ID PDXH_ACTP2 Reviewed; 209 AA. AC A3N3U7; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 27-MAR-2024, entry version 97. 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=APL_2009; OS Actinobacillus pleuropneumoniae serotype 5b (strain L20). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=416269; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L20; RX PubMed=18065534; DOI=10.1128/jb.01845-07; RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., RA Nash J.H.E.; RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20 RT (serotype 5b)."; RL J. Bacteriol. 190:1495-1496(2008). 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; CP000569; ABN75083.1; -; Genomic_DNA. DR RefSeq; WP_005606603.1; NC_009053.1. DR AlphaFoldDB; A3N3U7; -. DR SMR; A3N3U7; -. DR STRING; 416269.APL_2009; -. DR EnsemblBacteria; ABN75083; ABN75083; APL_2009. DR KEGG; apl:APL_2009; -. DR eggNOG; COG0259; Bacteria. DR HOGENOM; CLU_032263_2_2_6; -. DR UniPathway; UPA01068; UER00304. DR UniPathway; UPA01068; UER00305. DR Proteomes; UP000001432; 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; KW Reference proteome. FT CHAIN 1..209 FT /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase" FT /id="PRO_0000292284" FT BINDING 7..10 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 59..64 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 64 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 74..75 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 80 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 121 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 125 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 129 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 138..139 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 182 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 188..190 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 192 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" SQ SEQUENCE 209 AA; 23957 MW; F8A62FA6F1AE834C CRC64; MDLHNIREDY SKQELSQANC HADPIQQFEQ WLEEAITAKA NEPTAMNVAT VLDGKPTSRI VLLKEVNPNG FVFFTNYQSR KGQAIEQNPY VALTFFWAEL ERSVRIEGRI EKISAEQSDN YFASRPYTSR VGAWASNQSQ VLSSKSELVA KAALIAAKHP LHVPRPPHWG GYIVLPERIE FWQGRPSRLH DRICYRLVEG AWHKERLSP //