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Reviewed, UniProtKB/Swiss-Prot A3MHF0 (PDXH_BURM7)

Last modified June 16, 2009. Version 20. 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

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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: BMA10247_0107
OrganismBurkholderia mallei (strain NCTC 10247) [Complete proteome] [HAMAP]
Taxonomic identifier320389 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

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Protein attributes

Sequence length214 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 214214Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629
PRO_1000069684

Regions

Nucleotide binding76 – 772FMN By similarity
Nucleotide binding140 – 1412FMN By similarity
Region8 – 114Substrate binding By similarity
Region190 – 1923Substrate binding By similarity

Sites

Binding site611FMN By similarity
Binding site641FMN; via amide nitrogen By similarity
Binding site661Substrate By similarity
Binding site831FMN By similarity
Binding site1231Substrate By similarity
Binding site1271Substrate By similarity
Binding site1311Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
A3MHF0-1 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 0BA6365597CAB424

FASTA21424,295
        10         20         30         40         50         60 
MTTLADLRTN YSRASLDAAD VNPNPFVQFD VWFKEALDAQ LPEPNTMTLA TVDESGRPSA 

        70         80         90        100        110        120 
RIVLIKGADE RGFVFFTNYE SRKGRELAHN PNAALLFYWI ELERQVRVEG RIEKTSEEES 

       130        140        150        160        170        180 
DRYFASRPLG SRIGAWASEQ SAVIESRALL EAREKEIGAR FGENPPRPPH WGGYRLVPSS 

       190        200        210 
IEFWQGRPSR LHDRLLYTRD AASASGWKIT RLAP

« Hide

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References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000548 Genomic DNA. Translation: ABO04885.1.
RefSeqYP_001079686.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4892035.
GenomeReviewsGene locus BMA10247_0107 in contig CP000548_GR.
KEGGbmn:BMA10247_0107.
TIGRBMA10247_0107.

Phylogenomic databases

OMAA3MHF0. FTFFTNY.

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...

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Entry information

Entry namePDXH_BURM7
AccessionPrimary (citable) accession number: A3MHF0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: April 3, 2007
Last modified: June 16, 2009
This is version 20 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)

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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