NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
DOI=10.1042/0264-6021:3510107; PubMed=10998352 [NCBI, ExPASy, EBI, Israel, Japan]
Kong W., Shiota S., Shi Y., Nakayama H., Nakayama K.;
"A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp).";
Biochem. J. 351:107-114(2000).

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).
PTM: The Cys-80-SH group is the primary site of oxidation by H(2)O(2), 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.
SIMILARITY: Belongs to the ahpC/TSA family. PrxQ subfamily.
SIMILARITY: Contains 1 thioredoxin domain.

Copyright

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Cross-references

Sequence databases

EMBL

AB037598; BAA90524.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q63716; 1QQ2. [HSSP ENTRY / PDB]

ModBase

Q9MB35.

Protein family/group databases

PeroxiBase

4304; SlinPrxQ.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0051920;	Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.

ProDom

PD003679; Thioredoxin_like; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

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

ProtoNet

Q9MB35.

Other

UniRef

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 36`	`>36`	`Chloroplast (Potential).`
`CHAIN`	`37 186`	`150`	`Peroxiredoxin Q, chloroplastic.`	`PRO_5000049527`
`DOMAIN`	`38 186`	`149`	`Thioredoxin.`
`ACT_SITE`	`80 80`		`Cysteine sulfenic acid (-SOH) intermediate (By similarity).`
`DISULFID`	`80 85`		`Redox-active.`
`NON_TER`	`1 1`

Sequence information

Length: 186 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 20652 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 31E915D940CF2402 [This is a checksum on the sequence]

        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

Q9MB35 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