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Database: UniProt
Entry: F6AA55_PSEF1
LinkDB: F6AA55_PSEF1
Original site: F6AA55_PSEF1 
ID   F6AA55_PSEF1            Unreviewed;       247 AA.
AC   F6AA55;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 56.
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   OrderedLocusNames=Psefu_3232 {ECO:0000313|EMBL:AEF23194.1};
OS   Pseudomonas fulva (strain 12-X).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF23194.1, ECO:0000313|Proteomes:UP000000686};
RN   [1] {ECO:0000313|EMBL:AEF23194.1, ECO:0000313|Proteomes:UP000000686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA   Woyke T.;
RT   "Complete sequence of Pseudomonas fulva 12-X.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002727; AEF23194.1; -; Genomic_DNA.
DR   RefSeq; WP_013792321.1; NC_015556.1.
DR   AlphaFoldDB; F6AA55; -.
DR   STRING; 743720.Psefu_3232; -.
DR   KEGG; pfv:Psefu_3232; -.
DR   eggNOG; COG0854; Bacteria.
DR   HOGENOM; CLU_074563_0_0_6; -.
DR   OMA; SNAGWDT; -.
DR   OrthoDB; 9806590at2; -.
DR   UniPathway; UPA00244; UER00313.
DR   Proteomes; UP000000686; 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}; Reference proteome {ECO:0000313|Proteomes:UP000000686};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00279, ECO:0000313|EMBL:AEF23194.1}.
FT   ACT_SITE        48
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   ACT_SITE        75
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   ACT_SITE        196
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         12
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         14..15
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         23
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
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         55
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         105
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         197
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         218..219
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   SITE            156
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
SQ   SEQUENCE   247 AA;  26947 MW;  BDF98BDEDBB8E939 CRC64;
     MTEANRVLLG VNIDHVATLR QARGTRYPDP VKAALDAEEA GADGITVHLR EDRRHIQERD
     VRVLKEVMQT RMNFEMGVTD FMLDFAEEIC PEHVCLVPET RQELTTEGGL DVAGQEARIA
     AAVKRLAAVG SEVSLFIDAD PRQIEASKRV GAPAIELHTG RYADAHTPQE AAAELQRIRE
     GVALGVSLGL IVNAGHGLHY HNVEPVAAIP GINELNIGHA LVSHALFVGF KEAVREMKQL
     IQEAAPR
//
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