NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=301 / Serotype 2a;
DOI=10.1093/nar/gkf566; PubMed=12384590 [NCBI, ExPASy, EBI, Israel, Japan]
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157.";
Nucleic Acids Res. 30:4432-4441(2002).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700930 / 2457T / Serotype 2a;
DOI=10.1128/IAI.71.5.2775-2786.2003; PubMed=12704152 [NCBI, ExPASy, EBI, Israel, Japan]
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T.";
Infect. Immun. 71:2775-2786(2003).

Comments

FUNCTION: Directly reduces organic hydroperoxides in its reduced dithiol form (By similarity).
CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H₂O + ROH.
SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By similarity).
PTM: The Cys-47-SH group is the primary site of oxidation by H(2)O(2), and the oxidized Cys-47 (probably Cys-SOH) rapidly reacts with Cys-166-SH of the other subunit to form an intermolecular disulfide. This disulfide is subsequently reduced by thioredoxin (By similarity).
SIMILARITY: Belongs to the ahpC/TSA family.
SIMILARITY: Contains 1 thioredoxin domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE005674; AAN42170.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014073; AAP16040.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_706463.1; -.
NP_836234.1; -.

3D structure databases

HSSP

P19479; 1N8J. [HSSP ENTRY / PDB]

SMR

P0AE11; 2-187.

ModBase

P0AE11.

Enzyme and pathway databases

BioCyc

SFLE198214:AAN42170.1-MON; -.

Ontologies

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.
IPR017559; Peroxiredoxin.
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).

Genome annotation databases

GeneID

1023440; -.
1076966; -.

GenomeReviews

AE005674_GR; SF0524.
AE014073_GR; S0529.

KEGG

sfl:SF0524; -.
sfx:S0529; -.

Phylogenomic databases

HOGENOM

P0AE11; -.

Genome annotation databases

CMR

P0AE11; SF0524.

Other

ProtoNet

P0AE11.

UniRef

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

Keywords

Acetylation; Antioxidant; Complete proteome; Oxidoreductase; Peroxidase; Redox-active center.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 187`	`186`	`Alkyl hydroperoxide reductase subunit C.`	`PRO_0000135121`
`DOMAIN`	`2 157`	`156`	`Thioredoxin.`
`ACT_SITE`	`47 47`		`Cysteine sulfenic acid (-SOH) intermediate (By similarity).`
`MOD_RES`	`17 17`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`93 93`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`153 153`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`169 169`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`171 171`		`N6-acetyllysine (By similarity).`
`DISULFID`	`47 47`		`Interchain (with C-166); in linked form (By similarity).`
`DISULFID`	`166 166`		`Interchain (with C-47); in linked form (By similarity).`

Sequence information

Length: 187 AA [This is the length of the unprocessed precursor]

Molecular weight: 20761 Da [This is the MW of the unprocessed precursor]

CRC64: 40AB796E6F5CC2D6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLINTKIKP FKNQAFKNGE FIEITEKDTE GRWSVFFFYP ADFTFVCPTE LGDVADHYEE 

        70         80         90        100        110        120 
LQKLGVDVYA VSTDTHFTHK AWHSSSETIA KIKYAMIGDP TGALTRNFDN MREDEGLADR 

       130        140        150        160        170        180 
ATFVVDPQGI IQAIEVTAEG IGRDASDLLR KIKAAQYVAS HPGEVCPAKW KEGEATLAPS 


LDLVGKI

P0AE11 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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