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Reviewed, UniProtKB/Swiss-Prot Q492T8 (PDXH_BLOPB)

Last modified June 16, 2009. Version 30. 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: BPEN_381
OrganismBlochmannia pennsylvanicus (strain BPEN) [Complete proteome] [HAMAP]
Taxonomic identifier291272 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › ant endosymbionts › Candidatus Blochmannia

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Protein attributes

Sequence length216 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 – 216216Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629
PRO_0000167688

Regions

Nucleotide binding80 – 812FMN By similarity
Nucleotide binding144 – 1452FMN By similarity
Region12 – 154Substrate binding By similarity
Region195 – 1973Substrate binding By similarity

Sites

Binding site651FMN By similarity
Binding site681FMN; via amide nitrogen By similarity
Binding site701Substrate By similarity
Binding site871FMN By similarity
Binding site1271Substrate By similarity
Binding site1311Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q492T8-1 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: CC87E55758F56C8B

FASTA21625,738
        10         20         30         40         50         60 
MLIDKTNISN IRREYISGQL RHTDLTNQPI QLFSVWLHQA YFSKIPDPTA MCLATVDHTG 

        70         80         90        100        110        120 
QPYQRVVLLK NFTNKEMIFY TNLSSRKAMH LANNPKVSLC FLWNVIDRQV IITGSVDKLP 

       130        140        150        160        170        180 
EKEVLKYFYT RPKNNQISTW VSNQSKVISS KDLLENKFLE FKKNHLHKKV PFPEFWGGYK 

       190        200        210 
ININSMEFWQ GGTHRLHDRF IYQRYKHTWR IYRLSP

« Hide

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References

[1]"Genome sequence of Blochmannia pennsylvanicus indicates parallel evolutionary trends among bacterial mutualists of insects."
Degnan P.H., Lazarus A.B., Wernegreen J.J.
Genome Res. 15:1023-1033(2005) [PubMed: 16077009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000016 Genomic DNA. Translation: AAZ41005.1.
RefSeqYP_277880.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3562646.
GenomeReviewsGene locus BPEN_381 in contig CP000016_GR.
KEGGbpn:BPEN_381.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ492T8.
OMAQ492T8. FTFFTNY.

Enzyme and pathway databases

BioCycCBLO291272:BPEN_381-MON.

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_BLOPB
AccessionPrimary (citable) accession number: Q492T8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: September 13, 2005
Last modified: June 16, 2009
This is version 30 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