ID PDXH_MICAN Reviewed; 214 AA. AC B0JI39; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAR-2008, 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=MAE_57790; OS Microcystis aeruginosa (strain NIES-843 / IAM M-2473). OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae; OC Chroococcales; Microcystaceae; Microcystis. OX NCBI_TaxID=449447; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIES-843 / IAM M-247; RX PubMed=18192279; DOI=10.1093/dnares/dsm026; RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M., RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A., RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., RA Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.; RT "Complete genomic structure of the bloom-forming toxic cyanobacterium RT Microcystis aeruginosa NIES-843."; RL DNA Res. 14:247-256(2007). 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; AP009552; BAG05601.1; -; Genomic_DNA. DR RefSeq; WP_012267993.1; NC_010296.1. DR AlphaFoldDB; B0JI39; -. DR SMR; B0JI39; -. DR STRING; 449447.MAE_57790; -. DR PaxDb; 449447-MAE_57790; -. DR EnsemblBacteria; BAG05601; BAG05601; MAE_57790. DR GeneID; 66705468; -. DR KEGG; mar:MAE_57790; -. DR eggNOG; COG0259; Bacteria. DR HOGENOM; CLU_032263_2_2_3; -. DR BioCyc; MAER449447:MAE_RS25205-MONOMER; -. DR UniPathway; UPA01068; UER00304. DR UniPathway; UPA01068; UER00305. DR Proteomes; UP000001510; 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..214 FT /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase" FT /id="PRO_1000088114" FT BINDING 9..12 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 62..67 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 67 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 77..78 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 84 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 106 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 124 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 128 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 132 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 141..142 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 186 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 192..194 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 196 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" SQ SEQUENCE 214 AA; 24968 MW; C98893AC2E62B3A4 CRC64; MDISIADLRL DYNLEELLES ETSADPFIVF KQWLERAVSS GRLEPNAMTL ATISPEGKPR ARMVLLKDFD PRGFVLFTNY HSAKGQELIA NPNAALVFWW GELQRQIRIE GTVEKISEEE SDNYFFVRPW ESRLGAWASN QSEVISGRDI LEKRLTELKE EYAGREVPRP PHWGGFRLIP SLIEFWQGRP SRLHDRLCYY RQEDGSWQRQ RLAP //