ID PDXJ_SYNS9 Reviewed; 249 AA. AC Q3AVH3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 28-JAN-2026, entry version 105. DE RecName: Full=Pyridoxine 5'-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00279}; DE Short=PNP synthase {ECO:0000255|HAMAP-Rule:MF_00279}; DE EC=2.6.99.2 {ECO:0000255|HAMAP-Rule:MF_00279}; GN Name=pdxJ {ECO:0000255|HAMAP-Rule:MF_00279}; GN OrderedLocusNames=Syncc9902_1414; OS Synechococcus sp. (strain CC9902). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Synechococcaceae; Synechococcus. OX NCBI_TaxID=316279; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC9902; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Synechococcus sp. CC9902."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the complicated ring closure reaction between the CC two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino- CC 2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form CC pyridoxine 5'-phosphate (PNP) and inorganic phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00279}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-amino-2-oxopropyl phosphate + 1-deoxy-D-xylulose 5-phosphate CC = pyridoxine 5'-phosphate + phosphate + 2 H2O + H(+); CC Xref=Rhea:RHEA:15265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57279, ChEBI:CHEBI:57792, CC ChEBI:CHEBI:58589; EC=2.6.99.2; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00279}; CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5. CC {ECO:0000255|HAMAP-Rule:MF_00279}. CC -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000255|HAMAP- CC Rule:MF_00279}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00279}. CC -!- SIMILARITY: Belongs to the PNP synthase family. {ECO:0000255|HAMAP- CC Rule:MF_00279}. 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; CP000097; ABB26378.1; -; Genomic_DNA. DR RefSeq; WP_011360200.1; NC_007513.1. DR AlphaFoldDB; Q3AVH3; -. DR SMR; Q3AVH3; -. DR STRING; 316279.Syncc9902_1414; -. DR KEGG; sye:Syncc9902_1414; -. DR eggNOG; COG0854; Bacteria. DR HOGENOM; CLU_074563_0_0_3; -. DR OrthoDB; 9806590at2; -. DR UniPathway; UPA00244; UER00313. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0033856; F:pyridoxine 5'-phosphate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00003; PNPsynthase; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_00279; PdxJ; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004569; PyrdxlP_synth_PdxJ. DR InterPro; IPR036130; Pyridoxine-5'_phos_synth. DR NCBIfam; TIGR00559; pdxJ; 1. DR NCBIfam; NF003625; PRK05265.1-3; 1. DR NCBIfam; NF003627; PRK05265.1-5; 1. DR PANTHER; PTHR30456; PYRIDOXINE 5'-PHOSPHATE SYNTHASE; 1. DR PANTHER; PTHR30456:SF0; PYRIDOXINE 5'-PHOSPHATE SYNTHASE; 1. DR Pfam; PF03740; PdxJ; 1. DR SUPFAM; SSF63892; Pyridoxine 5'-phosphate synthase; 1. PE 3: Inferred from homology; KW Cytoplasm; Pyridoxine biosynthesis; Transferase. FT CHAIN 1..249 FT /note="Pyridoxine 5'-phosphate synthase" FT /id="PRO_1000022411" FT ACT_SITE 43 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT ACT_SITE 70 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT ACT_SITE 190 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 7 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 9..10 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 18 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 45 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 50 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 100 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 191 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 212..213 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT SITE 151 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" SQ SEQUENCE 249 AA; 27077 MW; FF18984A5AB9E5C6 CRC64; MASLGVNIDH IANIREARRT VEPDPVPMAM LAELGGADGI TVHLREDRRH IQDRDVELLR QTVRSRLNLE MAATAEMVAI ALRVKPDMVT LVPEHRQEVT TEGGLDVVAQ LSELTGMVSQ LQTSGIPVSL FVDPVASQLR GCTDSGARWV ELHTGRYAEG SWNDQPHELA RLTEGTATAR AMGLRVNAGH GLTYQNVEPV AAIPGMEELN IGHTIVARAV VVGLQQAVRE MKALIQNPRR DPLFGQALG //