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Q01MI9 (APX3_ORYSI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Probable L-ascorbate peroxidase 3

EC=1.11.1.11
Alternative name(s):
OsAPx03
Gene names
Name:APX3
ORF Names:H0515C11.2, OsI_014375
OrganismOryza sativa subsp. indica (Rice)
Taxonomic identifier39946 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length291 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays a key role in hydrogen peroxide removal By similarity.

Catalytic activity

2 L-ascorbate + H2O2 + 2 H+ = L-ascorbate + L-dehydroascorbate + 2 H2O.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group By similarity.

Subcellular location

Membrane; Single-pass membrane protein Potential.

Miscellaneous

Binds one cation per subunit; probably K+, but might also be Ca2+ By similarity.

Sequence similarities

Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Caution

According to Ref.1, it may be peroxisomal. There is however no experimental evidence to prove this.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   LigandCalcium
Heme
Iron
Metal-binding
Potassium
   Molecular functionOxidoreductase
Peroxidase
Gene Ontology (GO)
   Biological_processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionL-ascorbate peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

heme binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 291291Probable L-ascorbate peroxidase 3
PRO_0000300258

Regions

Transmembrane263 – 28321Helical; Potential

Sites

Active site411Proton acceptor By similarity
Metal binding1611Iron (heme axial ligand) By similarity
Metal binding1621Potassium or calcium By similarity
Metal binding1781Potassium or calcium By similarity
Metal binding1851Potassium or calcium By similarity
Site371Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01MI9 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 9D2E57C3DBC277F6

FASTA29132,076
        10         20         30         40         50         60 
MSAAPVVDAE YMAEVERARR DLRALIASKS CAPIMLRLAW HDAGTYDKAT KTGGPNGSIR 

        70         80         90        100        110        120 
FPQEYSHAAN AGIKIAIDLL EPMKQRHPKI TYADLYQLAG VVAVEVTGGP TIDYVPGRRD 

       130        140        150        160        170        180 
SSDSPEEGRL PDAKKGAAHL REVFYRMGLS DKDIVALSGG HTLGKARPER SGFDGAWTKD 

       190        200        210        220        230        240 
PLKFDNSYFI ELLKENSEGL LKLPTDKALV EDPTFRRYVE LYAKDEDAFF RDYAESHKKL 

       250        260        270        280        290 
SELGFTPPRS AFIYKSCQKP KSLLMQTAAG VAVAAAVVAW AYLCESNKRL G 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the molecular evolutionary history of the ascorbate peroxidase gene family: inferences from the rice genome."
Teixeira F.K., Menezes-Benavente L., Margis R., Margis-Pinheiro M.
J. Mol. Evol. 59:761-770(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], NOMENCLATURE.
[2]"Sequence and analysis of rice chromosome 4."
Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y., Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q., Zhang L. expand/collapse author list , Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T., Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R., Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G., Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C., Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J., Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J., Li J., Hong G., Xue Y., Han B.
Nature 420:316-320(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Guang-Lu-Ai No.4.
[3]"The genomes of Oryza sativa: a history of duplications."
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. expand/collapse author list , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. 93-11.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY382617 mRNA. Translation: AAQ88105.1.
CR855043 Genomic DNA. Translation: CAH66026.1.
CM000129 Genomic DNA. Translation: EAY93142.1.
UniGeneOs.4987.

3D structure databases

ProteinModelPortalQ01MI9.
SMRQ01MI9. Positions 5-245.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneQ01MI9.

Phylogenomic databases

eggNOGCOG0376.
HOGENOMHOG000189824.

Family and domain databases

InterProIPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMSSF48113. SSF48113. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAPX3_ORYSI
AccessionPrimary (citable) accession number: Q01MI9
Secondary accession number(s): A2XQN2, Q6TY83, Q7XWZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: November 14, 2006
Last modified: April 16, 2014
This is version 43 of the entry and version 1 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