ARGI_NEUCR
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 03-AUG-2022, entry version 155.
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 -!- 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 -!- 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}.
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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 STRING; 5141.EFNCRP00000003109; -.
DR EnsemblFungi; ESA41989; ESA41989; NCU02333. [P33280-1]
DR GeneID; 3875906; -.
DR KEGG; ncr:NCU02333; -.
DR VEuPathDB; FungiDB:NCU02333; -.
DR HOGENOM; CLU_039478_6_1_1; -.
DR InParanoid; P33280; -.
DR OMA; IATCFGQ; -.
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; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IBA:GO_Central.
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 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 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..180
FT /ligand="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="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 187..189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 233
FT /ligand="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="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 325
FT /ligand="substrate"
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
