ID D1CD35_THET1 Unreviewed; 342 AA. AC D1CD35; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-APR-2014, entry version 31. DE RecName: Full=6-phosphofructokinase; DE Short=Phosphofructokinase; DE EC=2.7.1.11; DE AltName: Full=Phosphohexokinase; GN Name=pfkA; OrderedLocusNames=Tter_1794; OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1). OC Bacteria; Thermobaculum. OX NCBI_TaxID=525904; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-798 / YNP1; RX DOI=10.4056/sigs.1153107; RA Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., RA Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M., RA Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T., RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Kyrpides N., Klenk H., Cheng J.; RT "Complete genome sequence of Thermobaculum terrenum type strain RT (YNP1T)."; RL Stand. Genomic Sci. 3:153-162(2010). 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; CP001825; ACZ42700.1; -; Genomic_DNA. DR RefSeq; YP_003323522.1; NC_013525.1. DR ProteinModelPortal; D1CD35; -. DR EnsemblBacteria; ACZ42700; ACZ42700; Tter_1794. DR GeneID; 8646305; -. DR KEGG; ttr:Tter_1794; -. DR PATRIC; 32503912; VBITheTer68767_1921. DR HOGENOM; HOG000248869; -. DR KO; K00850; -. DR OMA; CPGINAT; -. DR OrthoDB; EOG644ZRM; -. DR BioCyc; TTER525904:GHMJ-1850-MONOMER; -. 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: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:glycolysis; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00339; Phosphofructokinase; 1. DR InterPro; IPR012003; ATP_PFK_prok. DR InterPro; IPR022953; Phosphofructokinase. 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. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase; KW Magnesium; Metal-binding; Nucleotide-binding; Transferase. FT NP_BIND 20 24 ATP (By similarity). FT NP_BIND 153 157 ATP (By similarity). FT NP_BIND 170 186 ATP (By similarity). FT ACT_SITE 126 126 Proton acceptor (By similarity). FT METAL 184 184 Magnesium; via carbonyl oxygen (By FT similarity). FT METAL 186 186 Magnesium (By similarity). FT BINDING 161 161 Substrate (By similarity). FT BINDING 266 266 Substrate (By similarity). FT BINDING 272 272 Substrate (By similarity). FT BINDING 275 275 Substrate (By similarity). SQ SEQUENCE 342 AA; 36855 MW; 628C628D7B1BA090 CRC64; MKVGVLTGGG DAPGLNAAIR AVVLSALSRG DEVVGFLDGW KGVQDNLTIP LDREWVQDIH EVGGTNLGTS RTNPMKSEDT MKAVENHFRE NGLDVLIAIG GDDTLSVAAE LDRRGFPVVG VPKTMDNDVP ETDYCIGFDT AVNRLMESID RLRTTSRSHH RVMVVEAMGR DAGWVAGFGG LAGGADVILV PEIEVDLDDV AQRLEKVRSR GRSYAIVVAA EGISFGEAQV PENAKTDAFG HVILAEKAVG ERLAQEIESR LGWETRSIQI GHLHRGGSPT AFDRILGTRY GEKAVELAHN NSFGQMVVLH GLDLTTVPLA QIAGKTKTLY PQFIELIQNL NA //