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Q57PI9 (PDXH_SALCH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyridoxine/pyridoxamine 5'-phosphate oxidase

EC=1.4.3.5
Alternative name(s):
PNP/PMP oxidase
Short name=PNPOx
Pyridoxal 5'-phosphate synthase
Gene names
Name:pdxH
Ordered Locus Names:SCH_1466
OrganismSalmonella choleraesuis (strain SC-B67) [Complete proteome] [HAMAP]
Taxonomic identifier321314 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) By similarity. HAMAP-Rule MF_01629

Catalytic activity

Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2. HAMAP-Rule MF_01629

Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2. HAMAP-Rule MF_01629

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP-Rule MF_01629

Pathway

Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. HAMAP-Rule MF_01629

Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01629

Sequence similarities

Belongs to the pyridoxamine 5'-phosphate oxidase family.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   LigandFlavoprotein
FMN
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionFMN binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxamine-phosphate oxidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 218218Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000167750

Regions

Nucleotide binding82 – 832FMN By similarity
Nucleotide binding146 – 1472FMN By similarity
Region14 – 174Substrate binding By similarity
Region197 – 1993Substrate binding By similarity

Sites

Binding site671FMN By similarity
Binding site701FMN; via amide nitrogen By similarity
Binding site721Substrate By similarity
Binding site891FMN By similarity
Binding site1291Substrate By similarity
Binding site1331Substrate By similarity
Binding site1371Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q57PI9 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 43CAF2F67B6BFB70

FASTA21825,499
        10         20         30         40         50         60 
MSDNDQLQQI AHLRREYTKG GLRRRDLPAE PLTLFERWLG QACDARLADP TAMVVATVDD 

        70         80         90        100        110        120 
KGQPYQRIVL LKHYDEKGLV FYTNLGSRKA HQIEHNPRIS LLFPWHMLER QVMVTGKAER 

       130        140        150        160        170        180 
LSTLEVVRYF HSRPRDSQIG AWVSKQSSRI SARGILESKF LELKQKFQQG EVPLPSFWGG 

       190        200        210 
FRVSIEQMEF WQGGEHRLHD RFLYQRDDGA WKIDRLAP 

« Hide

References

[1]"The genome sequence of Salmonella enterica serovar Choleraesuis, a highly invasive and resistant zoonotic pathogen."
Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S., Lee Y.-S.
Nucleic Acids Res. 33:1690-1698(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC-B67.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017220 Genomic DNA. Translation: AAX65372.1.
RefSeqYP_216453.1. NC_006905.1.

3D structure databases

ProteinModelPortalQ57PI9.
SMRQ57PI9. Positions 5-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING321314.SC1466.

Proteomic databases

PRIDEQ57PI9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX65372; AAX65372; SCH_1466.
PATRIC32323696. VBISalEnt136302_1840.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
OMAPEHWGGY.
OrthoDBEOG60KN2Z.
ProtClustDBPRK05679.

Enzyme and pathway databases

BioCycSENT321314:GJCS-1530-MONOMER.
UniPathwayUPA00190; UER00304.
UPA00190; UER00305.

Family and domain databases

Gene3D2.30.110.10. 1 hit.
HAMAPMF_01629. PdxH.
InterProIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PANTHERPTHR10851. PTHR10851. 1 hit.
PfamPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMSSF50475. SSF50475. 1 hit.
TIGRFAMsTIGR00558. pdxH. 1 hit.
PROSITEPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXH_SALCH
AccessionPrimary (citable) accession number: Q57PI9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: May 10, 2005
Last modified: April 16, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways