P63622 (ARSC_NEIMB) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 49.
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: Putative arsenate reductase EC=1.20.4.1 | ||||
| Gene names |
| ||||
| Organism | Neisseria meningitidis serogroup B | ||||
| Taxonomic identifier | 491 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria |
Protein attributes
| Sequence length | 117 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Reduction of arsenate [As(V)] to arsenite [As(III)] Potential. |
| Catalytic activity | Arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H2O. |
| Sequence similarities | Belongs to the ArsC family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Arsenical resistance |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | response to arsenic-containing substance Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | arsenate reductase (glutaredoxin) activity Inferred 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 – 117 | 117 | Putative arsenate reductase | PRO_0000162542 | |||
Sequences
References
| [1] | "Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. Venter J.C.Science 287:1809-1815(2000) [PubMed: 10710307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58 / Serogroup B. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE002098 Genomic DNA. Translation: AAF40484.1. |
| PIR | C81247. |
| RefSeq | NP_273071.1. NC_003112.2. |
3D structure databases | |
| ProteinModelPortal | P63622. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBNEIT00000009106; EBNEIP00000008726; EBNEIG00000009106. |
| GeneID | 902107. |
| GenomeReviews | Gene locus NMB0005 in contig AE002098_GR. |
| KEGG | nme:NMB0005. |
| PATRIC | 20354937. VBINeiMen85645_0005. |
| TIGR | NMB0005. |
Phylogenomic databases | |
| GeneTree | EBGT00050000021443. |
| HOGENOM | HBG734370. |
| OMA | APTIVRY. |
| ProtClustDB | CLSK877347. |
Enzyme and pathway databases | |
| BioCyc | NMEN122586:NMB_0005-MONOMER. |
Family and domain databases | |
| InterPro | IPR006659. Arsenate_reductase. IPR006660. Arsenate_reductase-like. IPR012336. Thioredoxin-like_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| KO | K00537. |
| Pfam | PF03960. ArsC. 1 hit. [Graphical view] |
| SUPFAM | SSF52833. Thiordxn-like_fd. 1 hit. |
| TIGRFAMs | TIGR00014. ArsC. 1 hit. |
| PROSITE | PS51353. ARSC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ARSC_NEIMB | ||||||||
| Accession | Primary (citable) accession number: P63622 Secondary accession number(s): Q9JQU0 | ||||||||
| 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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