ID C7BRJ9_PHOAA Unreviewed; 243 AA.
AC C7BRJ9;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
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 ECO:0000313|EMBL:CAQ83400.1};
GN OrderedLocusNames=PAU_01308 {ECO:0000313|EMBL:CAQ83400.1};
OS Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77)
OS (Xenorhabdus luminescens (strain 2)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=553480 {ECO:0000313|EMBL:CAQ83400.1, ECO:0000313|Proteomes:UP000002747};
RN [1] {ECO:0000313|EMBL:CAQ83400.1, ECO:0000313|Proteomes:UP000002747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43949 / 3105-77 {ECO:0000313|Proteomes:UP000002747};
RX PubMed=19583835; DOI=10.1186/1471-2164-10-302;
RA Wilkinson P., Waterfield N.R., Crossman L., Corton C.,
RA Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L.,
RA Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C.,
RA Harris D., Thompson N.R., Quail M., Parkhill J., ffrench-Constant R.H.;
RT "Comparative genomics of the emerging human pathogen Photorhabdus
RT asymbiotica with the insect pathogen Photorhabdus luminescens.";
RL BMC Genomics 10:302-302(2009).
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}.
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DR EMBL; FM162591; CAQ83400.1; -; Genomic_DNA.
DR AlphaFoldDB; C7BRJ9; -.
DR STRING; 291112.PAU_01308; -.
DR KEGG; pay:PAU_01308; -.
DR eggNOG; COG0854; Bacteria.
DR UniPathway; UPA00244; UER00313.
DR Proteomes; UP000002747; 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 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:CAQ83400.1}.
FT ACT_SITE 45
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT ACT_SITE 72
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT ACT_SITE 193
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 9
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 11..12
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 20
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 47
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 52
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 102
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 194
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT BINDING 215..216
FT /ligand="3-amino-2-oxopropyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57279"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT SITE 153
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
SQ SEQUENCE 243 AA; 26627 MW; E2104CE50BDDB958 CRC64;
MAEVLLGVNI DHIATVRNAR GTNYPDPVQA AFVAEQAGAD GITIHLREDR RHITDRDVEL
LSQTIQTRMN LEMAVTDEMV DIACRIKPEF CCLVPEKRQE VTTEGGLDVV GQKDKVMAAV
KRLSEAGILV SLFIDADHQQ IDAAREVGAP FIEIHTGAYA DAENEIEQEK EFQRIKKAAT
YAVGIGLTVN AGHGLTYHNV QRIAALPEIY ELNIGHAIIG RAVFSGLTAA VADMKTQMRK
VRG
//
