ID B7WS18_COMTE Unreviewed; 351 AA. AC B7WS18; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 11-JUN-2014, entry version 26. DE RecName: Full=6-phosphofructokinase; DE Short=Phosphofructokinase; DE EC=2.7.1.11; DE AltName: Full=Phosphohexokinase; GN Name=pfkA; ORFNames=CtesDRAFT_PD4020; OS Comamonas testosteroni KF-1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=399795; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KF-1; 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 RT alkylbenzenesulfonate by defined pairs of heterotrophic bacteria."; RL Appl. Environ. Microbiol. 70:4053-4063(2004). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KF-1; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Lowry S., RA Sun H., Larimer F., Land M.L., Hauser L., Kjelleberg S., Cook A., RA Knepper T.P., Fischer K., Schleheck D., Richardson P.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D- CC fructose 1,6-bisphosphate. CC -!- COFACTOR: Magnesium (By similarity). CC -!- ENZYME REGULATION: Subject to allosteric activation by ADP and CC other diphosphonucleosides, and inhibition by phosphoenolpyruvate CC (By similarity). CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the phosphofructokinase family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. 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 ProteinModelPortal; B7WS18; -. DR EnsemblBacteria; EED69072; EED69072; CtesDRAFT_PD4020. DR PATRIC; 29059527; VBIComTes39478_3969. DR UniPathway; UPA00109; UER00182. DR GO; GO:0005945; C:6-phosphofructokinase complex; IEA:InterPro. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00339; Phosphofructokinase; 1. DR InterPro; IPR012003; ATP_PFK_prok. DR InterPro; IPR022953; Phosphofructokinase. DR InterPro; IPR015912; Phosphofructokinase_CS. DR InterPro; IPR000023; Phosphofructokinase_dom. 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 Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; KW Magnesium; Metal-binding; Nucleotide-binding; Transferase. FT NP_BIND 105 108 ATP (By similarity){EA11}. FT REGION 128 130 Substrate binding (By similarity). FT REGION 172 174 Substrate binding (By similarity). FT REGION 274 277 Substrate binding (By similarity). FT ACT_SITE 130 130 Proton acceptor (By similarity){EA11}. FT METAL 106 106 Magnesium; catalytic (By FT similarity){EA11}. FT BINDING 10 10 ATP; via amide nitrogen (By FT similarity){EA11}. FT BINDING 165 165 Substrate; shared with dimeric partner FT (By similarity){EA11}. FT BINDING 224 224 Substrate (By similarity){EA11}. FT BINDING 268 268 Substrate; shared with dimeric partner FT (By similarity){EA11}. 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 //