ID A0A1Z3W4I4_9FLAO Unreviewed; 328 AA. AC A0A1Z3W4I4; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 20-DEC-2017, entry version 3. 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:ASE62699.1}; GN ORFNames=CEQ15_14915 {ECO:0000313|EMBL:ASE62699.1}; OS Chryseobacterium indologenes. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=253 {ECO:0000313|EMBL:ASE62699.1, ECO:0000313|Proteomes:UP000197073}; RN [1] {ECO:0000313|EMBL:ASE62699.1, ECO:0000313|Proteomes:UP000197073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_337 {ECO:0000313|EMBL:ASE62699.1, RC ECO:0000313|Proteomes:UP000197073}; RA Kerrigan L., Tallon L., Sadzewicz L., Sengamalay N., Ott S., RA Godinez A., Nagaraj S., Vavikolanu K., Nadendla S., George J., RA Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx RT tests."; RL Submitted (JUN-2017) 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_00339, CC ECO:0000256|SAAS:SAAS00729178}. 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:SAAS00728855}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00339, ECO:0000256|SAAS:SAAS00640094}; 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:SAAS00640117}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS00643582}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS00640112}. 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 ECO:0000256|SAAS:SAAS00634686}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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; CP022058; ASE62699.1; -; Genomic_DNA. DR RefSeq; WP_027373764.1; NZ_FORL01000004.1. DR GeneID; 32136862; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000197073; 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 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|HAMAP-Rule:MF_00339}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00728960}; KW Complete proteome {ECO:0000313|Proteomes:UP000197073}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00640104}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00640111}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00640102, ECO:0000313|EMBL:ASE62699.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00640121}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00640110}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00728832}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00640113}. FT DOMAIN 8 282 PFK. {ECO:0000259|Pfam:PF00365}. FT NP_BIND 77 78 ATP. {ECO:0000256|HAMAP-Rule:MF_00339}. FT NP_BIND 107 110 ATP. {ECO:0000256|HAMAP-Rule:MF_00339}. FT REGION 26 30 Allosteric activator ADP binding; shared FT with dimeric partner. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 131 133 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 175 177 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 219 221 Allosteric activator ADP binding. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT REGION 258 261 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT ACT_SITE 133 133 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00339}. FT METAL 108 108 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT BINDING 16 16 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 160 160 Allosteric activator ADP. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 168 168 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 228 228 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00339}. FT BINDING 252 252 Substrate; shared with dimeric partner. FT {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 //