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A5EXX0 (PDXH_DICNV) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 53. 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:DNO_1023
OrganismDichelobacter nodosus (strain VCS1703A) [Complete proteome] [HAMAP]
Taxonomic identifier246195 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCardiobacterialesCardiobacteriaceaeDichelobacter

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-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 – 212212Pyridoxine/pyridoxamine 5'-phosphate oxidase HAMAP-Rule MF_01629
PRO_0000335783

Regions

Nucleotide binding76 – 772FMN By similarity
Nucleotide binding140 – 1412FMN By similarity
Region191 – 1933Substrate 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

Sequences

Sequence LengthMass (Da)Tools
A5EXX0 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: C8C9F5F3B890DFE5

FASTA21224,570
        10         20         30         40         50         60 
MDIGSIRHDF TEHPPLLEQD LAADPIEQFA AWFQYAVDSG ISEPNGFVLA TVAADGQPSQ 

        70         80         90        100        110        120 
RSVLLKLFDE EGFVFYTNYS SQKAEEIEKN AQVSMSFPWY ALQRQIHVYG RAEKIPREQS 

       130        140        150        160        170        180 
LAYFLTRPQG SQIGAWASPQ SKIIESRDFL MLKWQNMKAK FHEGKIPLPD FWGGYRVRPH 

       190        200        210 
KIEFWQGQPS RLHDRFLYEK TENGWTVSRR AP 

« Hide

References

[1]"Genome sequence and identification of candidate vaccine antigens from the animal pathogen Dichelobacter nodosus."
Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q., Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D., McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T., Fedorova N. expand/collapse author list , Khouri H., Bottomley S.P., Whittington R.J., Adler B., Songer J.G., Rood J.I., Paulsen I.T.
Nat. Biotechnol. 25:569-575(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VCS1703A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000513 Genomic DNA. Translation: ABQ13205.1.
RefSeqYP_001209911.1. NC_009446.1.

3D structure databases

ProteinModelPortalA5EXX0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246195.DNO_1023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ13205; ABQ13205; DNO_1023.
GeneID5122950.
KEGGdno:DNO_1023.
PATRIC21786386. VBIDicNod48475_1021.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
KOK00275.
OMAPEHWGGY.
OrthoDBEOG60KN2Z.

Enzyme and pathway databases

BioCycDNOD246195:GHHS-1020-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_DICNV
AccessionPrimary (citable) accession number: A5EXX0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 53 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