ID A0A246BB85_9FLAO Unreviewed; 328 AA. AC A0A246BB85; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 02-DEC-2020, entry version 13. 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=AP75_03435 {ECO:0000313|EMBL:OWK98915.1}; OS Chryseobacterium haifense DSM 19056. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; Weeksellaceae; OC Chryseobacterium. OX NCBI_TaxID=1450526 {ECO:0000313|EMBL:OWK98915.1, ECO:0000313|Proteomes:UP000197587}; RN [1] {ECO:0000313|EMBL:OWK98915.1, ECO:0000313|Proteomes:UP000197587} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19056 {ECO:0000313|EMBL:OWK98915.1, RC ECO:0000313|Proteomes:UP000197587}; RG Genome Consortium for Active Teaching; RA Sontag T.C., Newman J.D.; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:OWK98915.1, ECO:0000313|Proteomes:UP000197587} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19056 {ECO:0000313|EMBL:OWK98915.1, RC ECO:0000313|Proteomes:UP000197587}; RA Newman J.D.; RT "Genome of Chryseobacterium haifense."; RL Submitted (MAY-2017) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OWK98915.1}. 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; JASZ02000004; OWK98915.1; -; Genomic_DNA. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000197587; 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:OWK98915.1}; 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}. FT DOMAIN 8..281 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; 34971 MW; DCD57F83B1CD9348 CRC64; MNESAVKKIA VLTSGGDAPG MNAALRAVVR TANHYVIECF GVREGYNGLI NDDFTKMGPR SVKNIIGAGG TILRSARSLE FKTKEGRQKA YDNCIKHGID GLVCIGGDGT FTGAKIFNEE FGIKVIGVPG TIDNDIFGTD NTIGYDTALN TAMDAIDKIR DTATSHNRVF FVEVMGRDAG FIALNSGLAT GAVDILIPEK KDSIEDLFAT FERAEKAGKS SSIVVVAEGE KLGSIYDLAK ATKAGFPDYD IRVAILGHIQ RGGSPSCADR VLASRLGFGA VVGLMKGKTN VMAGLQSNNL VFTPFEEAIK KHNEINQELM LLSEILAI //