ID   ARGI_STAAS              Reviewed;         302 AA.
AC   Q6G7E9;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 35.
DE   RecName: Full=Arginase;
DE            EC=3.5.3.1;
GN   Name=arg; OrderedLocusNames=SAS2066;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- CATALYTIC ACTIVITY: L-arginine + H(2)O = L-ornithine + urea.
CC   -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
CC   -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea
CC       from L-arginine: step 1/1.
CC   -!- SIMILARITY: Belongs to the arginase family.
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DR   EMBL; BX571857; CAG43874.1; -; Genomic_DNA.
DR   RefSeq; YP_044175.1; -.
DR   GeneID; 2863909; -.
DR   GenomeReviews; BX571857_GR; SAS2066.
DR   KEGG; sas:SAS2066; -.
DR   HOGENOM; Q6G7E9; -.
DR   OMA; Q6G7E9; QIVKNPR.
DR   BioCyc; SAUR282459:SAS2066-MON; -.
DR   GO; GO:0004053; F:arginase activity; IEA:EC.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005924; Arginase.
DR   InterPro; IPR014033; Arginase_sub.
DR   InterPro; IPR006035; Ureohydrolase.
DR   Gene3D; G3DSA:3.40.800.10; Ureohydrolase; 1.
DR   PANTHER; PTHR11358:SF2; Arginase_sub; 1.
DR   PANTHER; PTHR11358; Ureohydrolase; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PRINTS; PR00116; ARGINASE.
DR   TIGRFAMs; TIGR01229; rocF_arginase; 1.
DR   PROSITE; PS01053; ARGINASE_1; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism; Complete proteome; Hydrolase; Manganese;
KW   Metal-binding.
FT   CHAIN         1    302       Arginase.
FT                                /FTId=PRO_0000173723.
FT   REGION      128    132       Substrate binding (By similarity).
FT   REGION      139    141       Substrate binding (By similarity).
FT   METAL       103    103       Manganese 1 (By similarity).
FT   METAL       126    126       Manganese 1 (By similarity).
FT   METAL       126    126       Manganese 2 (By similarity).
FT   METAL       128    128       Manganese 2 (By similarity).
FT   METAL       130    130       Manganese 1 (By similarity).
FT   METAL       229    229       Manganese 1 (By similarity).
FT   METAL       229    229       Manganese 2 (By similarity).
FT   METAL       231    231       Manganese 2 (By similarity).
FT   BINDING     180    180       Substrate (By similarity).
FT   BINDING     274    274       Substrate (By similarity).
SQ   SEQUENCE   302 AA;  33293 MW;  1D983B4783BAC772 CRC64;
     MTKTKAIDII GAPSTFGQRK LGVDLGPTAI RYAGLISRLK QLDLDVYDKG DIKVPVVNIE
     KFHSEQKGLR NYDEIIDVNQ KLNKEVSASI ENNRFPLVLG GDHSIAVGSV SAISKHYNNL
     GVIWYDAHGD LNIPEESPSG NIHGMPLRIL TGEGPKELLE LNSNVIKPEN IVLIGMRDLD
     KGERQFIKDH NIKTFTMSDI DKLGIKEVIE NTIEYLKSRN VDGVHLSLDV DALDPLETPG
     TGTRVLGGLS YRESHFALEL LHQSHLISSM DLVEVNPLID SNNHTAEQAV SLVGTFFGET
     LL
//