ID ARGI_COCP7 Reviewed; 322 AA. AC P40906; C5P9L4; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 03-NOV-2009, sequence version 2. DT 02-SEP-2026, entry version 124. DE RecName: Full=Arginase; DE EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089}; GN Name=ARG; ORFNames=CPC735_005980; OS Coccidioides posadasii (strain C735) (Valley fever fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides. OX NCBI_TaxID=222929; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C735; RX PubMed=7867937; DOI=10.1016/0378-1119(94)00837-i; RA Pan S., Zhang M., Cole G.T.; RT "Isolation and characterization of the arginase-encoding gene (arg) from RT Coccidioides immitis."; RL Gene 154:115-118(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C735; RX PubMed=19717792; DOI=10.1101/gr.087551.108; RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T., RA Henn M.R., Birren B.W., Taylor J.W.; RT "Comparative genomic analyses of the human fungal pathogens Coccidioides RT and their relatives."; RL Genome Res. 19:1722-1731(2009). CC -!- FUNCTION: Catalyzes the hydrolysis of L-arginine into urea and L- CC ornithine. {ECO:0000250|UniProtKB:P39138}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-arginine + H2O = urea + L-ornithine; 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 -!- ACTIVITY REGULATION: Allosterically activated by L-arginine. CC {ECO:0000250|UniProtKB:P53608}. CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L- CC arginine: step 1/1. {ECO:0000250|UniProtKB:P05089}. CC -!- SUBUNIT: Homotrimer. {ECO:0000250}. 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; L36550; AAA65960.1; -; Genomic_DNA. DR EMBL; ACFW01000030; EER26426.1; -; Genomic_DNA. DR PIR; JC4033; JC4033. DR AlphaFoldDB; P40906; -. DR SMR; P40906; -. DR KEGG; cpw:9694054; -. DR VEuPathDB; FungiDB:CPC735_005980; -. DR HOGENOM; CLU_039478_6_1_1; -. DR OrthoDB; 9992747at2759; -. DR UniPathway; UPA00158; UER00270. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter. DR GO; GO:0004053; F:arginase activity; ISS:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IEA:TreeGrafter. DR GO; GO:0006525; P:arginine metabolic process; IEA:InterPro. DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway. DR CDD; cd09989; Arginase; 1. DR FunFam; 3.40.800.10:FF:000012; 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 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..322 FT /note="Arginase" FT /id="PRO_0000173707" FT BINDING 113 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 141 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 141 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 143 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="1" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 143 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 145 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="1" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 145 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 147 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="1" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 154 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="1" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 158 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="1" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 159 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="1" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 200 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="1" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 203 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="1" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 221 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="2" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 247 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="1" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 247 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 247 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 249 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="1" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 249 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 261 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="1" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 277 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="2" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 292 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="1" FT /ligand_note="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 315 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="2" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 319 FT /ligand="arginine" FT /ligand_id="ChEBI:CHEBI:32696" FT /ligand_label="2" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P53608" FT CONFLICT 153 FT /note="D -> V (in Ref. 1; AAA65960)" FT /evidence="ECO:0000305" SQ SEQUENCE 322 AA; 35142 MW; D382603CC361F19A CRC64; MTSPSTIKQK FIAKGHQLGV VAVGFSDGQP NQGVDPSGLI EAGLLDQLRD DLEYDIRHDG QVHTYAEFVP EHDPNHRGMK KPRTVSAATQ QLSRQVYEHA REGRLVLTLG GDHSIAIGTI SGTAKAIRER LGREMAVIWV DAHADINRPE DSDSGNIHGM PLAFLTGLAK DDNEDMFGWL QPDNLISPRK LVYIGLRDVD RAEKRLLREH GIKAFSMHDI DKYGIGRVVE MALAHIGQDT PIHLSFDVDA LDPQWAPSTG TPVRGGLTLR EGDFIAESIH ETGSLVAMDL VEVNPTLETL GASETIRAGC SLVRSALGDT LL //