Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot A5VNZ1 (PDXH_BRUO2)

Last modified June 16, 2009. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

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 lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Hide | Top

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

Hide | Top

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.

Catalytic activity

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

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

Cofactor

Binds 1 FMN per subunit By similarity.

Pathway

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

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

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the pyridoxamine 5'-phosphate oxidase family.

Hide | Top

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

pyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionFMN binding

Inferred from electronic annotation. Source: HAMAP

pyridoxamine-phosphate oxidase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 208208Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP 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

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
A5VNZ1-1 [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

Hide | Top

References

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

Hide | Top

Cross-references

Sequence databases

CP000708 Genomic DNA. Translation: ABQ60142.1.
RefSeqYP_001258438.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5201318.
GenomeReviewsGene locus BOV_0424 in contig CP000708_GR.
KEGGbov:BOV_0424.
TIGRBOV_0424.

Phylogenomic databases

OMAA5VNZ1. EPFALFA.

Family and domain databases

HAMAPMF_01629.
[Tree]
InterProIPR011576. PNPOx_rel_FMN_bd_core.
IPR000659. Pyridoxamine_oxidase.
IPR019740. Pyridoxamine_oxidase_CS.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN_bd.
[Graphical view]
Gene3DG3DSA:2.30.110.10. PNPOx_FMN_bd. 1 hit.
PANTHERPTHR10851. Pyridox_oxidase. 1 hit.
PfamPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
ProDomPD006312. Pyridox_oxidase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00558. pdxH. 1 hit.
PROSITEPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

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: June 16, 2009
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents