ID   PDXH_SHIFL              Reviewed;         218 AA.
AC   P0AFI8; P28225;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 130.
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};
GN   OrderedLocusNames=SF1663, S1795;
OS   Shigella flexneri.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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=pyridoxamine 5'-phosphate + O2 + H2O = pyridoxal 5'-phosphate
CC         + H2O2 + NH4(+); 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=pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2;
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; AE005674; AAN43245.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17131.1; -; Genomic_DNA.
DR   RefSeq; NP_707538.1; NC_004337.2.
DR   RefSeq; WP_001282319.1; NZ_AP040250.1.
DR   AlphaFoldDB; P0AFI8; -.
DR   SMR; P0AFI8; -.
DR   STRING; 198214.SF1663; -.
DR   PaxDb; 198214-SF1663; -.
DR   GeneID; 1024832; -.
DR   GeneID; 75171699; -.
DR   KEGG; sfl:SF1663; -.
DR   KEGG; sfx:S1795; -.
DR   PATRIC; fig|198214.7.peg.1959; -.
DR   HOGENOM; CLU_032263_2_2_6; -.
DR   UniPathway; UPA01068; UER00304.
DR   UniPathway; UPA01068; UER00305.
DR   Proteomes; UP000001006; 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:InterPro.
DR   FunFam; 2.30.110.10:FF:000001; Pyridoxine/pyridoxamine 5'-phosphate oxidase; 1.
DR   Gene3D; 2.30.110.10; Electron Transport, Fmn-binding Protein, Chain A; 1.
DR   HAMAP; MF_01629; PdxH; 1.
DR   InterPro; IPR000659; Pyridox_Oxase.
DR   InterPro; IPR019740; Pyridox_Oxase_CS.
DR   InterPro; IPR011576; Pyridox_Oxase_N.
DR   InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   NCBIfam; TIGR00558; pdxH; 1.
DR   NCBIfam; NF004231; PRK05679.1; 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; PNPOx_N; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..218
FT                   /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase"
FT                   /id="PRO_0000167757"
FT   BINDING         14..17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         67..72
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         82..83
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         88
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         89
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         111
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         146..147
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         191
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         197..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         201
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
SQ   SEQUENCE   218 AA;  25545 MW;  8B47CEEEA6CEF5F9 CRC64;
     MSDNDELQQI AHLRREYTKG GLRRRDLPAD PLTLFERWLS QACEAKLADP TAMVVATVDE
     HGQPYQRIVL LKHYDEKGMV FYTNLGSRKA HQIENNPRVS LLFPWHTLER QVMVIGKAER
     LSTLEVMKYF HSRPRDSQIG AWVSKQSSRI SARGILESKF LELKQKFQQG EVPLPSFWGG
     FRVSLEQIEF WQGGEHRLHD RFLYQRENDA WKIDRLAP
//