ID PDXJ_LEPBP Reviewed; 260 AA. AC B0SJ25; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 80. 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=LEPBI_I0476; OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris). OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae; OC Leptospira. OX NCBI_TaxID=456481; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Patoc 1 / ATCC 23582 / Paris; RX PubMed=18270594; DOI=10.1371/journal.pone.0001607; RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.; RT "Genome sequence of the saprophyte Leptospira biflexa provides insights RT into the evolution of Leptospira and the pathogenesis of leptospirosis."; RL PLoS ONE 3:E1607-E1607(2008). 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=1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate CC = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate; 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; CP000786; ABZ96614.1; -; Genomic_DNA. DR RefSeq; WP_012387501.1; NC_010602.1. DR AlphaFoldDB; B0SJ25; -. DR SMR; B0SJ25; -. DR STRING; 456481.LEPBI_I0476; -. DR KEGG; lbi:LEPBI_I0476; -. DR HOGENOM; CLU_074563_1_0_12; -. DR OrthoDB; 9806590at2; -. DR BioCyc; LBIF456481:LEPBI_RS02330-MONOMER; -. DR UniPathway; UPA00244; UER00313. DR Proteomes; UP000001847; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 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 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; Reference proteome; Transferase. FT CHAIN 1..260 FT /note="Pyridoxine 5'-phosphate synthase" FT /id="PRO_1000114815" FT ACT_SITE 43 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT ACT_SITE 83 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT ACT_SITE 208 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 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 113 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 209 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 230..231 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT SITE 166 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" SQ SEQUENCE 260 AA; 29082 MW; F865749A1E31FBD6 CRC64; MTQLSVNVNK IATLRNSRGG SLPSVLKLSE LILDSGAHGI TVHPRSDERH ITKQDVFELQ EFLRTYNEKI TKLGISKKEY NIEGEPSERF LDLVLKAKPD QATLVPVKPG EITSDHGFQF ADQKTFSTLK PIVEAIRKEG IRVSLFMETD FTFYDQVVAL GAERIELYTG PFAHAFDLSE EKGKEIFTDY QRAAIEANKL GLAVNAGHDL DTNNLRVFAK LPYLKEVSIG HRLMAQSLVD GLETTVKSYL KVLSLGNETE //