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A8HRJ3 (PDXH_AZOC5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:AZC_1197
OrganismAzorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / ORS 571) [Complete proteome] [HAMAP]
Taxonomic identifier438753 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Xanthobacteraceae › Azorhizobium

Protein attributes

Sequence length212 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 MF_01629

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. HAMAP MF_01629

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. HAMAP MF_01629

Sequence similarities

Belongs to the pyridoxamine 5'-phosphate oxidase family.

Sequence caution

The sequence BAF87195.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   LigandFMN
Flavoprotein
   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: InterPro

pyridoxamine-phosphate oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP MF_01629
PRO_0000335780

Regions

Nucleotide binding74 – 752FMN By similarity
Nucleotide binding138 – 1392FMN By similarity
Region189 – 1913Substrate binding By similarity

Sites

Binding site591FMN By similarity
Binding site621FMN; via amide nitrogen By similarity
Binding site641Substrate By similarity
Binding site811FMN By similarity
Binding site1211Substrate By similarity
Binding site1251Substrate By similarity
Binding site1291Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A8HRJ3 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: 89376966E4892CDD

FASTA21224,177
        10         20         30         40         50         60 
MSDSAMEPQN PLTSGDFTAA DEPFRLFSEW LKDAERSEPN DPNAMTLATV DPDGLPDARM 

        70         80         90        100        110        120 
VLLKGLDDRG FVFYTNTESA KGRELTAHPK AALVFHWKSL RRQVRVRGPV ERVTDAEADA 

       130        140        150        160        170        180 
YFATRPRLSQ IGAWASQQSR PLEGRFALEA AVATTTARYA VGSVPRPPHW TGFRILPVQI 

       190        200        210 
EFWHDRPFRL HDRVVFKREN PEIDWEKSRL YP

« Hide

References

[1]"Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium caulinodans ORS571."
Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43989 / DSM 5975 / ORS 571.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009384 Genomic DNA. Translation: BAF87195.1. Different initiation.
RefSeqYP_001524113.1. NC_009937.1.

3D structure databases

ProteinModelPortalA8HRJ3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8HRJ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5690268.
GenomeReviewsGene locus AZC_1197 in contig AP009384_GR.
KEGGazc:AZC_1197.
PATRIC21018967. VBIAzoCau17976_1253.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG327559.
ProtClustDBCLSK979777.

Enzyme and pathway databases

BioCycACAU438753:AZC_1197-MONOMER.

Family and domain databases

HAMAPMF_01629. PdxH.
[Tree]
InterProIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
IPR009002. Split_barrel_FMN-bd-related.
[Graphical view]
Gene3DG3DSA:2.30.110.10. PNPOx_FMN_bd. 1 hit.
KOK00275.
PANTHERPTHR10851. Pyridox_oxidase. 1 hit.
PfamPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMSSF50475. FMN_binding. 1 hit.
TIGRFAMsTIGR00558. PdxH. 1 hit.
PROSITEPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXH_AZOC5
AccessionPrimary (citable) accession number: A8HRJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 34 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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