ID   PDXH_BACFN              Reviewed;         235 AA.
AC   Q5LFJ5;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase {ECO:0000255|HAMAP-Rule:MF_01629};
DE            EC=1.4.3.5 {ECO:0000255|HAMAP-Rule:MF_01629};
DE   AltName: Full=PNP/PMP oxidase {ECO:0000255|HAMAP-Rule:MF_01629};
DE            Short=PNPOx {ECO:0000255|HAMAP-Rule:MF_01629};
DE   AltName: Full=Pyridoxal 5'-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01629};
GN   Name=pdxH {ECO:0000255|HAMAP-Rule:MF_01629}; OrderedLocusNames=BF1385;
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidota; 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 /
RC   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 oxidation of either pyridoxine 5'-phosphate
CC       (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate
CC       (PLP). {ECO:0000255|HAMAP-Rule:MF_01629}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) +
CC         pyridoxal 5'-phosphate; Xref=Rhea:RHEA:15817, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58451, ChEBI:CHEBI:597326; EC=1.4.3.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01629};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + pyridoxine 5'-phosphate = H2O2 + pyridoxal 5'-phosphate;
CC         Xref=Rhea:RHEA:15149, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:58589, ChEBI:CHEBI:597326; EC=1.4.3.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01629};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01629};
CC       Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01629};
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC       5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01629}.
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC       5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01629}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01629}.
CC   -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01629}.
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DR   EMBL; CR626927; CAH07098.1; -; Genomic_DNA.
DR   RefSeq; WP_005786189.1; NZ_UFTH01000001.1.
DR   AlphaFoldDB; Q5LFJ5; -.
DR   SMR; Q5LFJ5; -.
DR   PaxDb; 272559-BF9343_1317; -.
DR   GeneID; 66329690; -.
DR   KEGG; bfs:BF9343_1317; -.
DR   eggNOG; COG0259; Bacteria.
DR   HOGENOM; CLU_032263_2_2_10; -.
DR   UniPathway; UPA01068; UER00304.
DR   UniPathway; UPA01068; UER00305.
DR   Proteomes; UP000006731; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004733; F:pyridoxamine phosphate oxidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01629; PdxH; 1.
DR   InterPro; IPR000659; Pyridox_Oxase.
DR   InterPro; IPR019740; Pyridox_Oxase_CS.
DR   InterPro; IPR011576; Pyridox_Oxase_put.
DR   InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   NCBIfam; TIGR00558; pdxH; 1.
DR   PANTHER; PTHR10851:SF0; PYRIDOXINE-5'-PHOSPHATE OXIDASE; 1.
DR   PANTHER; PTHR10851; PYRIDOXINE-5-PHOSPHATE OXIDASE; 1.
DR   Pfam; PF10590; PNP_phzG_C; 1.
DR   Pfam; PF01243; Putative_PNPOx; 1.
DR   PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1.
DR   SUPFAM; SSF50475; FMN-binding split barrel; 1.
DR   PROSITE; PS01064; PYRIDOX_OXIDASE; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; Oxidoreductase; Pyridoxine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..235
FT                   /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase"
FT                   /id="PRO_0000167682"
FT   BINDING         30..33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         83..88
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         98..99
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         104
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         105
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         127
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         162..163
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         207
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         213..215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         217
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
SQ   SEQUENCE   235 AA;  26673 MW;  6C6C85CC8E160374 CRC64;
     MSTDHVSTHP DSPLHGNGIG SEAINLAAIR QEYTKGGLKE GDLPDNPLSL FNRWLHEAID
     AQVDEPTAML VGTVSPEGQP STRTVLLKDL HDGKFIFYTN YESRKGTHLA KNPYISLSFV
     WHALERQVHI EGIASKVPAG ESDTYFRQRP YKSRIGARIS PQSRPLKSRM QLIRNFVAEA
     ARWVGREVER PAHWGGYAVT PHRIEFWQGR ANRLHDRFLY SLQPDGSWQK ERLAP
//