18; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 02-JUN-2021, entry version 65. 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=CtesDRAFT_PD4020 {ECO:0000313|EMBL:EED69072.1}; OS Comamonas testosteroni (strain DSM 14576 / KF-1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=399795 {ECO:0000313|EMBL:EED69072.1, ECO:0000313|Proteomes:UP000003039}; RN [1] {ECO:0000313|EMBL:EED69072.1, ECO:0000313|Proteomes:UP000003039} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14576 / KF-1 {ECO:0000313|Proteomes:UP000003039}; RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004; RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.; RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by RT defined pairs of heterotrophic bacteria."; RL Appl. Environ. Microbiol. 70:4053-4063(2004). 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 -!- 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01976}; 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_01976}; CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}. 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:EED69072.1}. 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; AAUJ02000001; EED69072.1; -; Genomic_DNA. DR RefSeq; WP_003057959.1; NZ_AAUJ02000001.1. DR STRING; 399795.CtesDRAFT_PD4020; -. DR EnsemblBacteria; EED69072; EED69072; CtesDRAFT_PD4020. DR GeneID; 60801090; -. DR eggNOG; COG0205; Bacteria. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000003039; 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 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; SSF53784; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01976}. FT DOMAIN 2..299 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT NP_BIND 105..108 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT REGION 128..130 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT REGION 172..174 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT REGION 274..277 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT ACT_SITE 130 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT METAL 106 FT /note="Magnesium; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 10 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 165 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 224 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 268 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT SITE 107 FT /note="Important for substrate specificity; cannot use PPi FT as phosphoryl donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" SQ SEQUENCE 351 AA; 37162 MW; 2055B26C6FCB5E9E CRC64; MRVGVLTGGG DCPGLNAVIR AVTKSLINHG QCEVLGIADG FEGLMDASPR VRALSWDEVS GILHIGGTIL GTSNSANPLR DAATLAQVGR NVKALALDVV VAIGGDGTMS LAHGLAQVGL QCVGVPKTID NDIANCERSF GFDTAVATVT ESLRRIESTA MSHHRVMIVE TMGRHAGWLA LESGIAGAAD IILLPEIDYD LQSIIKVCQE RERRQRYTII CIGEGAKESG QSLTVRERIA HSPDPVRLGG VGHVLRERLQ PHLQSEVRTT VLGHVQRGGD PTPFDRVLAT QFGHHAAQLV LGGQLGHMVT LQNGRIGSVA IADVANTQRT VPLDSPLLTM ARDIGICFGE A //