[1]	NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION. DOI=10.1016/j.plantsci.2004.05.004; AGRICOLA=IND43645556 Guo X.-L., Cao Y.-R., Cao Z.-Y., Zhao Y.-X., Zhang H.; "Molecular cloning and characterization of a stress-induced peroxiredoxin Q gene in halophyte Suaeda salsa."; Plant Sci. 167:969-975(2004).

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: Monomer.
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid (By similarity).
INDUCTION: Up-regulated by NaCl, mannitol, low temperature, H(2)O(2), methyl viologen, and abscisic acid (ABA).
PTM: The Cys-109-SH group is the primary site of oxidation by H(2)O(2), 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.
SIMILARITY: Belongs to the ahpC/TSA family. PrxQ subfamily.
SIMILARITY: Contains 1 thioredoxin domain.

Copyright

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Cross-references

Sequence databases

EMBL

AY373447; AAQ67661.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q6UBI3.

Protein family/group databases

PeroxiBase

4306; SsaPrxQ.

Family and domain databases

InterPro

IPR000866; AhpC-TSA.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

Pfam

PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.

PROSITE

PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Antioxidant; Chloroplast; Oxidoreductase; Peroxidase; Plastid; Redox-active center; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 64`	`64`	`Chloroplast (Potential).`
`CHAIN`	`65 214`	`150`	`Peroxiredoxin Q, chloroplastic.`	`PRO_0000285113`
`DOMAIN`	`67 214`	`148`	`Thioredoxin.`
`ACT_SITE`	`109 109`		`Cysteine sulfenic acid (-SOH) intermediate (By similarity).`
`DISULFID`	`109 114`		`Redox-active.`

Sequence information

Length: 214 AA [This is the length of the unprocessed precursor]

Molecular weight: 23589 Da [This is the MW of the unprocessed precursor]

CRC64: 83D5F660082AC855 [This is a checksum on the sequence]

        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

Q6UBI3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools