ID   PDXH_CAEEL              Reviewed;         253 AA.
AC   Q20939;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Putative pyridoxamine 5'-phosphate oxidase;
DE            EC=1.4.3.5;
DE   AltName: Full=PNP/PMP oxidase;
DE            Short=PNPOx;
GN   ORFNames=F57B9.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
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; U13876; AAA21167.1; -; Genomic_DNA.
DR   PIR; A88494; A88494.
DR   RefSeq; NP_498518.1; -.
DR   UniGene; Cel.10391; -.
DR   HSSP; Q9NVS9; 1NRG.
DR   IntAct; Q20939; 1.
DR   Ensembl; F57B9.1; Caenorhabditis elegans.
DR   GeneID; 175973; -.
DR   KEGG; cel:F57B9.1; -.
DR   NMPDR; fig|6239.3.peg.10352; -.
DR   WormBase; WBGene00018996; F57B9.1.
DR   WormPep; F57B9.1; CE01335.
DR   OMA; Q20939; RKGSELE.
DR   BRENDA; 1.4.3.5; 672.
DR   NextBio; 890562; -.
DR   ArrayExpress; Q20939; -.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Complete proteome; Flavoprotein; FMN; Oxidoreductase;
KW   Pyridoxine biosynthesis.
FT   CHAIN         1    253       Putative pyridoxamine 5'-phosphate
FT                                oxidase.
FT                                /FTId=PRO_0000167788.
FT   NP_BIND     114    115       FMN (By similarity).
FT   NP_BIND     178    179       FMN (By similarity).
FT   REGION      232    234       Substrate binding (By similarity).
FT   BINDING      99     99       FMN (By similarity).
FT   BINDING     102    102       FMN; via amide nitrogen (By similarity).
FT   BINDING     104    104       Substrate (By similarity).
FT   BINDING     121    121       FMN (By similarity).
FT   BINDING     161    161       Substrate (By similarity).
FT   BINDING     165    165       Substrate (By similarity).
FT   BINDING     169    169       Substrate (By similarity).
SQ   SEQUENCE   253 AA;  29402 MW;  887A80EC98B84958 CRC64;
     MFVVPRRLSS FLSLVHEYRH LARRSYVMET PSIDIQNIRA KYLNSHDPYL LESKLPTTSP
     FELFDIWFRN VASQSDLTFE EINAVSLSTV GKDLRPSSRM VLLKAYTPTG FSFYTNYTSR
     KGNQLEENPN AAMLFYWPKV NRQIRVEGVV EKLPDEMAVA YWNSRPVASR IGSKSSDQSK
     VVPDREFLES KKVALTELSV REGAQAITKP ESWGGYHLIP RYFEFWQGQS DRLHDRIVFE
     RDVDVWLLKR LSP
//