ID   PDXH_NEIMA              Reviewed;         210 AA.
AC   Q9JTZ1; A1ISG1;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 123.
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=NMA1572;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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; AL157959; CAM08717.1; -; Genomic_DNA.
DR   PIR; G81849; G81849.
DR   RefSeq; WP_002219133.1; NC_003116.1.
DR   AlphaFoldDB; Q9JTZ1; -.
DR   SMR; Q9JTZ1; -.
DR   EnsemblBacteria; CAM08717; CAM08717; NMA1572.
DR   GeneID; 83616466; -.
DR   KEGG; nma:NMA1572; -.
DR   HOGENOM; CLU_032263_2_2_4; -.
DR   UniPathway; UPA01068; UER00304.
DR   UniPathway; UPA01068; UER00305.
DR   Proteomes; UP000000626; 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.
FT   CHAIN           1..210
FT                   /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase"
FT                   /id="PRO_0000167726"
FT   BINDING         7..10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         60..65
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         75..76
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         81
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         82
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         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         139..140
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         183
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         189..191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         193
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
SQ   SEQUENCE   210 AA;  24201 MW;  6FA480903939ED5C CRC64;
     MDLHNIREDY SKRELSEGDC ADNPIEQFER WLDEAVRAQV NEPTAVNVAA VDGRGRPNSR
     MVLLKEVNSE GFVFFTNYHS RKGRSLDAHP FAAMTFFWPE LERQVRVEGR VERLAEKLSD
     EYFESRPYQS RLGAWASAQS EVIPNKAVLV AKAAAVGLKH PLHVPRPPHW GGYIVIPDLI
     EFWQGRPSRL HDRIQYRLLD GGWIRERLSP
//