ID   ARGI_STAAW              Reviewed;         302 AA.
AC   Q8NVE3;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Arginase;
DE            EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089};
GN   Name=arg; OrderedLocusNames=MW2091;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:46911; EC=3.5.3.1;
CC         Evidence={ECO:0000250|UniProtKB:P05089};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00742};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00742};
CC   -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-
CC       arginine: step 1/1. {ECO:0000250|UniProtKB:P05089}.
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00742}.
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DR   EMBL; BA000033; BAB95956.1; -; Genomic_DNA.
DR   RefSeq; WP_000167873.1; NC_003923.1.
DR   AlphaFoldDB; Q8NVE3; -.
DR   SMR; Q8NVE3; -.
DR   EnsemblBacteria; BAB95956; BAB95956; BAB95956.
DR   KEGG; sam:MW2091; -.
DR   HOGENOM; CLU_039478_6_2_9; -.
DR   OMA; IATCFGQ; -.
DR   UniPathway; UPA00158; UER00270.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0004053; F:arginase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd09989; Arginase; 1.
DR   InterPro; IPR014033; Arginase.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR   PANTHER; PTHR43782; PTHR43782; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; Arginase; 1.
DR   PRINTS; PR00116; ARGINASE.
DR   SUPFAM; SSF52768; SSF52768; 1.
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; Hydrolase; Manganese; Metal-binding.
FT   CHAIN           1..302
FT                   /note="Arginase"
FT                   /id="PRO_0000173724"
FT   BINDING         103
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         126
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         126
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         128..132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         128
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         130
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         139..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         229
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         229
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         231
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
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