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Pyridoxine/pyridoxamine 5'-phosphate oxidase (EC 1.4.3.5) (PNP/PMP oxidase) (PNPOx) (Pyridoxal 5'-phosphate synthase)

 PDXH_SALPC              Reviewed;         218 AA.
C0Q5T4;
28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 1.
07-JUN-2017, entry version 55.
RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase {ECO:0000255|HAMAP-Rule:MF_01629};
EC=1.4.3.5 {ECO:0000255|HAMAP-Rule:MF_01629};
AltName: Full=PNP/PMP oxidase {ECO:0000255|HAMAP-Rule:MF_01629};
Short=PNPOx {ECO:0000255|HAMAP-Rule:MF_01629};
AltName: Full=Pyridoxal 5'-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01629};
Name=pdxH {ECO:0000255|HAMAP-Rule:MF_01629};
OrderedLocusNames=SPC_2283;
Salmonella paratyphi C (strain RKS4594).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=476213;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RKS4594;
PubMed=19229335; DOI=10.1371/journal.pone.0004510;
Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T.,
Peng Y.-H., Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R.,
Liu S.-L.;
"Salmonella paratyphi C: genetic divergence from Salmonella
choleraesuis and pathogenic convergence with Salmonella typhi.";
PLoS ONE 4:E4510-E4510(2009).
-!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-
phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal
5'-phosphate (PLP). {ECO:0000255|HAMAP-Rule:MF_01629}.
-!- CATALYTIC ACTIVITY: Pyridoxamine 5'-phosphate + H(2)O + O(2) =
pyridoxal 5'-phosphate + NH(3) + H(2)O(2). {ECO:0000255|HAMAP-
Rule:MF_01629}.
-!- CATALYTIC ACTIVITY: Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'-
phosphate + H(2)O(2). {ECO:0000255|HAMAP-Rule:MF_01629}.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000255|HAMAP-Rule:MF_01629};
Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01629};
-!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
{ECO:0000255|HAMAP-Rule:MF_01629}.
-!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
{ECO:0000255|HAMAP-Rule:MF_01629}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01629}.
-!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase
family. {ECO:0000255|HAMAP-Rule:MF_01629}.
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EMBL; CP000857; ACN46400.1; -; Genomic_DNA.
RefSeq; WP_001282334.1; NC_012125.1.
ProteinModelPortal; C0Q5T4; -.
SMR; C0Q5T4; -.
EnsemblBacteria; ACN46400; ACN46400; SPC_2283.
KEGG; sei:SPC_2283; -.
HOGENOM; HOG000242755; -.
KO; K00275; -.
OMA; PEPNAMV; -.
UniPathway; UPA01068; UER00304.
UniPathway; UPA01068; UER00305.
Proteomes; UP000001599; Chromosome.
GO; GO:0010181; F:FMN binding; IEA:InterPro.
GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:UniProtKB-EC.
GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
Gene3D; 2.30.110.10; -; 1.
HAMAP; MF_01629; PdxH; 1.
InterPro; IPR000659; Pyridox_Oxase.
InterPro; IPR019740; Pyridox_Oxase_CS.
InterPro; IPR011576; Pyridox_Oxase_put.
InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C.
InterPro; IPR012349; Split_barrel_FMN-bd.
PANTHER; PTHR10851:SF4; PTHR10851:SF4; 1.
Pfam; PF10590; PNP_phzG_C; 1.
Pfam; PF01243; Putative_PNPOx; 1.
PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1.
SUPFAM; SSF50475; SSF50475; 1.
TIGRFAMs; TIGR00558; pdxH; 1.
PROSITE; PS01064; PYRIDOX_OXIDASE; 1.
3: Inferred from homology;
Complete proteome; Flavoprotein; FMN; Oxidoreductase;
Pyridoxine biosynthesis.
CHAIN 1 218 Pyridoxine/pyridoxamine 5'-phosphate
oxidase.
/FTId=PRO_1000186338.
NP_BIND 67 72 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}.
NP_BIND 82 83 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}.
NP_BIND 146 147 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}.
REGION 14 17 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01629}.
REGION 197 199 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01629}.
BINDING 72 72 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01629}.
BINDING 88 88 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}.
BINDING 89 89 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}.
BINDING 111 111 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}.
BINDING 129 129 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01629}.
BINDING 133 133 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01629}.
BINDING 137 137 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01629}.
BINDING 191 191 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}.
BINDING 201 201 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}.
SEQUENCE 218 AA; 25499 MW; 43CAF2F67B6BFB70 CRC64;
MSDNDQLQQI AHLRREYTKG GLRRRDLPAE PLTLFERWLG QACDARLADP TAMVVATVDD
KGQPYQRIVL LKHYDEKGLV FYTNLGSRKA HQIEHNPRIS LLFPWHMLER QVMVTGKAER
LSTLEVVRYF HSRPRDSQIG AWVSKQSSRI SARGILESKF LELKQKFQQG EVPLPSFWGG
FRVSIEQMEF WQGGEHRLHD RFLYQRDDGA WKIDRLAP


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