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Entry: A0A0N7KBE5_9GAMM
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ID   A0A0N7KBE5_9GAMM        Unreviewed;       241 AA.
AC   A0A0N7KBE5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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:BAS67791.1};
GN   ORFNames=BSEPE_0798 {ECO:0000313|EMBL:BAS67791.1};
OS   endosymbiont of Bathymodiolus septemdierum str. Myojin knoll.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1303921 {ECO:0000313|EMBL:BAS67791.1, ECO:0000313|Proteomes:UP000067399};
RN   [1] {ECO:0000313|EMBL:BAS67791.1, ECO:0000313|Proteomes:UP000067399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Myojin Knoll {ECO:0000313|EMBL:BAS67791.1,
RC   ECO:0000313|Proteomes:UP000067399};
RA   Fujiwara Y., Takai K., Uematsu K., Tsuchida S., Hunt J.C., Hashimoto J.;
RT   "Phylogenetic characterization of endosymbionts in three hydrothermal vent
RT   mussels: influence on host distributions.";
RL   Mar. Ecol. Prog. Ser. 208:147-155(2000).
RN   [2] {ECO:0000313|EMBL:BAS67791.1, ECO:0000313|Proteomes:UP000067399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Myojin Knoll {ECO:0000313|EMBL:BAS67791.1,
RC   ECO:0000313|Proteomes:UP000067399};
RX   PubMed=26418631; DOI=10.1038/ismej.2015.176;
RA   Ikuta T., Takaki Y., Nagai Y., Shimamura S., Tsuda M., Kawagucci S.,
RA   Aoki Y., Inoue K., Teruya M., Satou K., Teruya K., Shimoji M., Tamotsu H.,
RA   Hirano T., Maruyama T., Yoshida T.;
RT   "Heterogeneous composition of key metabolic gene clusters in a vent mussel
RT   symbiont population.";
RL   ISME J. 10:990-1001(2016).
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; AP013042; BAS67791.1; -; Genomic_DNA.
DR   RefSeq; WP_066044385.1; NZ_AP013042.1.
DR   AlphaFoldDB; A0A0N7KBE5; -.
DR   STRING; 1303921.BSEPE_0798; -.
DR   KEGG; ebh:BSEPE_0798; -.
DR   OrthoDB; 9806590at2; -.
DR   UniPathway; UPA00244; UER00313.
DR   Proteomes; UP000067399; 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:UP000067399};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00279, ECO:0000313|EMBL:BAS67791.1}.
FT   ACT_SITE        44
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   ACT_SITE        71
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   ACT_SITE        191
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         8
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         10..11
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         19
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         46
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         51
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         101
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
FT   BINDING         192
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            152
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00279"
SQ   SEQUENCE   241 AA;  26419 MW;  A1FADA1541071AAA CRC64;
     MSIYLGVNID HIATIRQARG TNYPSPVEGA LLCERSGADS ITLHLREDRR HIQDYDVEIL
     REKLTTKMNL EMATTDEMIA IASKIKPEDC CLVPEKREEL TTEGGLDVAG QIPRMTDVCA
     QLKNANIIVS LFIDAQKNQI DAAKECGAPV IELHTGHYAD TMGVEKVAEF ERIKTMATYA
     HSIGLQVNAG HGLTMENTTE IAKLPEIKEL NIGHAIIARA IFIGLAAATQ EMKDLIIGAR
     A
//
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