ID PDXH_PSEE4 Reviewed; 215 AA. AC Q1IDT9; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 1. DT 27-MAR-2024, entry version 101. 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=PSEEN1277; OS Pseudomonas entomophila (strain L48). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=384676; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L48; RX PubMed=16699499; DOI=10.1038/nbt1212; RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C., RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P., RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.; RT "Complete genome sequence of the entomopathogenic and metabolically RT versatile soil bacterium Pseudomonas entomophila."; RL Nat. Biotechnol. 24:673-679(2006). 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; CT573326; CAK14170.1; -; Genomic_DNA. DR RefSeq; WP_011532586.1; NC_008027.1. DR AlphaFoldDB; Q1IDT9; -. DR SMR; Q1IDT9; -. DR STRING; 384676.PSEEN1277; -. DR GeneID; 32804554; -. DR KEGG; pen:PSEEN1277; -. DR eggNOG; COG0259; Bacteria. DR HOGENOM; CLU_032263_2_2_6; -. DR OrthoDB; 9780392at2; -. DR UniPathway; UPA01068; UER00304. DR UniPathway; UPA01068; UER00305. DR Proteomes; UP000000658; 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_0000292317" 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; 24614 MW; 22BC3A1C2DB9516A CRC64; MTQSLADMRR DYTRDGLAEA QAPGEPFALF HHWFADAVKT EQLPVEANAM TLATVDADGR PHCRVLLLKA LDGRGFTFFT NYESAKGQHI AANPFAAMTF FWPALERQVR IEGRVEKVTA KESDDYYQVR PLGSRLGAWA SPQSRVIADR EELEGLVKAT EARFSDTQPH CPEHWGGYRL LPERIEFWQG RASRLHDRLN YRLVDGQWQR ERLAP //