ID A0A075R076_BRELA Unreviewed; 319 AA. AC A0A075R076; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 29-APR-2015, entry version 5. DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339}; DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_00339}; DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339}; DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_00339}; DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_00339}; GN Name=pfkA {ECO:0000256|HAMAP-Rule:MF_00339}; GN ORFNames=BRLA_c009080 {ECO:0000313|EMBL:AIG25249.1}; OS Brevibacillus laterosporus LMG 15441. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG25249.1, ECO:0000313|Proteomes:UP000005850}; RN [1] {ECO:0000313|EMBL:AIG25249.1, ECO:0000313|Proteomes:UP000005850} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG25249.1}; RX PubMed=21914864; DOI=10.1128/JB.05696-11; RA Djukic M., Poehlein A., Thurmer A., Daniel R.; RT "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen RT of invertebrates."; RL J. Bacteriol. 193:5535-5536(2011). 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_00339, CC ECO:0000256|SAAS:SAAS00197172}. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D- CC fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS00197186}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00339, ECO:0000256|SAAS:SAAS00195316}; CC -!- ENZYME REGULATION: Allosterically activated by ADP and other CC diphosphonucleosides, and allosterically inhibited by CC phosphoenolpyruvate. {ECO:0000256|HAMAP-Rule:MF_00339}. 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_00339, ECO:0000256|SAAS:SAAS00041065}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS00195319}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS00054613}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) CC family. ATP-dependent PFK group I subfamily. Prokaryotic clade CC "B1" sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_00339}. 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; CP007806; AIG25249.1; -; Genomic_DNA. DR EnsemblBacteria; AIG25249; AIG25249; BRLA_c009080. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000005850; Chromosome. 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: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_00339; Phosphofructokinase_I_B1; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR012003; ATP_PFK_prok-type. DR InterPro; IPR012828; PFKA_ATP_prok. 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 TIGRFAMs; TIGR02482; PFKA_ATP; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 3: Inferred from homology; KW Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_00339}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00197198}; KW Complete proteome {ECO:0000313|Proteomes:UP000005850}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00041050}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00041074}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|RuleBase:RU004092}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00041077}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00041029}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00197176}; KW Reference proteome {ECO:0000313|Proteomes:UP000005850}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|RuleBase:RU004092}. FT NP_BIND 72 73 ATP. {ECO:0000256|HAMAP-Rule:MF_00339}. FT NP_BIND 102 105 ATP. {ECO:0000256|HAMAP-Rule:MF_00339}. FT REGION 21 25 Allosteric activator ADP binding; shared FT with dimeric partner. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 125 127 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 169 171 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 185 187 Allosteric activator ADP binding. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT REGION 213 215 Allosteric activator ADP binding. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT REGION 249 252 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT ACT_SITE 127 127 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00339}. FT METAL 103 103 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT BINDING 11 11 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 154 154 Allosteric activator ADP. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 162 162 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 211 211 Allosteric activator ADP. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 222 222 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00339}. FT BINDING 243 243 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00339}. SQ SEQUENCE 319 AA; 34183 MW; E75D6E074AA640AF CRC64; MKKIAVLTSG GDAPGMNAAV RAAVRRAIYK GVQIFGVYNG YNGLISGNIK ELTLGSVGDI IHRGGTMLFT ARSDEFRTEE GRAKAVEQLK KHGIEGLIVI GGDGSFRGAQ KLTQLGFPTI GVPGTIDNDI PCTDFTIGFD TALNTVVECI DKIRDTATSH ERTYIVEVMG RDAGDLALWA GLAAGAESII IPEADTDMKD ILERLRSGHR RGKKHSIIIV AEGVGQASQF ADVIKAETGW ETRVTVLGHI QRGGSPTAFD RMLASRLGAA AVDLLLEGKA DRMVGIKNNT IVDVDIDEAL DQKHQLDLSI YQLARSLSI //