ID B7WS18_COMTE Unreviewed; 351 AA. AC B7WS18; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 07-JAN-2015, entry version 32. DE SubName: Full=6-phosphofructokinase {ECO:0000313|EMBL:EED69072.1}; DE EC=2.7.1.11 {ECO:0000313|EMBL:EED69072.1}; GN ORFNames=CtesDRAFT_PD4020 {ECO:0000313|EMBL:EED69072.1}; OS Comamonas testosteroni KF-1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=399795 {ECO:0000313|EMBL:EED69072.1}; RN [1] {ECO:0000313|EMBL:EED69072.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KF-1 {ECO:0000313|EMBL:EED69072.1}; 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] {ECO:0000313|EMBL:EED69072.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KF-1 {ECO:0000313|EMBL:EED69072.1}; 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. {ECO:0000256|SAAS:SAAS00016817}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000256|SAAS:SAAS00054603}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00054613}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 ProteinModelPortal; B7WS18; -. DR EnsemblBacteria; EED69072; EED69072; CtesDRAFT_PD4020. DR PATRIC; 29059527; VBIComTes39478_3969. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC. 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 GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00339; Phosphofructokinase; 1. DR InterPro; IPR012003; ATP_PFK_prok-type. 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 ATP-binding {ECO:0000256|RuleBase:RU004092, KW ECO:0000256|SAAS:SAAS00016785}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00054573}; KW Glycolysis {ECO:0000256|SAAS:SAAS00054606}; KW Kinase {ECO:0000256|RuleBase:RU004092, ECO:0000256|SAAS:SAAS00054644}; KW Magnesium {ECO:0000256|SAAS:SAAS00054585}; KW Metal-binding {ECO:0000256|SAAS:SAAS00054599}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU004092, KW ECO:0000256|SAAS:SAAS00016719}; KW Transferase {ECO:0000256|RuleBase:RU004092, KW ECO:0000256|SAAS:SAAS00054633}. 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 //