ID PDXJ_COXBU Reviewed; 240 AA. AC Q83BL1; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 106. 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=CBU_1494; OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae; OC Coxiella. OX NCBI_TaxID=227377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSA 493 / Nine Mile phase I; RX PubMed=12704232; DOI=10.1073/pnas.0931379100; RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., RA Fraser C.M., Heidelberg J.F.; RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003). 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 -!- SEQUENCE CAUTION: CC Sequence=AAO90991.2; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AE016828; AAO90991.2; ALT_INIT; Genomic_DNA. DR RefSeq; NP_820477.2; NC_002971.3. DR AlphaFoldDB; Q83BL1; -. DR SMR; Q83BL1; -. DR STRING; 227377.CBU_1494; -. DR EnsemblBacteria; AAO90991; AAO90991; CBU_1494. DR GeneID; 1209404; -. DR KEGG; cbu:CBU_1494; -. DR PATRIC; fig|227377.7.peg.1496; -. DR eggNOG; COG0854; Bacteria. DR HOGENOM; CLU_074563_0_0_6; -. DR OrthoDB; 9806590at2; -. DR UniPathway; UPA00244; UER00313. DR Proteomes; UP000002671; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0033856; F:pyridoxine 5'-phosphate synthase activity; IBA:GO_Central. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IBA:GO_Central. 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; Reference proteome; Transferase. FT CHAIN 1..240 FT /note="Pyridoxine 5'-phosphate synthase" FT /id="PRO_0000231800" 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 191 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 192 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 213..214 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 240 AA; 26013 MW; E15A78207718D673 CRC64; MVRLGVNIDH IATLRQARGV DYPDPVEAAM MAIEAGADGI TLHLREDRRH IQDDDVRNLK RKLTVPMNLE MATAEDIIQF AEEIKPEHCC LVPEKREELT TEGGLDVAGQ QNTLKKVCAR LAKVGIEVSL FIDPEEKQID AAKAAGAPVI EIHTGHYANA KTDHEHNQQL KRIADAAAYA DSLGLTVNAG HGLTIHNVQS IAAIPVINEL NIGHSIISRG VLIGLAEAVK EMKTLIAGAQ //