Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot Q6UBI3 (PERQ_SUASA)

Last modified June 16, 2009. Version 41. 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
OrganismSuaeda salsa (Seepweed) (Chenopodium salsum)
Taxonomic identifier126914 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsCaryophyllalesAmaranthaceaeSuaeda

Protein attributes

Sequence length214 AA.
Sequence statusComplete.
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.

Subcellular location

Plastidchloroplast thylakoid By similarity.

Induction

Up-regulated by NaCl, mannitol, low temperature, H2O2, methyl viologen, and abscisic acid (ABA). Ref.1

Post-translational modification

The Cys-109-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-109 (probably Cys-SOH) rapidly reacts with Cys-114-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 peptide1 – 6464Chloroplast Potential
Chain65 – 214150Peroxiredoxin Q, chloroplastic
PRO_0000285113

Regions

Domain67 – 214148Thioredoxin

Sites

Active site1091Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Disulfide bond109 ↔ 114Redox-active

Sequences

Sequence LengthMass (Da)Tools
Q6UBI3-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 83D5F660082AC855

FASTA21423,589
        10         20         30         40         50         60 
MATLSLPNHS PTFALPSQTP KPHSSQNLSI ISKSAHSQFC GIKLSHSSSL SPPLYPRSYK 

        70         80         90        100        110        120 
ASIVAKVSEG SMPPAFTLKD QDGKNVSLSK FKGKPVVVYF YPADETPGCT KQACAFRDSY 

       130        140        150        160        170        180 
EKFKKAGAEV IGISGDDSSS HKAFKQKYKL PYTLLSDEGN KVRKDWGVPS DLFGALPGRQ 

       190        200        210 
TYVLDRNGVV RLVYNNQFQP EKHIDETLKF LQSL 

« Hide

References

[1]"Molecular cloning and characterization of a stress-induced peroxiredoxin Q gene in halophyte Suaeda salsa."
Guo X.-L., Cao Y.-R., Cao Z.-Y., Zhao Y.-X., Zhang H.
Plant Sci. 167:969-975(2004) [Agricola: IND43645556]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.

Cross-references

Sequence databases

AY373447 mRNA. Translation: AAQ67661.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

PeroxiBase4306. SsaPrxQ.

Enzyme and pathway databases

BRENDA1.11.1.15. 291105.

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]
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePERQ_SUASA
AccessionPrimary (citable) accession number: Q6UBI3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: July 5, 2004
Last modified: June 16, 2009
This is version 41 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