(data stored in ACNUC7421 zone)

HOGENOM: STANL_1_PE1005

ID   STANL_1_PE1005                       STANDARD;      PRT;   214 AA.
AC   STANL_1_PE1005; D3QA16;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase; EC=1.4.3
DE   5;AltName: Full=PNP/PMP oxidase;AltName: Full=Pyridoxal 5'-phosphate
DE   synthase; (STANL_1.PE1005).
GN   Name=pdxH; OrderedLocusNames=Snas_1018;
OS   STACKEBRANDTIA NASSAUENSIS DSM 44728.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Glycomycineae; Glycomycetaceae; Stackebrandtia.
OX   NCBI_TaxID=446470;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STANL_1.PE1005.
CC       Stackebrandtia nassauensis DSM 44728 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D3QA16_STANL
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   -!- GENE_FAMILY: HOG000242755 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D3QA16; -.
DR   EMBL; CP001778; ADD40728.1; -; Genomic_DNA.
DR   RefSeq; YP_003509821.1; NC_013947.1.
DR   ProteinModelPortal; D3QA16; -.
DR   GeneID; 8882203; -.
DR   GenomeReviews; CP001778_GR; Snas_1018.
DR   KEGG; sna:Snas_1018; -.
DR   OMA; FTFFTNY; -.
DR   GO; GO:0010181; F:FMN binding; IEA:HAMAP.
DR   GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:HAMAP.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01629; PdxH; 1; -.
DR   InterPro; IPR000659; Pyridoxamine_Oxase.
DR   InterPro; IPR019740; Pyridoxamine_Oxase_CS.
DR   InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C.
DR   InterPro; IPR011576; PyridoxamineP_Oxase_FMN-bd.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   InterPro; IPR009002; Split_barrel_FMN-bd-related.
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   PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1.
DR   SUPFAM; SSF50475; FMN_binding; 1.
DR   TIGRFAMs; TIGR00558; PdxH; 1.
DR   PROSITE; PS01064; PYRIDOX_OXIDASE; 1.
DR   HOGENOMDNA; STANL_1.PE1005; -.
KW   Complete proteome; Flavoprotein; FMN; Oxidoreductase;
KW   Pyridoxine biosynthesis.
SQ   SEQUENCE   214 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKRTVNAEDL SRLRREYDEP DELDLETDPF GWFRRWFDEA ATVEPEPNAM VLATVDDQGF
     PRQRTVLLKS FDTSGFTFFT NYTSDKGVQL TANPKVNLLF GWYRLHRQVI VSGTAKRVPP
     EESARYFATR PRGAQLAAWA SPQSRPIPGR TDLESAFAQA EARFPDEVPV PPHWGGFLVE
     PRLIEFWQGR RNRMHDRVRY HRESSAWVPV RLAP
//

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