Q8GJ74 (ARSC_BACMD) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 55.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Protein ArsC | ||||
| Gene names |
| ||||
| Organism | Bacillus megaterium (strain DSM 319) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 592022 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 140 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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. |
| Sequence similarities | Belongs to the low molecular weight phosphotyrosine protein phosphatase superfamily. ArsC family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Arsenical resistance |
| Domain | Redox-active center |
| Molecular function | Hydrolase Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC response to arsenic-containing substanceInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | arsenate reductase (thioredoxin) activity Inferred from electronic annotation. Source: HAMAP protein tyrosine phosphatase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 140 | 140 | Protein ArsC HAMAP-Rule MF_01624 | PRO_0000162519 | |||||||
Sites | |||||||||||
| Active site | 10 | 1 | Nucleophile; for reductase activity and phosphatase activity By similarity | ||||||||
| Active site | 83 | 1 | Nucleophile; for reductase activity By similarity | ||||||||
| Active site | 90 | 1 | Nucleophile; for reductase activity By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 10 ↔ 83 | Redox-active; alternate By similarity | |||||||||
| Disulfide bond | 83 ↔ 90 | Redox-active; alternate By similarity | |||||||||
Sequences
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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. |
| RefSeq | YP_003596932.1. NC_014103.1. |
3D structure databases | |
| ProteinModelPortal | Q8GJ74. |
| SMR | Q8GJ74. Positions 1-140. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ADF38582; ADF38582; BMD_1727. |
| GeneID | 9117118. |
| KEGG | bmd:BMD_1727. |
| PATRIC | 37253484. VBIBacMeg104484_1668. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000273093. |
| KO | K03741. |
| ProtClustDB | CLSK2839638. |
Enzyme and pathway databases | |
| BioCyc | BMEG592022:GIVX-1727-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01624. Arsenate_reduct. |
| InterPro | IPR014064. Arsenate_reductase_ArsC. IPR023485. Ptyr_pPase_SF. IPR017867. Tyr_phospatase_low_mol_wt. [Graphical view] |
| PANTHER | PTHR11717. PTHR11717. 1 hit. |
| Pfam | PF01451. LMWPc. 1 hit. [Graphical view] |
| SMART | SM00226. LMWPc. 1 hit. [Graphical view] |
| SUPFAM | SSF52788. Tyr_Pase_low_mol_wt. 1 hit. |
| TIGRFAMs | TIGR02691. arsC_pI258_fam. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ARSC_BACMD | ||||||||
| Accession | Primary (citable) accession number: Q8GJ74 Secondary accession number(s): D5DDN1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
