ID   PDXH_BRUO2              Reviewed;         208 AA.
AC   A5VNZ1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   16-JUN-2009, entry version 17.
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=BOV_0424;
OS   Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=444178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Paulsen I.;
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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.
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DR   EMBL; CP000708; ABQ60142.1; -; Genomic_DNA.
DR   RefSeq; YP_001258438.1; -.
DR   GeneID; 5201318; -.
DR   GenomeReviews; CP000708_GR; BOV_0424.
DR   KEGG; bov:BOV_0424; -.
DR   TIGR; BOV_0424; -.
DR   OMA; A5VNZ1; 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    208       Pyridoxine/pyridoxamine 5'-phosphate
FT                                oxidase.
FT                                /FTId=PRO_1000069683.
FT   NP_BIND      70     71       FMN (By similarity).
FT   NP_BIND     134    135       FMN (By similarity).
FT   REGION      185    187       Substrate binding (By similarity).
FT   BINDING      55     55       FMN (By similarity).
FT   BINDING      58     58       FMN; via amide nitrogen (By similarity).
FT   BINDING      60     60       Substrate (By similarity).
FT   BINDING      77     77       FMN (By similarity).
FT   BINDING     117    117       Substrate (By similarity).
FT   BINDING     121    121       Substrate (By similarity).
FT   BINDING     125    125       Substrate (By similarity).
SQ   SEQUENCE   208 AA;  23865 MW;  25FFBEBC76187422 CRC64;
     MEPVKMTNSS DDFTQSAEPF KLFAEWLADA AKSEPNDPNA VALATVDPDG LPNVRMVLLK
     DFDETGFVFY TNYESKKGQE ILSAEKAAMC FHWKSLRRQV RVRGPVEKVS DAEANAYYAS
     RPRGSRIGAW ASKQSRPLES RFALEKAVAE YTAKYAIGDI PRPPYWSGFR IRPVSIEFWH
     DRPFRLHDRV LFTRPTPEGD WNKDRLYP
//