ID A0A3N2DLH2_9ENTR Unreviewed; 320 AA. AC A0A3N2DLH2; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 13-NOV-2019, 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=EC848_4567 {ECO:0000313|EMBL:ROS00631.1}; OS Enterobacter sp. BIGb0359. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=2485133 {ECO:0000313|EMBL:ROS00631.1, ECO:0000313|Proteomes:UP000281546}; RN [1] {ECO:0000313|EMBL:ROS00631.1, ECO:0000313|Proteomes:UP000281546} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BIGb0359 {ECO:0000313|EMBL:ROS00631.1, RC ECO:0000313|Proteomes:UP000281546}; RA Samuel B.; RT "Genomic analyses of the natural microbiome of Caenorhabditis RT elegans."; RL Submitted (NOV-2018) 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:SAAS01078966}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose CC 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, CC ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS01116210}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00339, ECO:0000256|SAAS:SAAS00609123}; CC -!- ACTIVITY REGULATION: Allosterically activated by ADP and other CC diphosphonucleosides, and allosterically inhibited by CC phosphoenolpyruvate. {ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS01070487}. 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 -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS00557934}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS00551378}. 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:SAAS01228968}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ROS00631.1}. 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; RKHS01000009; ROS00631.1; -; Genomic_DNA. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000281546; 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 CDD; cd00763; Bacterial_PFK; 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|HAMAP-Rule:MF_00339}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00016785}; KW Complete proteome {ECO:0000313|Proteomes:UP000281546}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00436108}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00436111}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00436062, ECO:0000313|EMBL:ROS00631.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00436079}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00436116}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00016719}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00436075}. FT DOMAIN 4 276 PFK. {ECO:0000259|Pfam:PF00365}. FT NP_BIND 73 74 ATP. {ECO:0000256|HAMAP-Rule:MF_00339}. FT NP_BIND 103 106 ATP. {ECO:0000256|HAMAP-Rule:MF_00339}. FT REGION 22 26 Allosteric activator ADP binding; shared FT with dimeric partner. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 55 60 Allosteric activator ADP binding; shared FT with dimeric partner. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 126 128 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 170 172 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 186 188 Allosteric activator ADP binding. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT REGION 214 216 Allosteric activator ADP binding. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT REGION 250 253 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT ACT_SITE 128 128 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00339}. FT METAL 104 104 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT BINDING 12 12 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 155 155 Allosteric activator ADP. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 163 163 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 212 212 Allosteric activator ADP. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 223 223 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00339}. FT BINDING 244 244 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00339}. SQ SEQUENCE 320 AA; 35005 MW; D15012D3F7858BD9 CRC64; MIKKIGVLTS GGDAPGMNAA IRGVVRSALA EGLEVFGIYD GYLGLYEDRM VQLDRYSVSD MINRGGTFLG SARFPEFRDD KVREIAIENM KKRGLDALVV IGGDGSYMGA KRLTEMGFPC IGLPGTIDND IKGTDYTIGY FTALGTVVEA IDRLRDTSSS HQRISIVEVM GRYCGDLTLA AAIAGGCEFV VVPEVEFSRE DLVAEIKAGI AKGKKHAIVA ITEHICDVDE LARFIETETK RETRSTVLGH IQRGGSPVPY DRILASRMGA YAIELLQQGY GGRCVGIQNE KLVHHDIIDA IENMKRPFKG DWLDCAKKLY //