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Reviewed, UniProtKB/Swiss-Prot Q9MB35 (PERQ_SEDLI)

Last modified June 16, 2009. Version 36. 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:
    Peroxiredoxin Q, chloroplastic
    EC=1.11.1.15
Alternative name(s):
    Thioredoxin reductase
Gene names
Name: PRXQ
OrganismSedum lineare (Needle stonecrop)
Taxonomic identifier114260 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsSaxifragalesCrassulaceaeSedum

Protein attributes

Sequence length186 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Reduces hydrogen peroxide with reducing equivalents provided through the thioredoxin system By similarity.

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Subunit structure

Monomer. Ref.1

Subcellular location

Plastidchloroplast thylakoid By similarity.

Post-translational modification

The Cys-80-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-80 (probably Cys-SOH) rapidly reacts with Cys-85-SH to form an intramolecular disulfide. This disulfide is subsequently reduced by thioredoxin to restore the reduced active form of the enzyme.

Sequence similarities

Belongs to the ahpC/TSA family. PrxQ subfamily.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   DomainRedox-active center
Transit peptide
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast thylakoid

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionperoxiredoxin activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide‹1 – 36›36Chloroplast Potential
Chain37 – 186150Peroxiredoxin Q, chloroplastic
PRO_5000049527

Regions

Domain38 – 186149Thioredoxin

Sites

Active site801Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Disulfide bond80 ↔ 85Redox-active

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q9MB35-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 31E915D940CF2402

FASTA18620,652
        10         20         30         40         50         60 
QTLQTSSQSQ FHGLKFSHAS SFKSPSAPLR KNSIFAKVTK GSTPPPFTLK DQEGRPVSLS 

        70         80         90        100        110        120 
KFKGKPVVVY FYPADETPGC TKQACAFRDS YEKFKKAGAE VVGISGDSSE SHKAFAKKYK 

       130        140        150        160        170        180 
LPFTLLSDEG NKVRKEWGVP SDLFGTLPGR ETYVLDKNGV VQLVYNNQFQ PEKHIDETLK 


LLQSLK 

« Hide

References

[1]"A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp)."
Kong W., Shiota S., Shi Y., Nakayama H., Nakayama K.
Biochem. J. 351:107-114(2000) [PubMed: 10998352] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.

Cross-references

Sequence databases

AB037598 mRNA. Translation: BAA90524.1.

3D structure databases

HSSPHSSP built from PDB template 1QQ2 based on UniProtKB Q63716.
ModBaseSearch...

Protein family/group databases

PeroxiBase4304. SlinPrxQ.

Enzyme and pathway databases

BRENDA1.11.1.15. 291237.

Family and domain databases

InterProIPR000866. Alkyl_hydroperoxide_Rdtase.
IPR017936. Thioredoxin-like.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF00578. AhpC-TSA. 1 hit.
[Graphical view]
ProDomPD003679. Thioredoxin_like. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePERQ_SEDLI
AccessionPrimary (citable) accession number: Q9MB35
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 36 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