ID D1CD35_THET1 Unreviewed; 342 AA. AC D1CD35; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAY-2015, entry version 42. DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01976}; DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01976}; GN Name=pfp {ECO:0000256|HAMAP-Rule:MF_01976}; GN OrderedLocusNames=Tter_1794 {ECO:0000313|EMBL:ACZ42700.1}; OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1). OC Bacteria; Thermobaculum. OX NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ42700.1, ECO:0000313|Proteomes:UP000000323}; RN [1] {ECO:0000313|Proteomes:UP000000323} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323}; 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 -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, CC the first committing step of glycolysis. Uses inorganic phosphate CC (PPi) as phosphoryl donor instead of ATP like common ATP-dependent CC phosphofructokinases (ATP-PFKs), which renders the reaction CC reversible, and can thus function both in glycolysis and CC gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of CC both the forward (ATP-PFK) and reverse (fructose-bisphosphatase CC (FBPase)) reactions. {ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate = CC phosphate + D-fructose 1,6-bisphosphate. {ECO:0000256|HAMAP- CC Rule:MF_01976}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01976}; CC -!- ENZYME REGULATION: Non-allosteric. {ECO:0000256|HAMAP- CC Rule:MF_01976}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000256|HAMAP-Rule:MF_01976, ECO:0000256|SAAS:SAAS00054603}. CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP- CC Rule:MF_01976}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976, CC ECO:0000256|SAAS:SAAS00054613}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) CC family. Mixed-substrate PFK group III subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01976}. 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; WP_012875732.1; NC_013525.1. DR RefSeq; YP_003323522.1; NC_013525.1. DR ProteinModelPortal; D1CD35; -. DR EnsemblBacteria; ACZ42700; ACZ42700; Tter_1794. DR KEGG; ttr:Tter_1794; -. DR PATRIC; 32503912; VBITheTer68767_1921. DR HOGENOM; HOG000248869; -. DR KO; K00850; -. DR OMA; MHYETQV; -. DR OrthoDB; EOG644ZRM; -. DR BioCyc; TTER525904:GHMJ-1850-MONOMER; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000000323; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. 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 GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01976; Phosphofructokinase_III; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR012003; ATP_PFK_prok-type. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR012829; Phosphofructokinase_III. 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 Complete proteome {ECO:0000313|Proteomes:UP000000323}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00054573}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00054606}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00054644}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00054585}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00054599}; KW Reference proteome {ECO:0000313|Proteomes:UP000000323}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00054633}. FT REGION 124 126 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 168 170 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 272 275 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT ACT_SITE 126 126 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT METAL 102 102 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT BINDING 10 10 Diphosphate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT BINDING 161 161 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT BINDING 221 221 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT BINDING 266 266 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT SITE 103 103 Important for catalytic activity and FT substrate specificity; stabilizes the FT transition state when the phosphoryl FT donor is PPi; prevents ATP from binding FT by mimicking the alpha-phosphate group of FT ATP. {ECO:0000256|HAMAP-Rule:MF_01976}. FT SITE 123 123 Important for catalytic activity; FT stabilizes the transition state when the FT phosphoryl donor is PPi. FT {ECO:0000256|HAMAP-Rule:MF_01976}. 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 //