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PDXJ_BLOFL
ID   PDXJ_BLOFL              Reviewed;         247 AA.
AC   Q7VRR1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 93.
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}; OrderedLocusNames=Bfl539;
OS   Blochmannia floridanus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=203907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA   Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA   Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA   van Ham R.C.H.J., Gross R., Moya A.;
RT   "The genome sequence of Blochmannia floridanus: comparative analysis of
RT   reduced genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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}.
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DR   EMBL; BX248583; CAD83225.1; -; Genomic_DNA.
DR   RefSeq; WP_011126801.1; NC_005061.1.
DR   AlphaFoldDB; Q7VRR1; -.
DR   SMR; Q7VRR1; -.
DR   STRING; 203907.Bfl539; -.
DR   EnsemblBacteria; CAD83225; CAD83225; Bfl539.
DR   KEGG; bfl:Bfl539; -.
DR   eggNOG; COG0854; Bacteria.
DR   HOGENOM; CLU_074563_0_0_6; -.
DR   OMA; SNAGWDT; -.
DR   OrthoDB; 1159993at2; -.
DR   UniPathway; UPA00244; UER00313.
DR   Proteomes; UP000002192; 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; -; 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   PANTHER; PTHR30456; PTHR30456; 1.
DR   Pfam; PF03740; PdxJ; 1.
DR   SUPFAM; SSF63892; SSF63892; 1.
DR   TIGRFAMs; TIGR00559; pdxJ; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Pyridoxine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..247
FT                   /note="Pyridoxine 5'-phosphate synthase"
FT                   /id="PRO_0000231785"
FT   ACT_SITE        45
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   ACT_SITE        72
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   ACT_SITE        193
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         9
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         20
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         47
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         52
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         194
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         215..216
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   SITE            153
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
SQ   SEQUENCE   247 AA;  28219 MW;  A5168497D9C83FC2 CRC64;
     MSNLLLALNI DHIATVRNAR GTQYPDPVYA AYIAEQSGID GITVHLREDR RHITDRDVKL
     LREIVQTTMN LEMAATDEMV MIACQLKPHY CCLVPERRRE LTTEGGLDLI YQIDKMQNIV
     LKLSDAGIRV SLFIDPDIEQ IDASYKIGVR CIELNTGKYA ESKNKEDRIL EYRRIEKSIK
     HALSYGLMIN AGHGLNYDNV KFIAMLSQIR ELNIGHAIVS RAVFCGLPKA IKDMKELLKE
     FRKKDDQ
 
 
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