ID A0A6G1ZCW8_9BACT Unreviewed; 239 AA. AC A0A6G1ZCW8; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 24-JAN-2024, entry version 10. DE RecName: Full=Pyridoxine 5'-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00279}; DE Short=PNP synthase {ECO:0000256|HAMAP-Rule:MF_00279}; DE EC=2.6.99.2 {ECO:0000256|HAMAP-Rule:MF_00279}; GN Name=pdxJ {ECO:0000256|HAMAP-Rule:MF_00279}; GN ORFNames=GKE01_09600 {ECO:0000313|EMBL:MRY11720.1}; OS Parabacteroides goldsteinii. OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; OC Parabacteroides. OX NCBI_TaxID=328812 {ECO:0000313|EMBL:MRY11720.1}; RN [1] {ECO:0000313|EMBL:MRY11720.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BIOML-A4 {ECO:0000313|EMBL:MRY11720.1}; RX PubMed=31477907; DOI=.1038/s41591-019-0559-3; RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X., RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D., RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J., RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A., RA Xavier R.J., Alm E.J.; RT "A library of human gut bacterial isolates paired with longitudinal RT multiomics data enables mechanistic microbiome research."; RL Nat. Med. 25:1442-1452(2019). 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00279}. CC -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000256|HAMAP- CC Rule:MF_00279}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00279}. CC -!- SIMILARITY: Belongs to the PNP synthase family. {ECO:0000256|HAMAP- CC Rule:MF_00279}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00279}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MRY11720.1}. 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; WKLP01000012; MRY11720.1; -; Genomic_DNA. DR RefSeq; WP_007658772.1; NZ_WKLS01000015.1. DR AlphaFoldDB; A0A6G1ZCW8; -. DR UniPathway; UPA00244; UER00313. 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00279}; KW Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096, ECO:0000256|HAMAP- KW Rule:MF_00279}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00279, ECO:0000313|EMBL:MRY11720.1}. FT ACT_SITE 43 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279" FT ACT_SITE 70 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279" FT ACT_SITE 190 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279" FT BINDING 7 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279" FT BINDING 18 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279" FT BINDING 45 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279" FT BINDING 50 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279" FT BINDING 100 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279" FT BINDING 191 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279" FT BINDING 213..214 FT /ligand="3-amino-2-oxopropyl phosphate" FT /ligand_id="ChEBI:CHEBI:57279" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279" FT SITE 151 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279" SQ SEQUENCE 239 AA; 26302 MW; 5BCBFCC69D44C297 CRC64; MTNLSVNINK VATIRNARGG NMPDILKVAQ DCENFGAQGI TVHPRPDERH IKYSDVYGLK PLIRTEFNIE GYPCNNFIDL VLKVKPTQVT LVPDAPDAIT SNAGWDVKTH FDQLSELVDT FTAQGIRTSI FVGTDLANIE LAAKTGTDRI ELYTEPYATN YPANKEEAVA PFVAAAQLAK NLGMGVNAGH DLSLENLAWF SQNIPWLEEV SIGHALICDA LYHGLQETIS LYKACLQQK //