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Q81NJ6 (ARSC_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. 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:BA_3196, GBAA_3196, BAS2971
OrganismBacillus anthracis [Reference proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length134 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 134134Protein ArsC HAMAP-Rule MF_01624
PRO_0000162511

Sites

Active site111Nucleophile; 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 bond11 ↔ 83Redox-active; alternate By similarity
Disulfide bond83 ↔ 90Redox-active; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81NJ6 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 73B208FC18C4683E

FASTA13415,066
        10         20         30         40         50         60 
MENKKTIYFL CTGNSCRSQM AEAWGKQYLG DKWNVYSAGI EAHGVNPNAI KAMNEVNIDI 

        70         80         90        100        110        120 
TNQTSDIIDA NILNRADLVV TLCSHADAVC PSTPPHVNRV HWGFDDPAGK EWPEFQRVRD 

       130 
EIGERIKRFS ETGE 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."
Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.
J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP26992.1.
AE017334 Genomic DNA. Translation: AAT32312.1.
AE017225 Genomic DNA. Translation: AAT55279.1.
RefSeqNP_845506.1. NC_003997.3.
YP_019837.1. NC_007530.2.
YP_029228.1. NC_005945.1.

3D structure databases

ProteinModelPortalQ81NJ6.
SMRQ81NJ6. Positions 1-134.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ81NJ6. 3 interactions.
STRING198094.BA_3196.

Protocols and materials databases

DNASU1086394.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP26992; AAP26992; BA_3196.
AAT32312; AAT32312; GBAA_3196.
AAT55279; AAT55279; BAS2971.
GeneID1086394.
2817664.
2850718.
KEGGban:BA_3196.
bar:GBAA_3196.
bat:BAS2971.

Phylogenomic databases

eggNOGCOG0394.
HOGENOMHOG000273093.
KOK03741.
OMAGHANETC.
OrthoDBEOG6JDWJC.
ProtClustDBPRK13530.

Enzyme and pathway databases

BioCycANTHRA:ARSC-MONOMER.
BANT260799:GJAJ-3033-MONOMER.
BANT261594:GJ7F-3137-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_BACAN
AccessionPrimary (citable) accession number: Q81NJ6
Secondary accession number(s): Q6HWR0, Q6KQV2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 80 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