ID   PDXH_BARHE              Reviewed;         207 AA.
AC   Q6G4D7;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 38.
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=BH04290;
OS   Bartonella henselae (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=38323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF27238.1; -; Genomic_DNA.
DR   RefSeq; YP_033267.1; -.
DR   GeneID; 2865013; -.
DR   GenomeReviews; BX897699_GR; BH04290.
DR   KEGG; bhe:BH04290; -.
DR   NMPDR; fig|283166.1.peg.395; -.
DR   HOGENOM; Q6G4D7; -.
DR   OMA; Q6G4D7; EPFALFA.
DR   BioCyc; BHEN283166:BH04290-MON; -.
DR   BRENDA; 1.4.3.5; 277357.
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    207       Pyridoxine/pyridoxamine 5'-phosphate
FT                                oxidase.
FT                                /FTId=PRO_0000167684.
FT   NP_BIND      68     69       FMN (By similarity).
FT   NP_BIND     132    133       FMN (By similarity).
FT   REGION      183    185       Substrate binding (By similarity).
FT   BINDING      53     53       FMN (By similarity).
FT   BINDING      56     56       FMN; via amide nitrogen (By similarity).
FT   BINDING      58     58       Substrate (By similarity).
FT   BINDING      75     75       FMN (By similarity).
FT   BINDING     115    115       Substrate (By similarity).
FT   BINDING     119    119       Substrate (By similarity).
FT   BINDING     123    123       Substrate (By similarity).
SQ   SEQUENCE   207 AA;  24271 MW;  7702729BA8E64A47 CRC64;
     MGNTVQTDND FMQMQKPFAL FAKWLEEATV SEINDPNAMA LATVDKTGFP NVRMVLLKDF
     SPQGFVFYTN YESPKGQEIL KSMKASLVFH WKSLRRQVRI RGIVEKVTPQ EADAYFQSRP
     RDSRIGAWAS KQSQPLESRF VLEKAIARYT TRYAVGNIPR PPYWSGFRVK PLSIEFWCDR
     PFRLHDRLLF TRDSVEHVDW KRQKLYP
//