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Reviewed, UniProtKB/Swiss-Prot Q20939 (PDXH_CAEEL)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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 [Complete proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length253 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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
   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: 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 – 253253Putative pyridoxamine 5'-phosphate oxidase
PRO_0000167788

Regions

Nucleotide binding114 – 1152FMN By similarity
Nucleotide binding178 – 1792FMN By similarity
Region232 – 2343Substrate binding By similarity

Sites

Binding site991FMN By similarity
Binding site1021FMN; via amide nitrogen By similarity
Binding site1041Substrate By similarity
Binding site1211FMN By similarity
Binding site1611Substrate By similarity
Binding site1651Substrate By similarity
Binding site1691Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q20939-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 887A80EC98B84958

FASTA25329,402
        10         20         30         40         50         60 
MFVVPRRLSS FLSLVHEYRH LARRSYVMET PSIDIQNIRA KYLNSHDPYL LESKLPTTSP 

        70         80         90        100        110        120 
FELFDIWFRN VASQSDLTFE EINAVSLSTV GKDLRPSSRM VLLKAYTPTG FSFYTNYTSR 

       130        140        150        160        170        180 
KGNQLEENPN AAMLFYWPKV NRQIRVEGVV EKLPDEMAVA YWNSRPVASR IGSKSSDQSK 

       190        200        210        220        230        240 
VVPDREFLES KKVALTELSV REGAQAITKP ESWGGYHLIP RYFEFWQGQS DRLHDRIVFE 

       250 
RDVDVWLLKR LSP 

« 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: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.

Cross-references

Sequence databases

U13876 Genomic DNA. Translation: AAA21167.1.
PIRA88494.
RefSeqNP_498518.1.
UniGeneCel.10391

3D structure databases

HSSPHSSP built from PDB template 1NRG based on UniProtKB Q9NVS9.
ModBaseSearch...

Protein-protein interaction databases

IntActQ20939. 1 interaction.

Genome annotation databases

EnsemblF57B9.1. Caenorhabditis elegans. [Contig view]
GeneID175973.
KEGGcel:F57B9.1.
NMPDRfig|6239.3.peg.10352.

Organism-specific databases

WormBaseWBGene00018996. F57B9.1.
WormPepF57B9.1. CE01335. [WorfDB]

Phylogenomic databases

OMAQ20939. RKGSELE.

Enzyme and pathway databases

BRENDA1.4.3.5. 672.

Gene expression databases

ArrayExpressQ20939.

Family and domain databases

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...

Other Resources

NextBio890562.

Entry information

Entry namePDXH_CAEEL
AccessionPrimary (citable) accession number: Q20939
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

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

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