ID   ARGI_BREBE              Reviewed;         298 AA.
AC   Q7M0Z3;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Arginase;
DE            EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089};
GN   Name=rocF;
OS   Brevibacillus brevis (Bacillus brevis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1393;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-36.
RC   STRAIN=TT02-8;
RX   PubMed=9339546; DOI=10.1271/bbb.61.1459;
RA   Shimotohno K.W., Miwa I., Endo T.;
RT   "Molecular cloning and nucleotide sequence of the arginase gene of Bacillus
RT   brevis TT02-8 and its expression in Escherichia coli.";
RL   Biosci. Biotechnol. Biochem. 61:1459-1464(1997).
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   PIR; JC5866; JC5866.
DR   AlphaFoldDB; Q7M0Z3; -.
DR   SMR; Q7M0Z3; -.
DR   eggNOG; COG0010; Bacteria.
DR   SABIO-RK; Q7M0Z3; -.
DR   UniPathway; UPA00158; UER00270.
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   1: Evidence at protein level;
KW   Arginine metabolism; Direct protein sequencing; Hydrolase; Manganese;
KW   Metal-binding.
FT   CHAIN           1..298
FT                   /note="Arginase"
FT                   /id="PRO_0000173713"
FT   BINDING         98
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         121
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         121
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         123..127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         123
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         125
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         134..136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         225
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         225
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         227
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
SQ   SEQUENCE   298 AA;  31879 MW;  E7D2FB198B9DD5E0 CRC64;
     MNKNMSIVGV PMDLGADRRG VDMGPSAIRY AGVVARLEKM GFNIEDRGDI FVTLPHHFTE
     TENHKYLDEV VEANEKLANV VSDIMTAGRF PLVLGGDHSI ALGTIAGVAK HVKNLGVICL
     DAHGDLNTGA TSPSGNIHGM PLAASLGYGH ERLTNIGGYT PKVKAENVVI IGARDLDQGE
     RELIKRIGMK VFTMHEIDKL GMARVMDEAI AHVSKNTDGV HLSLDLDGLD PHDAPGVGTP
     VIGGISYREG HVSLEMLADA DILCSAEFVE VNPILDRENM TARVAVALMS SVFGDKLL