ID   C0ZIM2_BREBN            Unreviewed;       298 AA.
AC   C0ZIM2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Arginase {ECO:0000256|ARBA:ARBA00018123, ECO:0000256|RuleBase:RU361159};
DE            EC=3.5.3.1 {ECO:0000256|ARBA:ARBA00012168, ECO:0000256|RuleBase:RU361159};
GN   Name=rocF {ECO:0000313|EMBL:BAH41240.1};
GN   OrderedLocusNames=BBR47_02630 {ECO:0000313|EMBL:BAH41240.1};
OS   Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH41240.1, ECO:0000313|Proteomes:UP000001877};
RN   [1] {ECO:0000313|EMBL:BAH41240.1, ECO:0000313|Proteomes:UP000001877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47 / JCM 6285 / NBRC 100599
RC   {ECO:0000313|Proteomes:UP000001877};
RA   Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA   Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA   Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA   Udaka S., Tanikawa S., Fujita N.;
RT   "Brevibacillus brevis strain 47, complete genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000227,
CC         ECO:0000256|RuleBase:RU361159};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU361159};
CC       Note=Binds 2 manganese ions per subunit.
CC       {ECO:0000256|RuleBase:RU361159};
CC   -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-
CC       arginine: step 1/1. {ECO:0000256|ARBA:ARBA00005098}.
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP008955; BAH41240.1; -; Genomic_DNA.
DR   RefSeq; WP_012684013.1; NC_012491.1.
DR   AlphaFoldDB; C0ZIM2; -.
DR   STRING; 358681.BBR47_02630; -.
DR   GeneID; 61035856; -.
DR   KEGG; bbe:BBR47_02630; -.
DR   eggNOG; COG0010; Bacteria.
DR   HOGENOM; CLU_039478_6_2_9; -.
DR   UniPathway; UPA00158; UER00270.
DR   Proteomes; UP000001877; 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   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR014033; Arginase.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR   NCBIfam; TIGR01229; rocF_arginase; 1.
DR   PANTHER; PTHR43782; ARGINASE; 1.
DR   PANTHER; PTHR43782:SF3; ARGINASE; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; Arginase; 1.
DR   PRINTS; PR00116; ARGINASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR   PROSITE; PS01053; ARGINASE_1; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism {ECO:0000256|ARBA:ARBA00022503,
KW   ECO:0000256|RuleBase:RU361159};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW   Manganese {ECO:0000256|RuleBase:RU361159};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361159};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001877}.
SQ   SEQUENCE   298 AA;  32039 MW;  5EF8E8AD92B8ABE2 CRC64;
     MNKNMSIVGV PMDLGADRRG VDMGPSAIRY AGVVARLEKM GFNIEDRGDI FVTRPHHFTE
     TENHKYLDEV VEANEKLANV VSDIMTAGRF PLVLGGDHSI ALGTIAGVAK HVKNLGVIWF
     DAHGDLNTGA TSPSGNIHGM PLAASLGYGH ERLTNIGGYT PKVKAENVVI IGARDLDQGE
     RELIKRIGMK VFTMHEIDKL GMARVMDEAI AHVSKNTDGV HLSLDLDGLD PHDAPGVGTP
     VIGGISYREG HVSLEMLADA DILCSAEFVE VNPILDRENM TARVAVALMS SVFGDKLL
//