[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Cramton S.E., Richard C., Oberfeld B., Pfitzner U., Gotz F.; Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tibor L., Cramton S.E., Goetz F., Hunt T.K.; Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.; "The Staphylococcus aureus NCTC8325 genome."; Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Reduces arsenate [As(V)] to arsenite [As(III)] and dephosphorylates tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Could switch between different functions in different circumstances (By similarity).
CATALYTIC ACTIVITY: Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate.
CATALYTIC ACTIVITY: Arsenate + thioredoxin = arsenite + thioredoxin disulfide + H₂O.
SUBUNIT: Monomer (By similarity).
SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein phosphatase superfamily. ArsC family.

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

AF422190; AAN32731.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY194063; AAP32342.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000253; ABD30957.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_500395.1; -.

3D structure databases

SMR

Q2FXF5; 1-131.

ModBase

Q2FXF5.

Enzyme and pathway databases

BioCyc

SAUR93061:SAOUHSC_01894-MON; -.

Ontologies

GO:0030612;	Molecular function: arsenate reductase (thioredoxin) activity (inferred from electronic annotation from HAMAP).
GO:0004725;	Molecular function: protein tyrosine phosphatase activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006470;	Biological process: protein amino acid dephosphorylation (inferred from electronic annotation from InterPro).
GO:0046685;	Biological process: response to arsenic (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01624; -; 1.
PBIL [Tree]

InterPro

IPR014064; Arsenate_reductase_StaphA.
IPR000106; Tyr_Pase_low_mol_wt.
Graphical view of domain structure.

PANTHER

PTHR11717; Low_mwt_PTPase; 1.

Pfam

PF01451; LMWPc; 1.
Pfam graphical view of domain structure.

SMART

SM00226; LMWPc; 1.
SMART graphical view of domain structure.

TIGRFAMs

TIGR02691; arsC_pI258_fam; 1.

ProtoNet

Q2FXF5.

Genome annotation databases

GeneID

3920841; -.

GenomeReviews

CP000253_GR; SAOUHSC_01894.

KEGG

sao:SAOUHSC_01894; -.

Phylogenomic databases

HOGENOM

Q2FXF5; -.

Genome annotation databases

CMR

Q2FXF5; SAOUHSC_01894.

Other

UniRef

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

Keywords

Arsenical resistance; Complete proteome; Hydrolase; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 131`	`131`	`Protein arsC.`	`PRO_0000290356`
`ACT_SITE`	`10 10`		`Nucleophile; for reductase activity and phosphatase activity (By similarity).`
`ACT_SITE`	`82 82`		`Nucleophile; for reductase activity (By similarity).`
`ACT_SITE`	`89 89`		`Nucleophile; for reductase activity (By similarity).`
`DISULFID`	`10 82`		`Redox-active; alternate (By similarity).`
`DISULFID`	`82 89`		`Redox-active; alternate (By similarity).`

Sequence information

Length: 131 AA [This is the length of the unprocessed precursor]

Molecular weight: 14687 Da [This is the MW of the unprocessed precursor]

CRC64: 9B6AA5A854D66C89 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTKKTIYFIC TGNSCRSQMA EGWAKQILAD DWNVYSAGIE THGVNPKAIE AMKEVGIDIS 

        70         80         90        100        110        120 
NHTSDLIDNN IIKNSNLVVT LCSDADVNCP SLPTNVKKEH WGFDDPAGKP WSEFQRVRDE 

       130 
IKIAIENFKS R

Q2FXF5 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