ID   PDXH_CYTH3              Reviewed;         215 AA.
AC   Q11U72;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-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=CHU_1775;
OS   Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469).
OC   Bacteria; Bacteroidetes; Sphingobacteria; Sphingobacteriales;
OC   Flexibacteraceae; Cytophaga.
OX   NCBI_TaxID=269798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17400776; DOI=10.1128/AEM.00225-07;
RA   Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C.,
RA   Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P.,
RA   Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B.,
RA   Wilson D.B., McBride M.J.;
RT   "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT   hutchinsonii.";
RL   Appl. Environ. Microbiol. 73:3536-3546(2007).
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; CP000383; ABG59042.1; -; Genomic_DNA.
DR   RefSeq; YP_678384.1; -.
DR   GeneID; 4186847; -.
DR   GenomeReviews; CP000383_GR; CHU_1775.
DR   KEGG; chu:CHU_1775; -.
DR   NMPDR; fig|269798.12.peg.1691; -.
DR   HOGENOM; Q11U72; -.
DR   OMA; Q11U72; RKGSELE.
DR   BioCyc; CHUT269798:CHU_1775-MON; -.
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    215       Pyridoxine/pyridoxamine 5'-phosphate
FT                                oxidase.
FT                                /FTId=PRO_0000255863.
FT   NP_BIND      77     78       FMN (By similarity).
FT   NP_BIND     141    142       FMN (By similarity).
FT   REGION        9     12       Substrate binding (By similarity).
FT   REGION      193    195       Substrate binding (By similarity).
FT   BINDING      62     62       FMN (By similarity).
FT   BINDING      65     65       FMN; via amide nitrogen (By similarity).
FT   BINDING      67     67       Substrate (By similarity).
FT   BINDING      84     84       FMN (By similarity).
FT   BINDING     124    124       Substrate (By similarity).
FT   BINDING     128    128       Substrate (By similarity).
FT   BINDING     132    132       Substrate (By similarity).
SQ   SEQUENCE   215 AA;  24745 MW;  46492608793B9759 CRC64;
     MKTNLADIRK EYSSRSLDTK DILPSPVEQF RLWLNQALEA GALEATAMNL ATVNEAGKPA
     SRIVLLKGIE HGSFVFYTNY KSHKGSDITH NSFGALNFFW PELERQVRIE GKITKVSPED
     SDTYFNSRPY QSKIGAWVSD QSKEVASREE LESKITYYEN KYPEGSVVPR PAHWGGYTLK
     PAYFEFWQGR PSRLHDRIVY DLEGDIRWNV FRICP
//