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PDXJ_BACFN
ID   PDXJ_BACFN              Reviewed;         237 AA.
AC   Q5L912;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=BF3740;
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
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; CR626927; CAH09420.1; -; Genomic_DNA.
DR   RefSeq; WP_005791132.1; NC_003228.3.
DR   AlphaFoldDB; Q5L912; -.
DR   SMR; Q5L912; -.
DR   STRING; 272559.BF9343_3639; -.
DR   EnsemblBacteria; CAH09420; CAH09420; BF9343_3639.
DR   GeneID; 66331427; -.
DR   KEGG; bfs:BF9343_3639; -.
DR   eggNOG; COG0854; Bacteria.
DR   HOGENOM; CLU_074563_1_0_10; -.
DR   OMA; SNAGWDT; -.
DR   OrthoDB; 1159993at2; -.
DR   UniPathway; UPA00244; UER00313.
DR   Proteomes; UP000006731; 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..237
FT                   /note="Pyridoxine 5'-phosphate synthase"
FT                   /id="PRO_0000231782"
FT   ACT_SITE        43
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   ACT_SITE        190
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         7
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         18
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         45
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         50
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         100
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         191
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   BINDING         213..214
FT                   /ligand="3-amino-2-oxopropyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57279"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
FT   SITE            151
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00279"
SQ   SEQUENCE   237 AA;  26275 MW;  6B505182B8B6C815 CRC64;
     MTKLSVNINK VATLRNARGG NVPNVVKVAL DCESFGADGI TVHPRPDERH IRRSDVYDLR
     PLLRTEFNIE GYPSPEFIDL VLKVKPHQVT LVPDDPSQIT SNSGWDTKVN FDFLTEVLDE
     FNGAGIRTSV FVAPDAEMIE YAAKAGADRV ELYTEPYATA YPKDPAAAVA PFVEAAKAAR
     RLGIGLNAGH DLSLLNLNYF YKNIPWLDEV SIGHALISDA LYLGLERTIQ EYKNCLR
 
 
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