AC   MF_00279;
DC   Protein; auto
TR   HAMAP; MF_00279; -; 1; level=0
XX
Names: PdxJ
XX
ID   PDXJ
DE   RecName: Full=Pyridoxine 5'-phosphate synthase;
DE            Short=PNP synthase;
DE            EC=2.6.99.2;
GN   Name=pdxJ;
XX
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   -!- 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;
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the PNP synthase family.
XX
DR   Pfam; PF03740; PdxJ; 1; trigger=no
DR   NCBIfam; TIGR00559; PdxJ; 1; trigger=no
XX
KW   Cytoplasm
KW   Pyridoxine biosynthesis
KW   Transferase
XX
GO   GO:0016769; F:transferase activity, transferring nitrogenous groups
GO   GO:0008615; P:pyridoxine biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: PDXJ_ECOLI (P0A794)
FT   BINDING         11..12
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT   Optional; Condition: D-H
FT   BINDING         215..216
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT   Condition: G-[HQFY]
FT   ACT_SITE        45
FT                   /note="Proton acceptor"
FT   Condition: H
FT   ACT_SITE        72
FT                   /note="Proton acceptor"
FT   Condition: E
FT   ACT_SITE        193
FT                   /note="Proton donor"
FT   Condition: H
FT   BINDING         9
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT   Condition: N
FT   BINDING         20
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT   Condition: R
FT   BINDING         47
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT   Condition: R
FT   BINDING         52
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT   Condition: H
FT   BINDING         102
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT   Condition: T
FT   BINDING         194
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT   Optional; Condition: [GASD]
FT   SITE            153
FT                   /note="Transition state stabilizer"
FT   Condition: E
XX
Size: 232-267;
Related: None;
Template: P0A794;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.31 2023/06/01
//