ID PDXH_PSEA7 Reviewed; 215 AA. AC A6V9E9; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 90. 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=PSPA7_4331; OS Pseudomonas aeruginosa (strain PA7). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=381754; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PA7; RA Dodson R.J., Harkins D., Paulsen I.T.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000744; ABR84483.1; -; Genomic_DNA. DR RefSeq; WP_003153441.1; NC_009656.1. DR AlphaFoldDB; A6V9E9; -. DR SMR; A6V9E9; -. DR GeneID; 77222349; -. DR KEGG; pap:PSPA7_4331; -. DR HOGENOM; CLU_032263_2_2_6; -. DR UniPathway; UPA01068; UER00304. DR UniPathway; UPA01068; UER00305. DR Proteomes; UP000001582; 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..215 FT /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase" FT /id="PRO_1000069697" FT BINDING 9..12 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 64..69 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 69 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 79..80 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 86 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 108 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" 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 134 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 143..144 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 188 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 194..196 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 198 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" SQ SEQUENCE 215 AA; 24832 MW; AC19AA36A1186A92 CRC64; MTQSLADMRR EYTRDGLSEA NAPSDPFSLF RQWFDDAVKT ERLPVEPNAM TLATVDADGH PHCRILLLKG LDERGFTFFT NYESAKGRQL AANPRAAMTF FWPALERQVR IEGEIEKVTA QESDAYYQVR PLGSRLGAWA SPQSRVIADR AELERLLAET ERRFADQAPS CPEHWGGYRL LPQRIEFWQG RPSRLHDRLD YRHQDGVWAR ERLAP //