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A5VNZ1 (PDXH_BRUO2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. 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:BOV_0424
OrganismBrucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) [Complete proteome] [HAMAP]
Taxonomic identifier444178 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length208 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 – 208208Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_1000069683

Regions

Nucleotide binding70 – 712FMN By similarity
Nucleotide binding134 – 1352FMN By similarity
Region185 – 1873Substrate binding By similarity

Sites

Binding site551FMN By similarity
Binding site581FMN; via amide nitrogen By similarity
Binding site601Substrate By similarity
Binding site771FMN By similarity
Binding site1171Substrate By similarity
Binding site1211Substrate By similarity
Binding site1251Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A5VNZ1 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 25FFBEBC76187422

FASTA20823,865
        10         20         30         40         50         60 
MEPVKMTNSS DDFTQSAEPF KLFAEWLADA AKSEPNDPNA VALATVDPDG LPNVRMVLLK 

        70         80         90        100        110        120 
DFDETGFVFY TNYESKKGQE ILSAEKAAMC FHWKSLRRQV RVRGPVEKVS DAEANAYYAS 

       130        140        150        160        170        180 
RPRGSRIGAW ASKQSRPLES RFALEKAVAE YTAKYAIGDI PRPPYWSGFR IRPVSIEFWH 

       190        200 
DRPFRLHDRV LFTRPTPEGD WNKDRLYP 

« Hide

References

[1]Paulsen I.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25840 / 63/290 / NCTC 10512.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000708 Genomic DNA. Translation: ABQ60142.1.
RefSeqYP_001258438.1. NC_009505.1.

3D structure databases

ProteinModelPortalA5VNZ1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING444178.BOV_0424.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ60142; ABQ60142; BOV_0424.
GeneID5201318.
KEGGbov:BOV_0424.
PATRIC17860642. VBIBruOvi136990_1739.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMANFESQKG.
OrthoDBEOG60KN2Z.
ProtClustDBPRK05679.

Enzyme and pathway databases

BioCycBOVI444178:GH2V-422-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_BRUO2
AccessionPrimary (citable) accession number: A5VNZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 10, 2007
Last modified: April 16, 2014
This is version 51 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