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Q9ZPY1 (PPOX2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 93. 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:
Pyridoxine/pyridoxamine 5'-phosphate oxidase 2

Short name=AtPPOX1
EC=1.4.3.5
Gene names
Name:PPOX2
Ordered Locus Names:At2g46580
ORF Names:F13A10.11
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). Has an in vitro catalytic efficiency for PNP approximately 300-fold lower than that of PPOX1. Ref.5

Catalytic activity

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

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

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_processpyridoxal 5'-phosphate salvage

Inferred from direct assay. Source: UniProtKB

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 direct assay. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 198198Pyridoxine/pyridoxamine 5'-phosphate oxidase 2
PRO_0000420550

Regions

Nucleotide binding59 – 602FMN By similarity
Nucleotide binding121 – 1222FMN By similarity
Compositional bias158 – 1614Poly-Leu

Sites

Binding site421FMN By similarity
Binding site661FMN By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZPY1 [UniParc].

Last modified June 1, 2002. Version 2.
Checksum: EFDE8DA20D6A4376

FASTA19822,620
        10         20         30         40         50         60 
MGTHVAPWKQ LLFGAIEANS HLSHSSYVQL ATIGLNGRPS NRTVVFRGFE ENSDRIQINT 

        70         80         90        100        110        120 
DLRSRKIEEL KHCPFSEMCW YFSDTWEQFR INGRIEVIDA SNPDQTKLQQ REKAWFANSL 

       130        140        150        160        170        180 
RSRLIYVCPT PGSPCNSEQS SQQVKLDPSS GPVPEYCLLL LEPEKVDYLN LKTNQRLFFS 

       190 
SMATGTGEKC WTSEKVNP 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Arabidopsis ORF clones."
Shinn P., Chen H., Kim C.J., Ecker J.R.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Identification of a second pyridoxine (pyridoxamine) 50-phosphate oxidase in Arabidopsis thaliana."
Sang Y., Goertzen L.R., Tzou Y.-M., Locy R.D., Singh N.K.
Acta Physiol. Plant. 33:559-566(2011)
Cited for: FUNCTION, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC006418 Genomic DNA. Translation: AAD20168.2.
CP002685 Genomic DNA. Translation: AEC10724.1.
AY086412 mRNA. Translation: AAM63414.1.
BT024917 mRNA. Translation: ABD94073.1.
PIRF84904.
RefSeqNP_566081.1. NM_130223.2.
UniGeneAt.21431.

3D structure databases

ProteinModelPortalQ9ZPY1.
SMRQ9ZPY1. Positions 2-198.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT2G46580.1-P.

Proteomic databases

PaxDbQ9ZPY1.
PRIDEQ9ZPY1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G46580.1; AT2G46580.1; AT2G46580.
GeneID819270.
KEGGath:AT2G46580.

Organism-specific databases

TAIRAT2G46580.

Phylogenomic databases

eggNOGCOG5135.
HOGENOMHOG000233130.
InParanoidQ9ZPY1.
OMANYVEECA.
PhylomeDBQ9ZPY1.

Enzyme and pathway databases

UniPathwayUPA00190; UER00304.
UPA00190; UER00305.

Gene expression databases

GenevestigatorQ9ZPY1.

Family and domain databases

Gene3D2.30.110.10. 1 hit.
InterProIPR000659. Pyridox_Oxase.
IPR024624. Pyridox_Oxase_Alr4036_FMN-bd.
IPR024015. Pyridox_Oxase_FMN-dep_Alr4036.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PANTHERPTHR10851. PTHR10851. 1 hit.
PfamPF12766. Pyridox_oxase_2. 1 hit.
[Graphical view]
SUPFAMSSF50475. SSF50475. 1 hit.
TIGRFAMsTIGR04026. PPOX_FMN_cyano. 1 hit.
ProtoNetSearch...

Other

PROQ9ZPY1.

Entry information

Entry namePPOX2_ARATH
AccessionPrimary (citable) accession number: Q9ZPY1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2013
Last sequence update: June 1, 2002
Last modified: May 14, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names