NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831;
DOI=10.1093/nar/gkf526; PubMed=12235376 [NCBI, ExPASy, EBI, Israel, Japan]
Takami H., Takaki Y., Uchiyama I.;
"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments.";
Nucleic Acids Res. 30:3927-3935(2002).

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

BA000028; BAC14379.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_693344.1; -.

3D structure databases

HSSP

P45947; 1JL3. [HSSP ENTRY / PDB]

SMR

Q8ENQ5; 4-139.

ModBase

Q8ENQ5.

Enzyme and pathway databases

BioCyc

OIHE221109:OB2423-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.

Genome annotation databases

1017228; -.

BA000028_GR; OB2423.

oih:OB2423; -.

fig|221109.1.peg.2420; -.

Phylogenomic databases

HOGENOM

Q8ENQ5; -.

Genome annotation databases

CMR

Q8ENQ5; OB2423.

Other

ProtoNet

Q8ENQ5.

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`	`1 139`	`139`	`Protein arsC.`	`PRO_0000162522`
`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: 139 AA [This is the length of the unprocessed precursor]

Molecular weight: 15676 Da [This is the MW of the unprocessed precursor]

CRC64: 09F5110ED5E43249 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKKIIYFLC TGNSCRSQMA EGWGKKILGE EWDVYSAGIE AHGLNPNAIK AMREVDIDIT 

        70         80         90        100        110        120 
NQTSDQIDKD ILNKADFVVT LCGDAKDKCP MTPPHVKRDH WGFEDPAKAQ GTEEEKWTVF 

       130 
QQVRDKIGDR IKVFAKTGE

Q8ENQ5 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