[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=DSM 319; DOI=10.1099/mic.0.27626-0; PubMed=15758224 [NCBI, ExPASy, EBI, Israel, Japan] Nahrstedt H., Schroder C., Meinhardt F.; "Evidence for two recA genes mediating DNA repair in Bacillus megaterium."; Microbiology 151:775-787(2005).

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

AJ515540; CAD56680.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P45947; 1JL3. [HSSP ENTRY / PDB]

SMR

Q8GJ74; 4-140.

ModBase

Q8GJ74.

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.

Other

ProtoNet

Q8GJ74.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 140`	`140`	`Protein arsC.`	`PRO_0000162519`
`ACT_SITE`	`10 10`		`Nucleophile; for reductase activity and phosphatase activity (By similarity).`
`ACT_SITE`	`83 83`		`Nucleophile; for reductase activity (By similarity).`
`ACT_SITE`	`90 90`		`Nucleophile; for reductase activity (By similarity).`
`DISULFID`	`10 83`		`Redox-active; alternate (By similarity).`
`DISULFID`	`83 90`		`Redox-active; alternate (By similarity).`

Sequence information

Length: 140 AA [This is the length of the unprocessed precursor]

Molecular weight: 15688 Da [This is the MW of the unprocessed precursor]

CRC64: 046DD5DB132DDCA9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKKTLYFLC TGNSCRSQMA EGWAKKYLNN NEWDVRSAGL EAHGLNPNAV KAMKEAGVDI 

        70         80         90        100        110        120 
SNQTSDVIDP EILNNADLVV TLCGHAADHC PVTPPHVKRE HWGFDDPAKA EGTDEEKWAF 

       130        140 
FQRVRDEIAE RIQRFAETGK

Q8GJ74 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