ID A0A1B9VNQ5_9PROT Unreviewed; 368 AA. AC A0A1B9VNQ5; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 03-AUG-2022, entry version 20. DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976}; DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_01976}; DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976}; DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_01976}; GN Name=pfkA {ECO:0000256|HAMAP-Rule:MF_01976}; GN ORFNames=KO164_4261 {ECO:0000313|EMBL:OCK10079.1}; OS Thalassospira sp. KO164. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Thalassospiraceae; Thalassospira; unclassified Thalassospira. OX NCBI_TaxID=1798192 {ECO:0000313|EMBL:OCK10079.1, ECO:0000313|Proteomes:UP000093204}; RN [1] {ECO:0000313|EMBL:OCK10079.1, ECO:0000313|Proteomes:UP000093204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KO164 {ECO:0000313|EMBL:OCK10079.1, RC ECO:0000313|Proteomes:UP000093204}; RA Hazen T., Woo H., Brown S., Utturkar S., Huntemann M., Clum A., Pillay M., RA Palaniappan K., Varghese N., Mikhailova N., Stamatis D., Reddy T., RA Ngan C.Y., Daum C., Shapiro N., Markowitz V., Ivanova N., Kyrpides N., RA Woyke T.; RT "Draft Genome Sequences for Thalassospira sp. KO164."; RL Submitted (JUN-2016) 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|HAMAP-Rule:MF_01976}. CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the CC first committing step of glycolysis. Uses inorganic phosphate (PPi) as CC phosphoryl donor instead of ATP like common ATP-dependent CC phosphofructokinases (ATP-PFKs), which renders the reaction reversible, CC and can thus function both in glycolysis and gluconeogenesis. CC Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- CC PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. CC {ECO:0000256|ARBA:ARBA00003138}. 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01976}; CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose CC 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; CC Evidence={ECO:0000256|ARBA:ARBA00000628}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_01976}; 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_01976}. CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC Mixed-substrate PFK group III subfamily. {ECO:0000256|HAMAP- CC Rule:MF_01976}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01976}. 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:OCK10079.1}. 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; MAJC01000002; OCK10079.1; -; Genomic_DNA. DR RefSeq; WP_007091088.1; NZ_MAJC01000002.1. DR EnsemblBacteria; OCK10079; OCK10079; KO164_4261. DR PATRIC; fig|1798192.3.peg.4538; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000093204; 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:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC. 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_01976; Phosphofructokinase_III; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR012003; ATP_PFK_prok-type. DR InterPro; IPR015912; Phosphofructokinase_CS. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR012829; Phosphofructokinase_III. 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 PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01976}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01976}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_01976}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01976}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01976}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01976}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01976}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01976}. FT DOMAIN 2..307 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT REGION 137..139 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT REGION 181..183 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT REGION 281..284 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT ACT_SITE 139 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 10 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 76..77 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 113..116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 114 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 174 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 234 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 275 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT SITE 115 FT /note="Important for substrate specificity; cannot use PPi FT as phosphoryl donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" SQ SEQUENCE 368 AA; 38954 MW; 2A3F530078979B2F CRC64; MRIGILTSGG DCAGLNAVIL AVVRRAVLGY GWDVVGIRQG THGLMQDPPQ AIDLNDYVNN DGMLRLGGTI LGTVNKGDPF HYPMPDGSFA DRSADVIAGY HKLGLDALIG VGGDGSMAIL HRLAEMGGIN LVGIPKTIDN DLALTEYSVG FTTAVNVAVE ALDRLQPTAA SHDRIMILEV MGRDAGHIAL FAGVAGGADA ILIPEMDYDL DALTEHCLNI RKRGRNHALV IVAEAVKRDD GAAVTQGDDG QKIRYGGIGH WLADELGART GWETRVTVLG HVQRGGIPSP RDRVIASAFG VHAVDLIAQK RFDRVVAWSK RKVIDVAMAD VIVGPRLVDT KGTMVSTAKG LGAYLGHPPE TARTAKTV //