ID PDXJ_BRUSU Reviewed; 246 AA. AC Q8FZT6; G0KB68; DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 99. 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=BR1385, BS1330_I1379; OS Brucella suis biovar 1 (strain 1330). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=204722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=12271122; DOI=10.1073/pnas.192319099; RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E., RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.; RT "The Brucella suis genome reveals fundamental similarities between animal RT and plant pathogens and symbionts."; RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=22038969; DOI=10.1128/jb.06181-11; RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.; RT "Revised genome sequence of Brucella suis 1330."; RL J. Bacteriol. 193:6410-6410(2011). 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; AE014291; AAN30298.1; -; Genomic_DNA. DR EMBL; CP002997; AEM18714.1; -; Genomic_DNA. DR RefSeq; WP_004690972.1; NZ_KN046804.1. DR AlphaFoldDB; Q8FZT6; -. DR SMR; Q8FZT6; -. DR GeneID; 55591042; -. DR KEGG; bms:BR1385; -. DR KEGG; bsi:BS1330_I1379; -. DR PATRIC; fig|204722.21.peg.861; -. DR HOGENOM; CLU_074563_1_0_5; -. DR PhylomeDB; Q8FZT6; -. DR UniPathway; UPA00244; UER00313. DR Proteomes; UP000007104; 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 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 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..246 FT /note="Pyridoxine 5'-phosphate synthase" FT /id="PRO_0000190110" FT ACT_SITE 44 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT ACT_SITE 76 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT ACT_SITE 198 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 8 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 19 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 46 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 51 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 106 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 199 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 221..222 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT SITE 157 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" SQ SEQUENCE 246 AA; 26447 MW; 6E44F12BD0FC15CF CRC64; MPAKLSVNLN AIAMLRNRRD LPWPSVTGLG RAALAAGAAG LTVHPRPDQR HIRFSDLGDI RALIDDEYPQ AEFNIEGFPS EAFLDLVEKH EPEQVTLVPD DPMQATSDHG WDFMSKADFL APIVARLKGR GMRVSLFADP DSLGYERAKA IGADHVELYT GPYGATHDDP AAAARELDRL EKAARAATAL GLAVNAGHDL TVDNLPALVK RIPQLAEVSI GHGLTADALM YGIPVTVSRY ITALAG //