ID   PDXH_BAUCH              Reviewed;         216 AA.
AC   Q1LU04;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=BCI_0082;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF14338.1; -; Genomic_DNA.
DR   RefSeq; YP_588560.1; -.
DR   GeneID; 4056190; -.
DR   GenomeReviews; CP000238_GR; BCI_0082.
DR   KEGG; bci:BCI_0082; -.
DR   HOGENOM; Q1LU04; -.
DR   OMA; Q1LU04; FTFFTNY.
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_0000255853.
FT   NP_BIND      80     81       FMN (By similarity).
FT   NP_BIND     144    145       FMN (By similarity).
FT   REGION       12     15       Substrate binding (By similarity).
FT   REGION      195    197       Substrate binding (By similarity).
FT   BINDING      65     65       FMN (By similarity).
FT   BINDING      68     68       FMN; via amide nitrogen (By similarity).
FT   BINDING      70     70       Substrate (By similarity).
FT   BINDING      87     87       FMN (By similarity).
FT   BINDING     127    127       Substrate (By similarity).
FT   BINDING     131    131       Substrate (By similarity).
FT   BINDING     135    135       Substrate (By similarity).
SQ   SEQUENCE   216 AA;  25278 MW;  225724267EE7639C CRC64;
     MNKQSINIAQ IRREYTHKRL RRADLTLEPM ELFERWFRQA STAQLLDLTV VSVATVDQTG
     QPYQRLVLLK HFDAKGMVFY TNLGSRKAQH LAHNARISLH FPWHALERQV MVLGTAKQLA
     LKEVMHYFSS RPRNSQISAW ASSQSSLIDT RDTLVSTFLK FNNYFHQGKV PLPSFWGGYR
     VHIDSMEFWQ GGAYRLHDRF IYQRIASGWR IDRLAP
//