ID PDXH_ACIC1 Reviewed; 224 AA. AC A0LR32; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 89. 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=Acel_0116; OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B). OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae; OC Acidothermus. OX NCBI_TaxID=351607; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43068 / DSM 8971 / 11B; RX PubMed=19270083; DOI=10.1101/gr.084848.108; RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V., RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C., RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.; RT "Complete genome of the cellulolytic thermophile Acidothermus RT cellulolyticus 11B provides insights into its ecophysiological and RT evolutionary adaptations."; RL Genome Res. 19:1033-1043(2009). 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; CP000481; ABK51892.1; -; Genomic_DNA. DR RefSeq; WP_011718956.1; NC_008578.1. DR AlphaFoldDB; A0LR32; -. DR SMR; A0LR32; -. DR STRING; 351607.Acel_0116; -. DR KEGG; ace:Acel_0116; -. DR eggNOG; COG0259; Bacteria. DR HOGENOM; CLU_032263_2_2_11; -. DR InParanoid; A0LR32; -. DR OrthoDB; 9780392at2; -. DR UniPathway; UPA01068; UER00304. DR UniPathway; UPA01068; UER00305. DR Proteomes; UP000008221; 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..224 FT /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase" FT /id="PRO_0000292281" FT BINDING 69..74 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 74 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 83..84 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 89 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 90 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 112 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" 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 138 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 148..149 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 194 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 200..202 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" FT BINDING 204 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01629" SQ SEQUENCE 224 AA; 25428 MW; D50A98E36BA4A6B9 CRC64; MRHGTHTGSN PYAEAYVEVT AGGLAETDLA ADPIEQFRRW LADAIRYNLP EPTAMVVATA DADGRPSSRH VLLKSVDDGF VFFTNYRSRK GRDLSENPSA SLCFPWFAIG RQVVVLGTVT KVTREETEEY FASRPRDSQC GAWSSENQSS VVPSRAWLDE RYAEVAQRFA GVEHIPPPPF WGGFRVIPET VEFWQARPAR MHDRLRYRRT ADGERPWIIE RLSP //