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-SEP-2021, entry version 39. 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; 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, RC ECO:0000313|Proteomes:UP000005850}; 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 of RT invertebrates."; RL J. Bacteriol. 193:5535-5536(2011). CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to CC fructose 1,6-bisphosphate by ATP, the first committing step of CC glycolysis. {ECO:0000256|ARBA:ARBA00002659, ECO:0000256|HAMAP- CC Rule:MF_00339}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6- CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, CC ChEBI:CHEBI:456216; EC=2.7.1.11; CC Evidence={ECO:0000256|ARBA:ARBA00000432, ECO:0000256|HAMAP- CC Rule:MF_00339}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_00339}; CC -!- ACTIVITY 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|ARBA:ARBA00004679, ECO:0000256|HAMAP-Rule:MF_00339}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00339}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00339}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub- CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00339}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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 RefSeq; WP_003335243.1; NZ_CP007806.1. DR STRING; 1042163.BRLA_c009080; -. DR EnsemblBacteria; AIG25249; AIG25249; BRLA_c009080. DR KEGG; blr:BRLA_c009080; -. DR eggNOG; COG0205; Bacteria. DR HOGENOM; CLU_020655_0_1_9; -. DR OrthoDB; 1421302at2; -. 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-UniRule. 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 Gene3D; 3.40.50.460; -; 1. 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 InterPro; IPR035966; PKF_sf. 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|ARBA:ARBA00022533, ECO:0000256|HAMAP- KW Rule:MF_00339}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00339}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00339}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_00339}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00339}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00339}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00339}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00339}; Reference proteome {ECO:0000313|Proteomes:UP000005850}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00339}. FT DOMAIN 3..275 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT NP_BIND 72..73 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT NP_BIND 102..105 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 21..25 FT /note="ADP binding; allosteric activator; shared with FT dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 125..127 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 169..171 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 185..187 FT /note="ADP binding; allosteric activator" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 213..215 FT /note="ADP binding; allosteric activator" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 249..252 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT ACT_SITE 127 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT METAL 103 FT /note="Magnesium; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 11 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 154 FT /note="ADP; allosteric activator" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 162 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 211 FT /note="ADP; allosteric activator" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 222 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 243 FT /note="Substrate; shared with dimeric partner" FT /evidence="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 //