ID A4SGR6_CHLPM Unreviewed; 359 AA. AC A4SGR6; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 113. 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 OrderedLocusNames=Cvib_1665 {ECO:0000313|EMBL:ABP37675.1}; OS Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris OS vibrioformis (strain DSM 265)). OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290318 {ECO:0000313|EMBL:ABP37675.1}; RN [1] {ECO:0000313|EMBL:ABP37675.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 265 {ECO:0000313|EMBL:ABP37675.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., RA Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., RA Schuster S.C., Bryant D.A., Richardson P.; RT "Complete sequence of Prosthecochloris vibrioformis DSM 265."; RL Submitted (MAR-2007) 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_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, ECO:0000256|HAMAP- CC 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; CP000607; ABP37675.1; -; Genomic_DNA. DR AlphaFoldDB; A4SGR6; -. DR STRING; 290318.Cvib_1665; -. DR KEGG; pvi:Cvib_1665; -. DR eggNOG; COG0205; Bacteria. DR HOGENOM; CLU_020655_0_1_10; -. DR UniPathway; UPA00109; UER00182. 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 Gene3D; 3.40.50.450; -; 1. DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 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 NCBIfam; TIGR02482; PFKA_ATP; 1. DR PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1. DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000532; ATP_PFK_prok; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; Phosphofructokinase; 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 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 38..314 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 163 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 46 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 56..60 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_note="allosteric activator; ligand shared between FT dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 107..108 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 137..140 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 138 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 161..163 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 190 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_note="allosteric activator; ligand shared between FT dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 198 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 205..207 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 221..223 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_note="allosteric activator; ligand shared between FT dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 258 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 282 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" FT BINDING 288..291 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339" SQ SEQUENCE 359 AA; 38658 MW; 9F7F93EA3913ECE8 CRC64; MKGQPRLRES RTLHPPMATM TRKSDNDQLS FTSGRIKKIG ILTSGGDAPG MNAAIRAATR SAIAAGREAV GILRGYQGMI DGDFIPLQST DVSGILQLGG TMLKTARCKE FRTPEGRRRA KEQLTAAAID AVIVIGGDGS FTGAWVMSQE CDIPFVGIPA TIDNDMYGTD YTIGYETALN SVVCAVDKIK DTARSHGRIF FIEVMGHEAG LLALNSGIAC GAEVILIPES KAQHEELQKF LEKGYRDKES SGIVMVAEGD EAGGALHIAE QIRRDHPDLD VRISILGHIQ RGGSPVARDR INATRMGIAA VDALLNDQKS IMIGLDNNRI VHVTFNKAVK MNHSIDTGLL EVHNLLNGM //