Q65IV4 (ARSC_BACLD) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 56.
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 licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 279010 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 139 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 MF_01624 |
| Catalytic activity | Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. HAMAP MF_01624 Arsenate + thioredoxin = arsenite + thioredoxin disulfide + H2O. HAMAP MF_01624 |
| Subunit structure | Monomer By similarity. HAMAP MF_01624 |
| 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 | response to arsenic-containing substance Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | arsenate reductase (thioredoxin) activity Inferred from electronic annotation. Source: InterPro protein tyrosine phosphatase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 139 | 139 | Protein ArsC HAMAP MF_01624 | PRO_0000162518 | |||||||
Sites | |||||||||||
| Active site | 10 | 1 | Nucleophile; for reductase activity and phosphatase activity By similarity | ||||||||
| Active site | 82 | 1 | Nucleophile; for reductase activity By similarity | ||||||||
| Active site | 89 | 1 | Nucleophile; for reductase activity By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 10 ↔ 82 | Redox-active; alternate By similarity | |||||||||
| Disulfide bond | 82 ↔ 89 | Redox-active; alternate By similarity | |||||||||
Sequences
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References
| [1] | "The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580. |
| [2] | "Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. Berka R.M.Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017333 Genomic DNA. Translation: AAU41010.1. CP000002 Genomic DNA. Translation: AAU23647.1. |
| RefSeq | YP_079285.1. NC_006270.3. YP_091703.1. NC_006322.1. |
3D structure databases | |
| ProteinModelPortal | Q65IV4. |
| SMR | Q65IV4. Positions 1-139. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q65IV4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000056177; EBBACP00000054708; EBBACG00000056168. EBBACT00000061320; EBBACP00000059753; EBBACG00000061311. |
| GeneID | 3031404. 3099922. |
| GenomeReviews | Gene locus BLi02122 in contig AE017333_GR. Gene locus BL01871 in contig CP000002_GR. |
| KEGG | bld:BLi02122. bli:BL01871. |
| NMPDR | fig|279010.5.peg.2819. |
| PATRIC | 18949861. VBIBacLic203714_2134. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0394. |
| GeneTree | EBGT00070000032125. |
| HOGENOM | HBG730979. |
| OMA | EMRIVIT. |
| PhylomeDB | Q65IV4. |
| ProtClustDB | PRK13530. |
Enzyme and pathway databases | |
| BioCyc | BLIC279010-1:BLI02122-MONOMER. BLIC279010:BL01871-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01624. Arsenate_reduct. [Tree] |
| InterPro | IPR014064. Arsenate_reductase_ArsC. IPR023485. Ptyr_pPase_SF. IPR017867. Tyr_phospatase_low_mol_wt. [Graphical view] |
| KO | K03741. |
| PANTHER | PTHR11717. Low_mwt_PTPase. 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_BACLD | ||||||||
| Accession | Primary (citable) accession number: Q65IV4 Secondary accession number(s): Q62UB2 | ||||||||
| 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 |

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