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   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=Acel_0116;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / 11B).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Frankineae; Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Berry A.M., Adney W.S., Normand P.,
RA   Leu D., Pujic P., Richardson P.;
RT   "Complete sequence of Acidothermus cellulolyticus 11B.";
RL   Submitted (OCT-2006) 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; CP000481; ABK51892.1; -; Genomic_DNA.
DR   RefSeq; YP_871878.1; -.
DR   GeneID; 4484559; -.
DR   GenomeReviews; CP000481_GR; Acel_0116.
DR   KEGG; ace:Acel_0116; -.
DR   OMA; A0LR32; 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   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    224       Pyridoxine/pyridoxamine 5'-phosphate
FT                                oxidase.
FT                                /FTId=PRO_0000292281.
FT   NP_BIND      83     84       FMN (By similarity).
FT   NP_BIND     148    149       FMN (By similarity).
FT   REGION      200    202       Substrate binding (By similarity).
FT   BINDING      69     69       FMN (By similarity).
FT   BINDING      72     72       FMN; via amide nitrogen (By similarity).
FT   BINDING      74     74       Substrate (By similarity).
FT   BINDING      90     90       FMN (By similarity).
FT   BINDING     130    130       Substrate (By similarity).
FT   BINDING     134    134       Substrate (By similarity).
FT   BINDING     138    138       Substrate (By similarity).
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
//