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P60088 (ARGI_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Arginase

EC=3.5.3.1
Gene names
Name:arg
Ordered Locus Names:SA1968
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 processArginine metabolism
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionarginase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302Arginase
PRO_0000173721

Regions

Region128 – 1325Substrate binding By similarity
Region139 – 1413Substrate binding By similarity

Sites

Metal binding1031Manganese 1 By similarity
Metal binding1261Manganese 1 By similarity
Metal binding1261Manganese 2 By similarity
Metal binding1281Manganese 2 By similarity
Metal binding1301Manganese 1 By similarity
Metal binding2291Manganese 1 By similarity
Metal binding2291Manganese 2 By similarity
Metal binding2311Manganese 2 By similarity
Binding site1801Substrate By similarity
Binding site2741Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P60088 [UniParc].

Last modified November 28, 2003. Version 1.
Checksum: DD98335783BAC146

FASTA30233,265
        10         20         30         40         50         60 
MTKTKAIDII GAPSTFGQRK LGVDLGPTAI RYAGLISRLK QLDLDVYDKG DIKVPAVNIE 

        70         80         90        100        110        120 
KFHSEQKGLR NYDEIIDVNQ KLNKEVSASI ENNRFPLVLG GDHSIAVGSV SAISKHYNNL 

       130        140        150        160        170        180 
GVIWYDAHGD LNIPEESPSG NIHGMPLRIL TGEGPKELLE LNSNVIKPEN IVLIGMRDLD 

       190        200        210        220        230        240 
KGERQFIKDH NIKTFTMSDI DKLGIKEVIE NTIEYLKSRN VDGVHLSLDV DALDPLETPG 

       250        260        270        280        290        300 
TGTRVLGGLS YRESHFALEL LHQSHLISSM DLVEVNPLID SNNHTAEQAV SLVGTFFGET 


LL 

« Hide

References

« Hide 'large scale' references
[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: N315.
[2]"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth."
Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.
J. Microbiol. Methods 60:247-257(2005) [PubMed: 15590099] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
Strain: N315.
[3]"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
Submitted (OCT-2007) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: N315.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000018 Genomic DNA. Translation: BAB43257.1.
PIRH90011.
RefSeqNP_375278.1. NC_002745.2.

3D structure databases

ProteinModelPortalP60088.
SMRP60088. Positions 5-302.
ModBaseSearch...

Protein-protein interaction databases

STRINGP60088.

2D gel databases

SWISS-2DPAGEP60088.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000001264; EBSTAP00000001264; EBSTAG00000001264.
GeneID1124874.
GenomeReviewsGene locus SA1968 in contig BA000018_GR.
KEGGsau:SA1968.
PATRIC19576402. VBIStaAur116463_2128.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0010.
GeneTreeEBGT00050000025100.
HOGENOMHBG391953.
OMAADIPNDS.
ProtClustDBCLSK885803.

Enzyme and pathway databases

BioCycSAUR158879:SA1968-MONOMER.

Family and domain databases

InterProIPR014033. Arginase_subgr.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
Gene3DG3DSA:3.40.800.10. Ureohydrolase. 1 hit.
KOK01476.
PANTHERPTHR11358:SF2. Arginase_sub. 1 hit.
PTHR11358. Ureohydrolase. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFPIRSF036979. Arginase. 1 hit.
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01229. RocF_arginase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGI_STAAN
AccessionPrimary (citable) accession number: P60088
Secondary accession number(s): Q9R2U3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: November 28, 2003
Last modified: January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families