(data stored in ACNUC7421 zone)

SWISSPROT: PDXH_SINFN

ID   PDXH_SINFN              Reviewed;         206 AA.
AC   C3MHI2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase {ECO:0000255|HAMAP-Rule:MF_01629};
DE            EC=1.4.3.5 {ECO:0000255|HAMAP-Rule:MF_01629};
DE   AltName: Full=PNP/PMP oxidase {ECO:0000255|HAMAP-Rule:MF_01629};
DE            Short=PNPOx {ECO:0000255|HAMAP-Rule:MF_01629};
DE   AltName: Full=Pyridoxal 5'-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01629};
GN   Name=pdxH {ECO:0000255|HAMAP-Rule:MF_01629};
GN   OrderedLocusNames=NGR_c05140;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-
CC       phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal
CC       5'-phosphate (PLP). {ECO:0000255|HAMAP-Rule:MF_01629}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) +
CC         pyridoxal 5'-phosphate; Xref=Rhea:RHEA:15817, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58451, ChEBI:CHEBI:597326; EC=1.4.3.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01629};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + pyridoxine 5'-phosphate = H2O2 + pyridoxal 5'-
CC         phosphate; Xref=Rhea:RHEA:15149, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:58589, ChEBI:CHEBI:597326;
CC         EC=1.4.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01629};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01629};
CC       Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01629};
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC       pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01629}.
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC       pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01629}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01629}.
CC   -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01629}.
DR   EMBL; CP001389; ACP24310.1; -; Genomic_DNA.
DR   RefSeq; WP_012707095.1; NC_012587.1.
DR   RefSeq; YP_002825063.1; NC_012587.1.
DR   SMR; C3MHI2; -.
DR   STRING; 394.NGR_c05140; -.
DR   EnsemblBacteria; ACP24310; ACP24310; NGR_c05140.
DR   GeneID; 7791740; -.
DR   KEGG; rhi:NGR_c05140; -.
DR   PATRIC; fig|394.7.peg.3327; -.
DR   eggNOG; ENOG4108S7T; Bacteria.
DR   eggNOG; COG0259; LUCA.
DR   HOGENOM; HOG000242755; -.
DR   KO; K00275; -.
DR   OMA; PEPNAMV; -.
DR   OrthoDB; 1542844at2; -.
DR   UniPathway; UPA01068; UER00304.
DR   UniPathway; UPA01068; UER00305.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.110.10; -; 1.
DR   HAMAP; MF_01629; PdxH; 1.
DR   InterPro; IPR000659; Pyridox_Oxase.
DR   InterPro; IPR019740; Pyridox_Oxase_CS.
DR   InterPro; IPR011576; Pyridox_Oxase_put.
DR   InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   PANTHER; PTHR10851; PTHR10851; 1.
DR   Pfam; PF10590; PNP_phzG_C; 1.
DR   Pfam; PF01243; Putative_PNPOx; 1.
DR   PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1.
DR   TIGRFAMs; TIGR00558; pdxH; 1.
DR   PROSITE; PS01064; PYRIDOX_OXIDASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MHI2.
DR   SWISS-2DPAGE; C3MHI2.
KW   Complete proteome; Flavoprotein; FMN; Oxidoreductase;
KW   Pyridoxine biosynthesis; Reference proteome.
FT   CHAIN         1    206       Pyridoxine/pyridoxamine 5'-phosphate
FT                                oxidase.
FT                                /FTId=PRO_1000186330.
FT   NP_BIND      53     58       FMN. {ECO:0000255|HAMAP-Rule:MF_01629}.
FT   NP_BIND      68     69       FMN. {ECO:0000255|HAMAP-Rule:MF_01629}.
FT   NP_BIND     132    133       FMN. {ECO:0000255|HAMAP-Rule:MF_01629}.
FT   REGION      183    185       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01629}.
FT   BINDING      58     58       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01629}.
FT   BINDING      75     75       FMN. {ECO:0000255|HAMAP-Rule:MF_01629}.
FT   BINDING      97     97       FMN. {ECO:0000255|HAMAP-Rule:MF_01629}.
FT   BINDING     115    115       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01629}.
FT   BINDING     119    119       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01629}.
FT   BINDING     123    123       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01629}.
FT   BINDING     177    177       FMN. {ECO:0000255|HAMAP-Rule:MF_01629}.
FT   BINDING     187    187       FMN. {ECO:0000255|HAMAP-Rule:MF_01629}.
SQ   SEQUENCE   206 AA;  23876 MW;  406150CF528CD6C2 CRC64;
     MTANELTTGD FTDADEPFSL FGTWLKDAEK NEVNDPNAVA LATVDPDGLP NVRMVLLKGF
     DEHGFVFYTN FESQKGQELL STRKAAMCFH WKSLRRQVRL RGPVEIVTAE EADEYFRSRP
     RGSRIGAWAS KQSRPLESRF ALEKAVAEFT ARHAIGEIPR PEYWSGFRIR PTSIEFWHDR
     PFRLHDRVEF RRPVPEGGWE KVRMYP
//

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