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Q20939 (PDXH_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Putative pyridoxamine 5'-phosphate oxidase

EC=1.4.3.5
Alternative name(s):
PNP/PMP oxidase
Short name=PNPOx
Gene names
ORF Names:F57B9.1
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length226 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.

Catalytic activity

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

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

Cofactor

Binds 1 FMN per subunit By similarity.

Pathway

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

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.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   LigandFlavoprotein
FMN
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference 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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 226226Putative pyridoxamine 5'-phosphate oxidase
PRO_0000167788

Regions

Nucleotide binding87 – 882FMN By similarity
Nucleotide binding151 – 1522FMN By similarity
Region205 – 2073Substrate binding By similarity

Sites

Binding site721FMN By similarity
Binding site751FMN; via amide nitrogen By similarity
Binding site771Substrate By similarity
Binding site941FMN By similarity
Binding site1341Substrate By similarity
Binding site1381Substrate By similarity
Binding site1421Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q20939 [UniParc].

Last modified October 19, 2011. Version 2.
Checksum: 99E80C34C740AE2B

FASTA22626,101
        10         20         30         40         50         60 
METPSIDIQN IRAKYLNSHD PYLLESKLPT TSPFELFDIW FRNVASQSDL TFEEINAVSL 

        70         80         90        100        110        120 
STVGKDLRPS SRMVLLKAYT PTGFSFYTNY TSRKGNQLEE NPNAAMLFYW PKVNRQIRVE 

       130        140        150        160        170        180 
GVVEKLPDEM AVAYWNSRPV ASRIGSKSSD QSKVVPDREF LESKKVALTE LSVREGAQAI 

       190        200        210        220 
TKPESWGGYH LIPRYFEFWQ GQSDRLHDRI VFERDVDVWL LKRLSP 

« Hide

References

[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FO081266 Genomic DNA. Translation: CCD70322.1.
PIRA88494.
RefSeqNP_498518.2. NM_066117.3.
UniGeneCel.10391.

3D structure databases

ProteinModelPortalQ20939.
SMRQ20939. Positions 25-226.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ20939. 1 interaction.
STRING6239.F57B9.1.

Proteomic databases

PaxDbQ20939.
PRIDEQ20939.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaF57B9.1; F57B9.1; F57B9.1.
GeneID175973.
KEGGcel:CELE_F57B9.1.
UCSCF57B9.1. c. elegans.

Organism-specific databases

CTD175973.
WormBaseF57B9.1; CE44186; WBGene00018996.

Phylogenomic databases

eggNOGCOG0259.
HOGENOMHOG000242755.
InParanoidQ20939.
OMANFESQKG.
OrthoDBEOG7B8S4P.

Enzyme and pathway databases

UniPathwayUPA00190; UER00304.
UPA00190; UER00305.

Family and domain databases

Gene3D2.30.110.10. 1 hit.
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...

Other

NextBio890562.
PROQ20939.

Entry information

Entry namePDXH_CAEEL
AccessionPrimary (citable) accession number: Q20939
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 19, 2011
Last modified: April 16, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase