ID PDXJ_HELPH Reviewed; 262 AA. AC Q1CR25; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 94. 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=HPAG1_1530; OS Helicobacter pylori (strain HPAG1). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=357544; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HPAG1; RX PubMed=16788065; DOI=10.1073/pnas.0603784103; RA Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A., RA Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G., RA Gordon J.I.; RT "The complete genome sequence of a chronic atrophic gastritis Helicobacter RT pylori strain: evolution during disease progression."; RL Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006). 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; CP000241; ABF85597.1; -; Genomic_DNA. DR RefSeq; WP_001210844.1; NC_008086.1. DR AlphaFoldDB; Q1CR25; -. DR SMR; Q1CR25; -. DR KEGG; hpa:HPAG1_1530; -. DR HOGENOM; CLU_074563_0_0_7; -. DR UniPathway; UPA00244; UER00313. DR Proteomes; UP000008835; Chromosome. 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; Transferase. FT CHAIN 1..262 FT /note="Pyridoxine 5'-phosphate synthase" FT /id="PRO_1000022375" 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 215 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 6 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 8..9 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 17 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 102 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 216 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00279" FT BINDING 237..238 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 262 AA; 29663 MW; CFC43A73505EC354 CRC64; MRFGLNIDHI VTLREIRKTY EPEILEALFI AKNTHKVDLI TIHLREDKRH IQNEDVLRLL EISPLPINIE CSINVAITDF LCSLKNKPSK VTIVPENRNE VTTEGGLDCS LKGLGEVIRA YHNKGIEVSL FVDPLKDALH FAKEHQVKQV EFHTGVYANL HNALYSNANN QIHAISALKD KCPKELKEEL HNAFLQLRRM SKEAFFMGIV VCAGHGLNYT NVKELLKIPS LRELNIGHSV VSKAVLVGLE KAILEMAQLI KR //