ID ARGI_BRUAB Reviewed; 306 AA. AC P0A2Y1; Q579C0; Q59174; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 102. DE RecName: Full=Arginase; DE EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089}; GN Name=arcB; Synonyms=rocF; OrderedLocusNames=BruAb2_0333; OS Brucella abortus biovar 1 (strain 9-941). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=262698; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=19; RX PubMed=9375792; DOI=10.1016/s0167-4781(97)00125-5; RA Kim J., Mayfield J.E.; RT "Brucella abortus arginase and ornithine cyclodeaminase genes are similar RT to Ti plasmid arginase and ornithine cyclodeaminase."; RL Biochim. Biophys. Acta 1354:55-57(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9-941; RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005; RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.; RT "Completion of the genome sequence of Brucella abortus and comparison to RT the highly similar genomes of Brucella melitensis and Brucella suis."; RL J. Bacteriol. 187:2715-2726(2005). 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; Evidence={ECO:0000255|PROSITE- CC 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}. 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; U57319; AAC05588.1; -; Genomic_DNA. DR EMBL; AE017224; AAX75764.1; -; Genomic_DNA. DR RefSeq; WP_002965747.1; NC_006933.1. DR AlphaFoldDB; P0A2Y1; -. DR SMR; P0A2Y1; -. DR EnsemblBacteria; AAX75764; AAX75764; BruAb2_0333. DR GeneID; 45053898; -. DR KEGG; bmb:BruAb2_0333; -. DR HOGENOM; CLU_039478_6_2_5; -. DR UniPathway; UPA00158; UER00270. DR Proteomes; UP000000540; Chromosome II. 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; Hydrolase; Manganese; Metal-binding. FT CHAIN 1..306 FT /note="Arginase" FT /id="PRO_0000173716" FT BINDING 96 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 123 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" 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..129 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 125 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 127 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 136..138 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 178 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 226 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 226 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 228 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 240 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 271 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" SQ SEQUENCE 306 AA; 33182 MW; A953867BC04570B3 CRC64; MHCKILGLPV QEGTGRKGCN MGPDSYRAAG IADAIRELGH ECTDLGNLAP AAQRPLQHPN HAIKALPYAV AWIEAISEAA YRESAEGFPI FLGGDHLLAA GTVPGIARRA AEKGRKQFVL WLDAHTDFHT LETTTSGNLH GTPVAYYTGQ KGFEGYFPKL AAPIDPHNVC MLGIRSVDPA EREAVKKTEV IVYDMRLIDE HGVAALLRRF LERVKAEDGL LHVSLDVDFL DPSIAPAVGT TVPGGATFRE AHLIMEMLHD SGLVTSLDLV ELNPFLDERG RTAAVMVDLM ASLLGRSVMD RPTISY //