Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8GJ74 (ARSC_BACMD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein ArsC
Alternative name(s):
Arsenate reductase
EC=1.20.4.-
Arsenical pump modifier
Low molecular weight protein-tyrosine-phosphatase
EC=3.1.3.48
Gene names
Name:arsC
Ordered Locus Names:BMD_1727
OrganismBacillus megaterium (strain DSM 319) [Complete proteome] [HAMAP]
Taxonomic identifier592022 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length140 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (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. HAMAP-Rule MF_01624

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. HAMAP-Rule MF_01624

Arsenate + thioredoxin = arsenite + thioredoxin disulfide + H2O. HAMAP-Rule MF_01624

Subunit structure

Monomer By similarity. HAMAP-Rule MF_01624

Sequence similarities

Belongs to the low molecular weight phosphotyrosine protein phosphatase superfamily. ArsC family.

Ontologies

Keywords
   Biological processArsenical resistance
   DomainRedox-active center
   Molecular functionHydrolase
Oxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processresponse to arsenic-containing substance

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionarsenate reductase (thioredoxin) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 140140Protein ArsC HAMAP-Rule MF_01624
PRO_0000162519

Sites

Active site101Nucleophile; for reductase activity and phosphatase activity By similarity
Active site831Nucleophile; for reductase activity By similarity
Active site901Nucleophile; for reductase activity By similarity

Amino acid modifications

Disulfide bond10 ↔ 83Redox-active; alternate By similarity
Disulfide bond83 ↔ 90Redox-active; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8GJ74 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 046DD5DB132DDCA9

FASTA14015,688
        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 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for two recA genes mediating DNA repair in Bacillus megaterium."
Nahrstedt H., Schroder C., Meinhardt F.
Microbiology 151:775-787(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome sequences of the industrial vitamin B12-producers B. megaterium QM B1551 and DSM319 reveal new insights into the Bacillus genome evolution and pan-genome structure."
Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J., Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J., Vary P.S.
Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 319.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ515540 Genomic DNA. Translation: CAD56680.1.
CP001982 Genomic DNA. Translation: ADF38582.1.
RefSeqYP_003596932.1. NC_014103.1.

3D structure databases

ProteinModelPortalQ8GJ74.
SMRQ8GJ74. Positions 1-140.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADF38582; ADF38582; BMD_1727.
GeneID9117118.
KEGGbmd:BMD_1727.
PATRIC37253484. VBIBacMeg104484_1668.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000273093.
KOK03741.
OMAGDRYEAY.

Enzyme and pathway databases

BioCycBMEG592022:GIVX-1727-MONOMER.

Family and domain databases

HAMAPMF_01624. Arsenate_reduct.
InterProIPR014064. Arsenate_reductase_ArsC.
IPR023485. Ptyr_pPase_SF.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERPTHR11717. PTHR11717. 1 hit.
PfamPF01451. LMWPc. 1 hit.
[Graphical view]
SMARTSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMSSF52788. SSF52788. 1 hit.
TIGRFAMsTIGR02691. arsC_pI258_fam. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARSC_BACMD
AccessionPrimary (citable) accession number: Q8GJ74
Secondary accession number(s): D5DDN1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families