ID PDXH_BRASO Reviewed; 216 AA. AC A4YQ21; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 16-JUN-2009, entry version 18. DE RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase; DE EC=1.4.3.5; DE AltName: Full=PNP/PMP oxidase; DE Short=PNPOx; DE AltName: Full=Pyridoxal 5'-phosphate synthase; GN Name=pdxH; OrderedLocusNames=BRADO2146; OS Bradyrhizobium sp. (strain ORS278). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=114615; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17540897; DOI=10.1126/science.1139548; RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C., RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., RA Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L., RA Chang W.-S., Saunders E., Bruce D., Richardson P., Normand P., RA Dreyfus B., Pignol D., Stacey G., Emerich D., Vermeglio A., RA Medigue C., Sadowsky M.; RT "Legumes symbioses: absence of nod genes in photosynthetic RT bradyrhizobia."; RL Science 316:1307-1312(2007). CC -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'- CC phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal CC 5'-phosphate (PLP) (By similarity). CC -!- CATALYTIC ACTIVITY: Pyridoxamine 5'-phosphate + H(2)O + O(2) = CC pyridoxal 5'-phosphate + NH(3) + H(2)O(2). CC -!- CATALYTIC ACTIVITY: Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'- CC phosphate + H(2)O(2). CC -!- COFACTOR: Binds 1 FMN per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; B6 vitamer interconversion; CC pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. CC -!- PATHWAY: Cofactor biosynthesis; B6 vitamer interconversion; CC pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU234118; CAL75997.1; -; Genomic_DNA. DR RefSeq; YP_001204234.1; -. DR GeneID; 5120050; -. DR GenomeReviews; CU234118_GR; BRADO2146. DR KEGG; bra:BRADO2146; -. DR OMA; A4YQ21; EPFALFA. DR GO; GO:0010181; F:FMN binding; IEA:HAMAP. DR GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW. DR HAMAP; MF_01629; -; 1. DR InterPro; IPR011576; PNPOx_rel_FMN_bd_core. DR InterPro; IPR000659; Pyridoxamine_oxidase. DR InterPro; IPR019740; Pyridoxamine_oxidase_CS. DR InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C. DR InterPro; IPR012349; Split_barrel_FMN_bd. DR Gene3D; G3DSA:2.30.110.10; PNPOx_FMN_bd; 1. DR PANTHER; PTHR10851; Pyridox_oxidase; 1. DR Pfam; PF10590; PNPOx_C; 1. DR Pfam; PF01243; Pyridox_oxidase; 1. DR ProDom; PD006312; Pyridox_oxidase; 1. DR TIGRFAMs; TIGR00558; pdxH; 1. DR PROSITE; PS01064; PYRIDOX_OXIDASE; 1. PE 3: Inferred from homology; KW Complete proteome; Flavoprotein; FMN; Oxidoreductase; KW Pyridoxine biosynthesis. FT CHAIN 1 216 Pyridoxine/pyridoxamine 5'-phosphate FT oxidase. FT /FTId=PRO_1000069682. FT NP_BIND 78 79 FMN (By similarity). FT NP_BIND 142 143 FMN (By similarity). FT REGION 193 195 Substrate binding (By similarity). FT BINDING 63 63 FMN (By similarity). FT BINDING 66 66 FMN; via amide nitrogen (By similarity). FT BINDING 68 68 Substrate (By similarity). FT BINDING 85 85 FMN (By similarity). FT BINDING 125 125 Substrate (By similarity). FT BINDING 129 129 Substrate (By similarity). SQ SEQUENCE 216 AA; 24373 MW; 4108D54342535456 CRC64; MTDPTSIKHQ TTLTSGTSAD FTQAGEPFAL FAEWFAEASK SEPNDPNAMA LSTVDADGLP DVRMVLMKGY DADGFVFYSH KASQKGQELA ANPKAALLFH WKSLRRQVRI RGLVTPVTDA EADAYFATRP KQAQLGAWAS KQSQPLESRF AFEQAIAKVA TQYIIGEVPR PPGWSGWRIT PVRMEFWHDR PFRLHDRIEF RREAAGQPWT KVRMYP //