ID   PDXH_ECOLC              Reviewed;         218 AA.
AC   B1IQB6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   16-JUN-2009, entry version 10.
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=EcolC_1991;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) 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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000946; ACA77637.1; -; Genomic_DNA.
DR   RefSeq; YP_001724964.1; -.
DR   GeneID; 6068157; -.
DR   GenomeReviews; CP000946_GR; EcolC_1991.
DR   KEGG; ecl:EcolC_1991; -.
DR   OMA; B1IQB6; 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   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_1000088113.
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;  25545 MW;  8B47CEEEA6CEF5F9 CRC64;
     MSDNDELQQI AHLRREYTKG GLRRRDLPAD PLTLFERWLS QACEAKLADP TAMVVATVDE
     HGQPYQRIVL LKHYDEKGMV FYTNLGSRKA HQIENNPRVS LLFPWHTLER QVMVIGKAER
     LSTLEVMKYF HSRPRDSQIG AWVSKQSSRI SARGILESKF LELKQKFQQG EVPLPSFWGG
     FRVSLEQIEF WQGGEHRLHD RFLYQRENDA WKIDRLAP
//