ID A0A1Z3W4I4_9FLAO Unreviewed; 328 AA. AC A0A1Z3W4I4; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 12-AUG-2020, entry version 20. 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 ECO:0000313|EMBL:VFA42203.1}; GN ORFNames=FE904_21755 {ECO:0000313|EMBL:TLX23455.1}, NCTC11409_02214 GN {ECO:0000313|EMBL:VFA42203.1}; OS Chryseobacterium indologenes. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=253 {ECO:0000313|EMBL:VFA42203.1, ECO:0000313|Proteomes:UP000290630}; RN [1] {ECO:0000313|EMBL:VFA42203.1, ECO:0000313|Proteomes:UP000290630} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3012STDY6981895 {ECO:0000313|EMBL:VFA42203.1, RC ECO:0000313|Proteomes:UP000290630}; RG Pathogen Informatics; RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:TLX23455.1, ECO:0000313|Proteomes:UP000309139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0243 {ECO:0000313|EMBL:TLX23455.1, RC ECO:0000313|Proteomes:UP000309139}; RA Rabenandrasana M.A.N., Collard J.M., Rafetrarivony L.F.; RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases. 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; VCBR01000031; TLX23455.1; -; Genomic_DNA. DR EMBL; LR215967; VFA42203.1; -; Genomic_DNA. DR RefSeq; WP_027373764.1; NZ_VCBR01000031.1. DR KEGG; cio:CEQ15_14915; -. DR KO; K00850; -. DR OrthoDB; 1421302at2; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000290630; Chromosome 1. DR Proteomes; UP000309139; Unassembled WGS sequence. 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 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 ECO:0000313|EMBL:VFA42203.1}; 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}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00339, ECO:0000313|EMBL:VFA42203.1}. FT DOMAIN 8..282 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT NP_BIND 77..78 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT NP_BIND 107..110 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 26..30 FT /note="Allosteric activator ADP binding; shared with FT dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 131..133 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 175..177 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 219..221 FT /note="Allosteric activator ADP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT REGION 258..261 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT ACT_SITE 133 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT METAL 108 FT /note="Magnesium; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 16 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 160 FT /note="Allosteric activator ADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 168 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 228 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 252 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" SQ SEQUENCE 328 AA; 35365 MW; C50BBBF6DDC48545 CRC64; MKESAVKKIA VLTSGGDSPG MNAALRAVVR TANYYNIECY GVREGYNGLI NNDFLKMGAR SVKNIINQGG TILKSARSAE FRTKEGRQKA YDNCVKLGID GLVCIGGDGT FTGAKIFNEE FGIRVIGIPG TIDNDIFGTD NTIGYDTALN TAMDAIDKIR DTATSHNRVF FVEVMGRDAG FIALNSGLAA GALDILIPEK KDSIDELFAK FRNAEKTGKA SSIVVVAEGE KLANVYELAE KTKKTFPDYD IRVAILGHMQ RGGSPSCADR VLASRLGYGA VTGLMEGQTN VMAGMRSNDL TYTPIEEAIK KHNEINKDLL LISEILAL //