ID ARGI_NEUCR Reviewed; 358 AA. AC P33280; Q7RV08; Q9URL4; V5ILL2; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 31-AUG-2004, sequence version 3. DT 02-SEP-2026, entry version 170. DE RecName: Full=Arginase; DE EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089}; GN Name=aga-1; Synonyms=aga, car1; ORFNames=NCU02333; OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / OS FGSC 987). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora. OX NCBI_TaxID=367110; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE INITIATION, AND SUBCELLULAR RP LOCATION. RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; RX PubMed=9792692; DOI=10.1074/jbc.273.45.29776; RA Marathe S.V., Yu Y.G., Turner G.E., Palmier C., Weiss R.L.; RT "Multiple forms of arginase are differentially expressed from a single RT locus in Neurospora crassa."; RL J. Biol. Chem. 273:29776-29785(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; RX PubMed=12712197; DOI=10.1038/nature01554; RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.; RT "The genome sequence of the filamentous fungus Neurospora crassa."; RL Nature 422:859-868(2003). RN [3] RP CHARACTERIZATION. RX PubMed=2953715; DOI=10.1016/s0021-9258(18)48206-3; RA Borkovich K.A., Weiss R.L.; RT "Purification and characterization of arginase from Neurospora crassa."; RL J. Biol. Chem. 262:7081-7086(1987). 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: Homohexamer. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9792692}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=41 kDa; CC IsoId=P33280-1; Sequence=Displayed; CC Name=36 kDa; CC IsoId=P33280-2; Sequence=VSP_018650; 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; L20687; AAC82503.1; -; Genomic_DNA. DR EMBL; L20687; AAC82504.1; -; Genomic_DNA. DR EMBL; CM002242; ESA41989.1; -; Genomic_DNA. DR PIR; T47228; T47228. DR PIR; T47229; T47229. DR RefSeq; XP_011395140.1; XM_011396838.1. [P33280-1] DR AlphaFoldDB; P33280; -. DR SMR; P33280; -. DR FunCoup; P33280; 1269. DR STRING; 367110.P33280; -. DR PaxDb; 367110-P33280; -. DR EnsemblFungi; ESA41989; ESA41989; NCU02333. DR GeneID; 3875906; -. DR KEGG; ncr:NCU02333; -. DR VEuPathDB; FungiDB:NCU02333; -. DR HOGENOM; CLU_039478_6_1_1; -. DR InParanoid; P33280; -. DR OMA; YKEFRYA; -. DR OrthoDB; 9992747at2759; -. DR SABIO-RK; P33280; -. DR UniPathway; UPA00158; UER00270. DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004053; F:arginase activity; ISS:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central. DR GO; GO:0090369; F:ornithine carbamoyltransferase inhibitor activity; IEA:EnsemblFungi. DR GO; GO:0008270; F:zinc ion binding; IEA:EnsemblFungi. DR GO; GO:0006525; P:arginine metabolic process; IEA:InterPro. DR GO; GO:0000050; P:urea cycle; IBA:GO_Central. DR CDD; cd09989; Arginase; 1. DR FunFam; 3.40.800.10:FF:000009; 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 1: Evidence at protein level; KW Alternative initiation; Arginine metabolism; Cytoplasm; Hydrolase; KW Manganese; Metal-binding; Reference proteome. FT CHAIN 1..358 FT /note="Arginase" FT /id="PRO_0000002087" FT BINDING 146 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 174 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 174 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 176 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 176 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 178 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 178 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 180 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 187 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 191 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 192 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 233 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 236 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 254 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 280 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 280 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 280 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 282 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 282 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742" FT BINDING 294 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 310 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 325 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 355 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 VAR_SEQ 1..33 FT /note="Missing (in isoform 36 kDa)" FT /evidence="ECO:0000305" FT /id="VSP_018650" FT CONFLICT 351..358 FT /note="CALGESLL -> SRSRRNVL (in Ref. 1; AAC82503/AAC82504)" FT /evidence="ECO:0000305" SQ SEQUENCE 358 AA; 38265 MW; 259CF279863D6977 CRC64; MSPSLVDNHA AAYIAAPSSA KAPMIQKPGN TFGMSSPIES KFLSQPRDLG IVAVGFSGGQ CKPGVDAAPS ALIESGLLTQ LREELGYRLH GDDEVHLYTD LVPKEDPPHR NMKNPRAVSN VTKRIAEQVH SHAKEGRLVL TLGGDHSIAI GTIAGSAKAI KERLGREIAV IWVDAHADIN TPETSGSGNI HGMPVSFLTG LASEDKEEFF GWLKPDHLLS VKKLVYIGLR DVDPGEKRIL RENGIKAFSM HDIDKHGIGR VMEMALGHIG NDTPIHLSFD VDALDPMWAP STGTPVRGGL TLREGDFICE CVHETGSLVA VDLVEVNPTL AAPNDVGAHE TVRAGCSLVR CALGESLL //