ID   PDXH_RHIWR              Reviewed;         200 AA.
AC   A5VFM5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   02-SEP-2026, 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};
GN   OrderedLocusNames=Swit_4754;
OS   Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC
OS   105917 / EY 4224 / RW1) (Sphingomonas wittichii).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Sphingomonadales; Rhizorhabdaceae; Rhizorhabdus.
OX   NCBI_TaxID=392499;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 /
RC   RW1;
RX   PubMed=20833805; DOI=10.1128/jb.01030-10;
RA   Miller T.R., Delcher A.L., Salzberg S.L., Saunders E., Detter J.C.,
RA   Halden R.U.;
RT   "Genome sequence of the dioxin-mineralizing bacterium Sphingomonas
RT   wittichii RW1.";
RL   J. Bacteriol. 192:6101-6102(2010).
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; CP000699; ABQ71091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5VFM5; -.
DR   SMR; A5VFM5; -.
DR   STRING; 392499.Swit_4754; -.
DR   PaxDb; 392499-Swit_4754; -.
DR   KEGG; swi:Swit_4754; -.
DR   eggNOG; COG0259; Bacteria.
DR   HOGENOM; CLU_032263_2_3_5; -.
DR   OrthoDB; 9780392at2; -.
DR   UniPathway; UPA01068; UER00304.
DR   UniPathway; UPA01068; UER00305.
DR   Proteomes; UP000001989; 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   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   CHAIN           1..200
FT                   /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase"
FT                   /id="PRO_0000335804"
FT   BINDING         49..54
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         64..65
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         70
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         71
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         93
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         128..129
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         173
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01629"
FT   BINDING         179..181
FT                   /ligand="substrate"
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"
SQ   SEQUENCE   200 AA;  22901 MW;  C6D144FF26E258D8 CRC64;
     MSEAQLTTEP TDPHSLFRSW FAEAKASEPN DPEAMAVATV GADGQPSVRM VLLKGHDARG
     FVFYTNYESR KATQLLETGR AALLFHWKSL RRQVRIEGPV SKVSPEEGDA YFATRHRDSQ
     IGAWASDQSR PLDSRATFEA RYEEMLRRFE GGPVPRPPHW SGFRVAPERI EFWQDRAHRL
     HERRLFTRSG DGWSEGLLYP
//