ID   PDXH_ECO24              Reviewed;         218 AA.
AC   A7ZMA0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 14.
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=EcE24377A_1848;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic
RT   analysis of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV21134.1; -; Genomic_DNA.
DR   RefSeq; YP_001462929.1; -.
DR   GeneID; 5587953; -.
DR   GenomeReviews; CP000800_GR; EcE24377A_1848.
DR   KEGG; ecw:EcE24377A_1848; -.
DR   NMPDR; fig|331111.3.peg.4275; -.
DR   OMA; A7ZMA0; 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    218       Pyridoxine/pyridoxamine 5'-phosphate
FT                                oxidase.
FT                                /FTId=PRO_1000069691.
FT   NP_BIND      82     83       FMN (By similarity).
FT   NP_BIND     146    147       FMN (By similarity).
FT   REGION       14     17       Substrate binding (By similarity).
FT   REGION      197    199       Substrate binding (By similarity).
FT   BINDING      67     67       FMN (By similarity).
FT   BINDING      70     70       FMN; via amide nitrogen (By similarity).
FT   BINDING      72     72       Substrate (By similarity).
FT   BINDING      89     89       FMN (By similarity).
FT   BINDING     129    129       Substrate (By similarity).
FT   BINDING     133    133       Substrate (By similarity).
FT   BINDING     137    137       Substrate (By similarity).
SQ   SEQUENCE   218 AA;  25573 MW;  D4E7CB0742CF5A39 CRC64;
     MSDNDELQQI AHLRREYTKG GLRRRDLPAD PLTLFERWLS QACEAKLADP TAMVVATVDE
     HAQPYQRIVL LKHYDEKGMV FYTNLGSRKA HQIENNPRVS LLFPWHTLER QVMVIGKAER
     LSTLEVMKYF HSRPRDSQIG AWVSKQSSRI SARGILESKF LELKQKFQQG EVPLPSFWGG
     FRISLEQIEF WQGGEHRLHD RFLYQRENDA WKIDRLAP
//