ID K6PF_BAUCH Reviewed; 320 AA. AC Q1LTT2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 29. DE RecName: Full=6-phosphofructokinase; DE Short=Phosphofructokinase; DE EC=2.7.1.11; DE AltName: Full=Phosphohexokinase; GN Name=pfkA; OrderedLocusNames=BCI_0171; OS Baumannia cicadellinicola subsp. Homalodisca coagulata. OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia. OX NCBI_TaxID=374463; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16729848; DOI=10.1371/journal.pbio.0040188; RA Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., RA Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., RA Moran N.A., Eisen J.A.; RT "Metabolic complementarity and genomics of the dual bacterial RT symbiosis of sharpshooters."; RL PLoS Biol. 4:1079-1092(2006). 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 http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000238; ABF13987.1; -; Genomic_DNA. DR RefSeq; YP_588632.1; -. DR SMR; Q1LTT2; 1-320. DR GeneID; 4056734; -. DR GenomeReviews; CP000238_GR; BCI_0171. DR KEGG; bci:BCI_0171; -. DR HOGENOM; Q1LTT2; -. DR OMA; Q1LTT2; DTCLNTV. 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:0000287; F:magnesium ion 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; -; 1. DR InterPro; IPR012003; ATP_PFK_prok. DR InterPro; IPR012828; PFKA_ATP. DR InterPro; IPR000023; Phosphofructokinase. DR InterPro; IPR015912; Phosphofructokinase_CS. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000532; ATP_PFK_prok; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR ProDom; PD000707; Ppfruckinase; 1. DR TIGRFAMs; TIGR02482; PFKA_ATP; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase; KW Magnesium; Metal-binding; Nucleotide-binding; Transferase. FT CHAIN 1 320 6-phosphofructokinase. FT /FTId=PRO_1000059747. FT NP_BIND 22 26 ATP (By similarity). FT NP_BIND 155 159 ATP (By similarity). FT NP_BIND 172 188 ATP (By similarity). FT ACT_SITE 128 128 Proton acceptor (By similarity). FT METAL 186 186 Magnesium; via carbonyl oxygen (By FT similarity). FT METAL 188 188 Magnesium (By similarity). FT BINDING 163 163 Substrate (By similarity). FT BINDING 244 244 Substrate (By similarity). FT BINDING 250 250 Substrate (By similarity). FT BINDING 253 253 Substrate (By similarity). SQ SEQUENCE 320 AA; 35151 MW; 5D589CA6F26A332A CRC64; MINKIGVLTS GGDSPGMNAA IRSVVRAGLS EGLEIYGISD GYQGLYQDRM RKLDRYSVSD IINRGGTFLG SARFQEFREE AIRAIALNNM SKYGLGALVV IGGDGSYMGA KLLTEMGLPC IGLPGTIDND VAGTDYTIGY FTALETVVEA IDRLRDTSTS HQRISIVEVM GRYCGDLTMA AAIAGGCEFI VLPEVEFQPE DLVYEIKASI AQGKKHAIVA ITEYICNVFE LALYIEKETG RETRATVLGH IQRGGNPVAY DRILASRMGA YSIELLLQGY RGRCVGVQNE RLVHHDIADV IQNMKRPFRR DFLETARKLF //