NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/S0140-6736(02)08713-5; PubMed=12044378 [NCBI, ExPASy, EBI, Israel, Japan]
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
"Genome and virulence determinants of high virulence community-acquired MRSA.";
Lancet 359:1819-1827(2002).

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-49-SH group is the primary site of oxidation by H(2)O(2), and the oxidized Cys-49 (probably Cys-SOH) rapidly reacts with Cys-168-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

BA000033; BAB94222.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_645174.1; -.

3D structure databases

HSSP

P19479; 1N8J. [HSSP ENTRY / PDB]

ModBase

P0A0B6.

Protein family/group databases

PeroxiBase

4924; SaurAhpC.

Enzyme and pathway databases

BioCyc

SAUR196620:MW0357-MON; -.

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).

BLOCKS

P0A0B6.

Genome annotation databases

GeneID

1002457; -.

GenomeReviews

BA000033_GR; MW0357.

KEGG

sam:MW0357; -.

Phylogenomic databases

HOGENOM

P0A0B6; -.

Genome annotation databases

CMR

P0A0B6; MW0357.

Other

ProtoNet

P0A0B6.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 189`	`189`	`Alkyl hydroperoxide reductase subunit C.`	`PRO_0000135127`
`DOMAIN`	`2 159`	`158`	`Thioredoxin.`
`ACT_SITE`	`49 49`		`Cysteine sulfenic acid (-SOH) intermediate (By similarity).`
`DISULFID`	`49 49`		`Interchain (with C-168); in linked form (By similarity).`
`DISULFID`	`168 168`		`Interchain (with C-49); in linked form (By similarity).`

Sequence information

Length: 189 AA [This is the length of the unprocessed precursor]

Molecular weight: 20977 Da [This is the MW of the unprocessed precursor]

CRC64: B7134A9C84066B73 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLINKEILP FTAQAFDPKK DQFKEVTQED LKGSWSVVCF YPADFSFVCP TELEDLQNQY 

        70         80         90        100        110        120 
EELQKLGVNV FSVSTDTHFV HKAWHDHSDA ISKITYTMIG DPSQTITRNF DVLDEATGLA 

       130        140        150        160        170        180 
QRGTFIIDPD GVVQASEINA DGIGRDASTL AHKIKAAQYV RKNPGEVCPA KWEEGAKTLQ 


PGLDLVGKI

P0A0B6 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