ID B7WS18_COMTE Unreviewed; 351 AA. AC B7WS18; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 31-OCT-2012, entry version 20. 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 -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the phosphofructokinase family. 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 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: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:glycolysis; IEA: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; Ppfruckinase; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding; KW Transferase. FT NP_BIND 20 24 ATP (By similarity). FT NP_BIND 157 161 ATP (By similarity). FT NP_BIND 174 190 ATP (By similarity). FT ACT_SITE 130 130 Proton acceptor (By similarity). FT BINDING 165 165 Substrate (By similarity). FT BINDING 268 268 Substrate (By similarity). FT BINDING 274 274 Substrate (By similarity). FT BINDING 277 277 Substrate (By similarity). 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 //