P60086 (ARGI_STAAC) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 60.
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: Arginase EC=3.5.3.1 | ||||||
| Gene names |
| ||||||
| Organism | Staphylococcus aureus (strain COL) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 93062 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 302 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | L-arginine + H2O = L-ornithine + urea. |
| Cofactor | Binds 2 manganese ions per subunit By similarity. |
| Pathway | Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. |
| Sequence similarities | Belongs to the arginase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Arginine metabolism |
| Ligand | Manganese Metal-binding |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | arginine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | arginase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 302 | 302 | Arginase | PRO_0000173719 | |||||
Regions | |||||||||
| Region | 128 – 132 | 5 | Substrate binding By similarity | ||||||
| Region | 139 – 141 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 103 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 126 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 126 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 128 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 130 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 229 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 229 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 231 | 1 | Manganese 2 By similarity | ||||||
| Binding site | 180 | 1 | Substrate By similarity | ||||||
| Binding site | 274 | 1 | Substrate By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Mrp -- a new auxiliary gene essential for optimal expression of methicillin resistance in Staphylococcus aureus." Wu S.-W., de Lencastre H. Microb. Drug Resist. 5:9-18(1999) [PubMed: 10332717] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain." Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. Fraser C.M.J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: COL. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Y09927 Genomic DNA. Translation: CAB55326.1. Y09594 Genomic DNA. Translation: CAA70781.1. CP000046 Genomic DNA. Translation: AAW38462.1. |
| RefSeq | YP_186967.1. NC_002951.2. |
3D structure databases | |
| ProteinModelPortal | P60086. |
| SMR | P60086. Positions 5-302. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P60086. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTAT00000009789; EBSTAP00000009524; EBSTAG00000009788. |
| GeneID | 3237431. |
| GenomeReviews | Gene locus SACOL2154 in contig CP000046_GR. |
| KEGG | sac:SACOL2154. |
| PATRIC | 19530573. VBIStaAur112458_2098. |
| TIGR | SACOL2154. |
Phylogenomic databases | |
| eggNOG | COG0010. |
| GeneTree | EBGT00050000025100. |
| HOGENOM | HBG391953. |
| OMA | ADIPNDS. |
| ProtClustDB | CLSK885803. |
Enzyme and pathway databases | |
| BioCyc | SAUR93062:SACOL2154-MONOMER. |
Family and domain databases | |
| InterPro | IPR014033. Arginase_subgr. IPR006035. Ureohydrolase. IPR023696. Ureohydrolase_domain. IPR020855. Ureohydrolase_Mn_BS. [Graphical view] |
| Gene3D | G3DSA:3.40.800.10. Ureohydrolase. 1 hit. |
| KO | K01476. |
| PANTHER | PTHR11358:SF2. Arginase_sub. 1 hit. PTHR11358. Ureohydrolase. 1 hit. |
| Pfam | PF00491. Arginase. 1 hit. [Graphical view] |
| PIRSF | PIRSF036979. Arginase. 1 hit. |
| PRINTS | PR00116. ARGINASE. |
| TIGRFAMs | TIGR01229. RocF_arginase. 1 hit. |
| PROSITE | PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ARGI_STAAC | ||||||||
| Accession | Primary (citable) accession number: P60086 Secondary accession number(s): Q9R2U3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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