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Reviewed, UniProtKB/Swiss-Prot P81833 (APX4_SPIOL)

Last modified June 16, 2009. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 L-ascorbate peroxidase, chloroplastic
    EC=1.11.1.11
Alternative name(s):
    Thylakoid lumenal 29 kDa protein
      Short name=TL29
    P29
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsCaryophyllalesAmaranthaceaeSpinacia

Protein attributes

Sequence length30 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Plays a key role in hydrogen peroxide removal By similarity.

Catalytic activity

L-ascorbate + H2O2 = dehydroascorbate + 2 H2O.

Subcellular location

Plastidchloroplast thylakoid lumen.

Sequence similarities

Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentChloroplast
Plastid
Thylakoid
   Molecular functionOxidoreductase
Peroxidase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast thylakoid lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-ascorbate peroxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›30›30Putative L-ascorbate peroxidase, chloroplastic
PRO_0000055598

Experimental info

Non-terminal residue301

Sequences

Sequence LengthMass (Da)Tools
P81833-1 [UniParc].

Last modified May 30, 2000. Version 1.
Checksum: 62CFECD847A3FA52

FASTA303,546
        10         20         30 
ADLIQRRQRS EFQSDIKGIL YTVIKKNPDL 

« Hide

References

[1]"The thylakoid lumen of chloroplasts. Isolation and characterization."
Kieselbach T., Hagman A., Andersson B., Schroeder W.P.
J. Biol. Chem. 273:6710-6716(1998) [PubMed: 9506969] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Leaf.

Cross-references

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.11.1.11. 286.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameAPX4_SPIOL
AccessionPrimary (citable) accession number: P81833
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: June 16, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

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