ID A0A641ARF4_9ACTN Unreviewed; 342 AA. AC A0A641ARF4; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 28-JUN-2023, entry version 13. DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01976}; DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976}; DE Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01976}; GN Name=pfp {ECO:0000256|HAMAP-Rule:MF_01976}; GN ORFNames=ESP62_010005 {ECO:0000313|EMBL:KAA1378662.1}; OS Aeromicrobium fastidiosum. OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales; OC Nocardioidaceae; Aeromicrobium. OX NCBI_TaxID=52699 {ECO:0000313|EMBL:KAA1378662.1}; RN [1] {ECO:0000313|EMBL:KAA1378662.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRBC 14897 {ECO:0000313|EMBL:KAA1378662.1}; RA Li J.; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. 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|HAMAP-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|HAMAP-Rule:MF_01976}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_01976}; CC -!- ACTIVITY REGULATION: Non-allosteric. {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:KAA1378662.1}. 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; SDPP02000002; KAA1378662.1; -; Genomic_DNA. DR AlphaFoldDB; A0A641ARF4; -. DR OrthoDB; 9802503at2; -. 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:InterPro. 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; 3.40.50.450; -; 1. DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 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 PANTHER; PTHR13697:SF52; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 3; 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 TIGRFAMs; TIGR02483; PFK_mixed; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 3: Inferred from homology; 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}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01976}. FT DOMAIN 2..297 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT ACT_SITE 127 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 10 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 103 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 125..127 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 162 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 169..171 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 221 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 266 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 272..275 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT SITE 104 FT /note="Important for catalytic activity and substrate FT specificity; stabilizes the transition state when the FT phosphoryl donor is PPi; prevents ATP from binding by FT mimicking the alpha-phosphate group of ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT SITE 124 FT /note="Important for catalytic activity; stabilizes the FT transition state when the phosphoryl donor is PPi" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" SQ SEQUENCE 342 AA; 36468 MW; B1DCACDBA0250605 CRC64; MRVGMLTGGG DCPGLNAVIR AAVRKGVQQY RHEFIGFRDG WRGPLEDDTM TLGVDEVRGI LPRGGTILGS SRTNPFAIDD GVQRIKDNLD RNGCDALIAI GGEDTLGVAT KLADLGVAVV GVPKTIDNDL SGTDFTFGFD TAVNIATEAI DRLHTTAESH HRVLVVEVMG RHAGWIALHS GLAGGANIIL IPERPFDIEQ VCAQVESRFA THYAPIIVVS EGAVPAEGGD MSLVSGQKDA FGHVRLGGIG DRLASEIEHR TGKEARAVVL GHVQRGGSPT AFDRWLATRF GLHAITAVHE GDFGTMMSLR GTEIARVPLA DGTEKLKTVR ADLYEEAEVF FG //