ID A0A014MT88_9BURK Unreviewed; 354 AA. AC A0A014MT88; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 24-JUN-2015, entry version 13. DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976}; DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_01976}; DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976}; DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_01976, ECO:0000256|SAAS:SAAS00016842}; DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_01976}; GN Name=pfkA {ECO:0000256|HAMAP-Rule:MF_01976}; GN ORFNames=AX13_10620 {ECO:0000313|EMBL:EXU81249.1}; OS Comamonas aquatica DA1877. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=1457173 {ECO:0000313|EMBL:EXU81249.1}; RN [1] {ECO:0000313|EMBL:EXU81249.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DA1877 {ECO:0000313|EMBL:EXU81249.1}; RA Watson E., Macneil L.T., Ritter A.D., Yilmaz L.S., Rosebrock A.P., RA Caudy A.A., Walhout A.J.; RT "Interspecies Systems Biology Uncovers Metabolites Affecting C. RT elegans Gene Expression and Life History Traits."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate CC to fructose 1,6-bisphosphate by ATP, the first committing step of CC glycolysis. {ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D- CC fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-Rule:MF_01976, CC ECO:0000256|SAAS:SAAS00016817}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={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:SAAS00041065}. 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 -!- 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:EXU81249.1}. 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; JBOK01000003; EXU81249.1; -; Genomic_DNA. DR EnsemblBacteria; EXU81249; EXU81249; AX13_10620. DR UniPathway; UPA00109; UER00182. 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:UniProtKB-KW. DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro. 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; IPR015912; Phosphofructokinase_CS. 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. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|RuleBase:RU004092}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00041050}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00041074}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|RuleBase:RU004092}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00041077}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00041029}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|RuleBase:RU004092}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|RuleBase:RU004092}. FT NP_BIND 105 108 ATP. {ECO:0000256|HAMAP-Rule:MF_01976}. FT REGION 129 131 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 173 175 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 275 278 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT ACT_SITE 131 131 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT METAL 106 106 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT BINDING 10 10 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT BINDING 166 166 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT BINDING 225 225 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT BINDING 269 269 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT SITE 107 107 Important for substrate specificity; FT cannot use PPi as phosphoryl donor. FT {ECO:0000256|HAMAP-Rule:MF_01976}. SQ SEQUENCE 354 AA; 37274 MW; A08790ECBE13938C CRC64; MKVGVLTGGG DCPGLNAVIR AVTKSLISQG QCEVIGIADG FEGLMGATPR VKPLTWDEVS GILHIGGTIL GTSNSANPLK SEATLAQVKS NVQALGLDVV VAIGGDGTMS LANGLANAVG MQCVGVPKTI DNDIASCERS FGFDTAVATA TEALRRIEST ANSHHRVMIV ETMGRNAGWL ALEAGVAGAA DIILLPEIDY DLQAIVDVCQ AREQRQRYTI ICIGEGAKES GHSLTVRETI AHSPDPVRLG GVGHVLRERL QPHLRSEVRT TVLGHVQRGG DPTPFDRVLA TQFGHHAAQL VLSGRFGRMV TLQQGQIGSV EIAQVANTQR RIDLAHPLLT MARDIGICLG EAAR //